Information on EC 1.3.5.1 - succinate dehydrogenase (quinone)

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.3.5.1
-
RECOMMENDED NAME
GeneOntology No.
succinate dehydrogenase (quinone)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
succinate + a quinone = fumarate + a quinol
show the reaction diagram
-
-
-
-
succinate + a quinone = fumarate + a quinol
show the reaction diagram
can also function as a fumarate reductase
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
aerobic respiration (alternative oxidase pathway)
-
aerobic respiration (cytochrome c)
-
aerobic respiration (cytochrome c) (yeast)
-
anaerobic energy metabolism (invertebrates, mitochondrial)
-
Biosynthesis of secondary metabolites
-
Butanoate metabolism
-
Citrate cycle (TCA cycle)
-
Metabolic pathways
-
methylaspartate cycle
-
Microbial metabolism in diverse environments
-
Oxidative phosphorylation
-
succinate to cytochrome bd oxidase electron transfer
-
succinate to cytochrome bo oxidase electron transfer
-
superpathway of glyoxylate cycle and fatty acid degradation
-
TCA cycle I (prokaryotic)
-
TCA cycle II (plants and fungi)
-
TCA cycle IV (2-oxoglutarate decarboxylase)
-
TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
-
TCA cycle VII (acetate-producers)
-
TCA cycle VIII (metazoan)
-
SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase
A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria and archaea. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
complex II
-
-
-
-
complex II
-
-
complex II
-
-
complex II
-
-
complex II
-
-
complex II
-
-
complex II
-
-
complex II of the respiratory chain
-, P21912, Q99643
-
complex II succinate:ubiquinone oxidoreductase
-
-
DCPIP oxidoreductase
-
-
dehydrogenase, succinate
-
-
-
-
dehydrogenase/complex II
-, P21912, Q99643
-
Fcc3
-
-
-
-
FL cyt
-
-
-
-
Flavocytochrome c3
-
-
-
-
fumarate reductase
-
-
-
-
fumarate reductase
-
-
fumarate reductase
Shewanella frigidimarina NCIMB400
-
-
-
fumarate reductase
-
-
fumarate reductase complex
-
-
-
-
fumaric hydrogenase
-
-
-
-
Ifc3
-
-
-
-
Iron(III)-induced flavocytochrome C3
-
-
-
-
menaquinol:fumarate oxidoreductase
-
-
-
-
menaquinol:fumarate oxidoreductase
-
-
methylmenaquinol:fumarate reductase
-
-
mitochondrial complex II
-
-
mitochondrial complex II
-
-
mitochondrial complex II
-
-
mitochondrial succinate dehydrogenase
-
-
quinol-fumarate reductase
-
-
quinol:fumarate reductase
-
-
SDH
P21912, Q99643
-
SDH
Q920L2
-
SDH
Rattus norvegicus Wistar
-
-
-
SDH
Xanthomonas oryzae pv. oryzae ZJ173
Q6DLZ2, Q6DLZ3
-
-
SDH2-1
Q8LBZ7
-
SDH2-2
Q8LB02
-
sdhABE
-
operon encoding for non-classical succinate quinone reductase
SDHB
-
iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase
SDHB
C4T9C3
sdhB gene encodes an iron-sulfur subunit of succinate dehydrogenase
SDHB
-
iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase
sdhCAB
-
operon encoding succinate dehydrogenase
SdhCDAB
-
-
SdhD
-
succinate dehydrogenase subunit that also coordinate the low spin hexa-coordinated heme b
SDISP
Schistosoma japonicum Chinese
-
-
-
SQR
-
ambiguous
SQR
Bacillus subtilis 3G18
-
-
-
SQR
P0AC41
-
SQR
-
non-classical succinate quinone reductase
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
P0AC41
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase
P77943 and P77944 and P77945 and P77946
ambiguous
succinate dehydrogenase
P77943 and P77944 and P77945 and P77946
ambiguous
-
succinate dehydrogenase (caldariellaquinone)
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
-
succinate dehydrogenase (caldariellaquinone)
Sulfolobus tokodaii 7
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
-
-
succinate dehydrogenase B
-
-
succinate dehydrogenase complex
-
-
-
-
succinate dehydrogenase flavoprotein subunit Sdh1p
-
-
succinate dehydrogenase iron-sulfur protein
-
-
succinate dehydrogenase iron-sulfur protein
Schistosoma japonicum Chinese
-
-
-
succinate dehydrogenase subunit B
-
-
succinate oxidoreductase
-
-
-
-
succinate-2,6-dichlorophenolindophenol oxidoreductase
-
-
succinate-coenzyme Q reductase
-
-
-
-
succinate-quinone oxidoreductase
-
-
succinate-quinone oxidoreductase
-
-
succinate-quinone oxidoreductase
-
-
succinate-quinone oxidoreductase
-
-
succinate-quinone reductase
-
-
succinate-ubiquinone oxidoreductase
-
-
succinate-ubiquinone oxidoreductase
-
cf. EC 1.3.5.4, menaquinol-fumarate oxidoreductase, structurally and functionally related membrane-bound enzyme complexes
succinate:caldariellaquinone oxidoreductase
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
-
succinate:caldariellaquinone oxidoreductase
Sulfolobus tokodaii 7
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
-
-
succinate:menaquinone oxidoreductase
-
-
succinate:quinone oxidoreductase
O73937 and O73937 and O73939 and O73940
-
succinate:quinone oxidoreductase
-
-
succinate:quinone oxidoreductase
-
ambiguous
succinate:quinone oxidoreductase
Bacillus subtilis 3G18
-
-
-
succinate:quinone oxidoreductase
-
ambiguous
succinate:quinone oxidoreductase
-
-
succinate:quinone oxidoreductase
Sulfolobus sp. 7
-
-
-
succinate:quinone reductase
-
-
succinate:quinone reductase
-
-
succinate:quinone reductase
-
-
-
succinate:quinone reductase
-
-
succinate:quinone reductases
-
-
succinate:ubiquinone oxidoreductase
-
-
succinate:ubiquinone oxidoreductase
-
-
succinate:ubiquinone reductase
-
-
succinic acid dehydrogenase
-
-
-
-
succinic dehydrogenase
-
-
-
-
succinodehydrogenase
-
-
-
-
succinyl dehydrogenase
-
-
-
-
mitochondrial succinate:ubiquinone oxidoreductase
-
-
additional information
-
SDH belongs to the highly conserved complex II family of enzymes that reduce ubiquinone
additional information
-
cf. EC 1.3.5.1; cf. EC 1.3.99.1
additional information
-
cf.EC 1.3.99.1
additional information
-
cf. EC 1.3.5.1
additional information
-
cf. EC 1.3.5.1; cf. EC 1.3.99.1
CAS REGISTRY NUMBER
COMMENTARY
9002-02-2
-
9028-11-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
O73937: FAD-containing subunit SdhA, O73937: iron-sulfur subunit SdhB, O73939: subunit SdhC, O73940: subunit SdhD
O73937 and O73937 and O73939 and O73940
SwissProt
Manually annotated by BRENDA team
strains MRK,Webster, NY8, USG3 and Bridgeport grown in HL-60 cells, genes sdhA, sdhB, sdhC and sdhD
-
-
Manually annotated by BRENDA team
genes sdh1-2 and sdh2-3
-
-
Manually annotated by BRENDA team
; fumarate reductase; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
fumarate reductase; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
strain 3G18, that harbors the entire sdh operon on a low copy number plasmid
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
Bacillus subtilis 3G18
strain 3G18, that harbors the entire sdh operon on a low copy number plasmid
-
-
Manually annotated by BRENDA team
; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
fumarate reductase
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
encoded by the sdhCDAB gene clusters
-
-
Manually annotated by BRENDA team
fumarate reductase
-
-
Manually annotated by BRENDA team
fumarate reductase, recombinant strain, containing amplified activity
-
-
Manually annotated by BRENDA team
fumarate reductase; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
strains HB101 and FRD117
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
facultative anaerobic bacterium
-
-
-
Manually annotated by BRENDA team
soybean, succinate dehydrogenase
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
; genes SDHC, SDHD, and SDHB
-
-
Manually annotated by BRENDA team
gene SDHB; subunit B encoding gene SDHB
UniProt
Manually annotated by BRENDA team
gene SDHC; subunit C encoding gene SDHC
UniProt
Manually annotated by BRENDA team
genes SDHB and SDHD
-
-
Manually annotated by BRENDA team
genes SDHD and SDHB
-
-
Manually annotated by BRENDA team
patients with pheochromocytomas or paragangliomas
-
-
Manually annotated by BRENDA team
subunit encoding genes SDHA, and SDHD
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
sweet potato, succinate dehydrogenase
-
-
Manually annotated by BRENDA team
; lysodeikticus, succinate dehydrogenase
-
-
Manually annotated by BRENDA team
lysodeikticus, succinate dehydrogenase
-
-
Manually annotated by BRENDA team
lysodeikticus, succinate dehydrogenase; Micrococcus luteus
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
GenBank, Accession No. U31902
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
fumarate reductase
-
-
Manually annotated by BRENDA team
cultured BRL cells
-
-
Manually annotated by BRENDA team
flavoprotein subunit of thr succinate dehydrogenase; gene sdhA
UniProt
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Sprague Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
male
-
-
Manually annotated by BRENDA team
; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
Rhodospirillum sp.
fumarate reductase
-
-
Manually annotated by BRENDA team
genes SDHA, SDHB, SDHC, and SDHD encding the four subunits of the enzyme
-
-
Manually annotated by BRENDA team
succinate dehydrogenase
-
-
Manually annotated by BRENDA team
wild-type strain YPH499
-
-
Manually annotated by BRENDA team
Chinese strain
-
-
Manually annotated by BRENDA team
Schistosoma japonicum Chinese
Chinese strain
-
-
Manually annotated by BRENDA team
Shewanella frigidimarina NCIMB400
NCIMB400
-
-
Manually annotated by BRENDA team
Shewanella putrefaciens MR-1
MR-1
-
-
Manually annotated by BRENDA team
Staphylococcus aureus in biofilms, genes sdhCAB
-
-
Manually annotated by BRENDA team
Staphylococcus aureus HG001
Staphylococcus aureus in biofilms, genes sdhCAB
-
-
Manually annotated by BRENDA team
Staphylococcus aureus SA113
Staphylococcus aureus in biofilms, genes sdhCAB
-
-
Manually annotated by BRENDA team
infective larvae
-
-
Manually annotated by BRENDA team
P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, 77946: subunit sdhD
P77943 and P77944 and P77945 and P77946
UniProt
Manually annotated by BRENDA team
P77943: subunit sdhA (flavoprotein subunit), P77944: subunit sdhB, P77945: subunit sdhC, 77946: subunit sdhD
P77943 and P77944 and P77945 and P77946
UniProt
Manually annotated by BRENDA team
Q97W79: subunit sdhA, Q97W78: subunit sdhB, Q97W77: subunit sdhE (formerly SdhC), Q97W76: subunit sdhD
Q97W79 and Q97W78 and Q97W77 and Q97W76
UniProt
Manually annotated by BRENDA team
Q97W79: subunit sdhA, Q97W78: subunit sdhB, Q97W77: subunit sdhE (formerly SdhC), Q97W76: subunit sdhD
Q97W79 and Q97W78 and Q97W77 and Q97W76
UniProt
Manually annotated by BRENDA team
Sulfolobus sp. 7
-
-
-
Manually annotated by BRENDA team
F9VN10: subunit sdhA, Q9C4L8: subunit sdhB, F9VN12: subunit sdhC, F9VN13: subunit sdhD
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
UniProt
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
F9VN10: subunit sdhA, Q9C4L8: subunit sdhB, F9VN12: subunit sdhC, F9VN13: subunit sdhD
F9VN10 and Q9C4L8 and F9VN12 and F9VN13
UniProt
Manually annotated by BRENDA team
cultured PK-15
-
-
Manually annotated by BRENDA team
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase
-
-
Manually annotated by BRENDA team
mung bean, succinate dehydrogenase
-
-
Manually annotated by BRENDA team
formerly Vibrio succinogenes, fumarate reductase
-
-
Manually annotated by BRENDA team
formerly Vibrio succinogenes, fumarate reductase; succinate dehydrogenase
-
-
Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae ZJ173
subunit SdhA
UniProt
Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae ZJ173
subunit SdhB
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme as respiratory complex II belongs to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases and quinol:fumarate reductases
malfunction
-
the presentation of three synchronous extra-adrenal abdominal paragangliomas in an adolescent boy who carries a germline mutation in the SDHB gene are reported. Loss of heterozygosity of this allele is demonstrated by direct sequencing of DNA from two of his tumors, confirming loss of tumor suppressor function in the pathogenesis of these paragangliomas
malfunction
-
the frequency of polymorphisms of SDHs, hypoxia-inducible factor type 1 and angiotensin converting enzyme genes is compared between 40 subjects with intolerance to high altitude and a low hypoxic ventilatory response at exercise and 41 subjects without intolerance to high altitude and a high hypoxic ventilatory. No significant association between low or high hypoxic ventilatory response and the allele frequencies for nine single nucleotide polymorphisms in the SDHD and SDHB genes, the ACE insertion/deletion polymorphism and four single nucleotide polymorphisms in the hypoxia-inducible factor type 1 a gene is found. No clear association is found between gene variants involved in oxygen sensing and chemoresponsiveness, although some mutations in the SDHB and SDHD genes deserve further investigations in a larger population
malfunction
-
the succinate:ubiquinone oxidoreductase activity of the mitochondrial respiratory complex II is specifically impaired by reactive oxygen species without affecting the second enzymatic activity of this complex as a succinate dehydrogenase. The different pro-apoptotic agents responsible for complex II inhibition lead to mitochondrial matrix acidification. Complex II contributes to apoptosis induction only when the SQR activity is inhibited while the SDH activity is still fully functioning,creating an uncoupling phenomenon at the complex II level. The association of an active SDH activity with an inhibited SQR function is not possible, rendering complex II incapable of apoptosis induction and promoting tumourigenesis
physiological function
-
the enzyme is involved in electron transfer via the respiratory chain
physiological function
-
the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain
physiological function
-
the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional
physiological function
-
using the submitochondrial particles from the adult worms and L3 larvae of the parasitic nematode Ascaris suum, it is shown that reactive oxygen species are produced from the flavin adenine dinucleotide-binding site as well as the quinone binding site in the mitochondrial complex II
physiological function
-
using pharmacological and siRNA methodologies it is shown that increased methylation of histone H3 is a general consequence of SDH loss-of-function in cultured mammalian cells and can be reversed by overexpression of the JMJD3 histone demethylase. ChIP analysis reveals that the core promoter of IGFBP7, which encodes a secreted protein upregulated after loss of SDHB, shows decreased occupancy by H3K27me3 (histone 3 methylated on residue K27) in the absence of SDH
physiological function
-
the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview
physiological function
-
succinate:ubiquinone oxidoreductase is part of the mitochondrial respiratory complex II
physiological function
-
succinate:quinone reductase serves as the respiratory complex II
physiological function
-
the enzyme is involved in electron transfer via the respiratory chain
-
metabolism
-
enzymatic activity, quinone content and complex II subunit composition in mitochondria of lung stage L3 (LL3) Ascaris suum larvae is examined. Lung stage L3 Ascaris suum larvae mitochondria show higher quinolfumarate reductase activity than mitochondria of Ascaris suum at other stages. Ubiquinone content in lung stage L3 larvae mitochondria is more abundant than rhodoquinone. It is shown that lung stage L3 larvae mitochondria contain larval flavoprotein subunit (Fp) and adult flavoprotein subunit at a ratio of 1:0.56, and that most lung stage L3 larvae cytochrome b containing subunits CybS are of the adult form. This clearly indicates that the rearrangement of complex II begins with a change in the isoform of the anchor CybS subunit, followed by a similar change in the Fp subunit
additional information
-
the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
fumarate + 2,3-dimethyl-1,4-naphthoquinol
succinate + 2,3-dimethyl-1,4-naphthoquinone
show the reaction diagram
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
?
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
-
-
-
?
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
-
-
-
r
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
-
-
-
-
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
donor: anthrahydroquinonesulfonate
-
-
r
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
donor: benzyl viologen
-
-
?
fumarate + electron donor
succinate + oxidized donor
show the reaction diagram
-
main reaction for fumarate reductase, reverse reaction only 1% of fumarate reduction
-
-
?
fumarate + menaquinol
succinate + menaquinone
show the reaction diagram
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
fumarate + quinol
succinate + ubiquinone
show the reaction diagram
-
-
-
r
fumarate + quinol
succinate + ubiquinone
show the reaction diagram
-
-
-
r
fumarate + reduced acceptor
succinate + acceptor
show the reaction diagram
-
FrdCAB functions in vivo as both the fumarate reductase and the succinate dehydrogenase, with an apparent energetic cost when catalyzing succinate oxidation
-
-
r
fumarate + reduced benzyl viologen
succinate + benzyl viologen
show the reaction diagram
-
-
-
-
r
fumarate + reduced benzyl viologen
succinate + benzyl viologen
show the reaction diagram
-
-
-
-
?
fumarate + reduced benzyl viologen
succinate + benzyl viologen
show the reaction diagram
-
-
-
-
?
fumarate + reduced decylubiquinone
succinate + decylubiquinone
show the reaction diagram
-
-
-
-
r
fumarate + reduced phenazine methosulfate
succinate + phenazine methosulfate
show the reaction diagram
-
enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
-
-
r
succinate + 1,4-naphthoquinone
fumarate + 1,4-naphthoquinol
show the reaction diagram
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + 1-methoxy-5-methylphenazinium methyl sulfate
fumarate + ?
show the reaction diagram
-
-
-
-
?
succinate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol
show the reaction diagram
-
the redox potential of the 2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinone/2,3-dimethoxy-5-ethyl-6-methyl-1,4-benzoquinol couple is 90 mV higher than that of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple
-
-
?
succinate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-1,4-benzohydroquinone
show the reaction diagram
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-(3,7-dimethyl-2,6-octadienyl)-1,4-benzoquinol
show the reaction diagram
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
show the reaction diagram
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
show the reaction diagram
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
show the reaction diagram
-
-
-
-
r
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
show the reaction diagram
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
show the reaction diagram
-
-
-
-
-
succinate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol
show the reaction diagram
-
-
-
-
?
succinate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
fumarate + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol
show the reaction diagram
-
-
-
-
r
succinate + 2,3-dimethyl-1,4-naphthoquinone
fumarate + 2,3-dimethyl-1,4-naphthoquinol
show the reaction diagram
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
r
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
succinate + 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Bacillus subtilis 3G18
-
-
-
-
?
succinate + 2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
?
show the reaction diagram
-
i.e. MTT, in presence of phenazine methosulfate, i.e. PMS
-
-
?
succinate + 2-ethyl-3-methyl-1,4-naphthoquinone
fumarate + 2-ethyl-3-methyl-1,4-naphthoquinol
show the reaction diagram
-
the redox potential of the 2-ethyl-3-methyl-1,4-naphthoquinone/2-ethyl-3-methyl-1,4-naphthoquinol couple is identical to that of the 2,3-dimethyl-1,4-naphthoquinone/2,3-dimethyl-1,4-naphthoquinol couple
-
-
?
succinate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone
fumarate + 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol
show the reaction diagram
-
the succinate dehydrogenase C subunit is responsible for ubiquinone binding
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
Q8LB02, Q8LBZ7
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
Sdh produces only superoxide and no H2O2 upon flavin autoxidation, even at high concentrations of succinate
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + benzyl viologen
fumarate + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-, O73937 and O73937 and O73939 and O73940
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
caldariellaquinone, the physiologically acting electron mediator in Sulfolobus membranes is slowly reduced as compared to water-soluble dyes
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-, caldariellaquinone, the physiologically acting electron mediator in Sulfolobus membranes is slowly reduced as compared to water-soluble dyes
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
Sulfolobus sp. 7
-
-
-
-
?
succinate + decylubiquinone
fumarate + ?
show the reaction diagram
-
-
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
show the reaction diagram
-
-
-
-
?
succinate + decylubiquinone
fumarate + decylubiquinol
show the reaction diagram
-
decylubiquinone-mediated reduction of dichlorophenol indophenol
-
-
?
succinate + decylubiquinone
fumarate + reduced decylubiquinone
show the reaction diagram
-
-
-
-
r
succinate + duroquinone
fumarate + duroquinol
show the reaction diagram
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: methylene blue (oxidized)
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
main reaction for succinate dehydrogenase, acceptor: phenazine methosulfate (oxidized)
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: phenazine methosulfate and 2,6-dichloroindophenol
-
-
-
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: phenazine methosulfate and 2,6-dichloroindophenol
-
-
-
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
succinate can be replaced by L-chlorosuccinate, L-methylsuccinate, monofluorosuccinate, 2,2-difluorosuccinate, L-, or D-malate
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: dichloroindophenol
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: ferricyanide
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
acceptor: ferricyanide
-
-
r
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
comparison of assay methods
-
-
-
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
active in aerobic respiration, repressed during anaerobic respiration
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
Shewanella putrefaciens MR-1
-
-
-
-
r
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Q6DLZ2, Q6DLZ3
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Xanthomonas oryzae pv. oryzae ZJ173
Q6DLZ2, Q6DLZ3
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Staphylococcus aureus HG001
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Staphylococcus aureus SA113
-
-
-
-
?
succinate + ferricyanide
fumarate + ferrocyanide
show the reaction diagram
-
the assay is based on the reduction of ferricyanide to ferrocyanide by SDH activity and on the coupled capture of ferrocyanide by copper. The granular reaction product (copperferrocyanide) is highly electron opaque and is confined exclusively to the mitochondrial membranes.The use of a chelating agent in the incubating medium prevents the diffusion of the dark spots and guarantees their precise localization at the site of SDH activity
-
-
?
succinate + ferrocyanide
fumarate + ferricyanide
show the reaction diagram
-
-
-
-
?
succinate + menadione
fumarate + menadiol
show the reaction diagram
-
with 2,6-dichlorophenolindophenol
-
-
?
succinate + menaquinone
fumarate + menaquinol
show the reaction diagram
-
-
-
-
?
succinate + nitro blue tetrazolium
fumarate + formazan
show the reaction diagram
-
yellow dye
blue dye
-
?
succinate + oxidised 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
-
succinic acid is incubated with mitochondria and its oxidation by SDH is measured by the reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 1,4-dichloroindophenol
fumarate + reduced 1,4-dichloroindophenol
show the reaction diagram
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
succinate-dependent, phenazine methosulfate-mediated malonate-sensitive reduction of 2,6-dichlorophenol indophenol
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Sulfolobus sp. 7
-
-
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
show the reaction diagram
-
in presence of phenazine methosulfate
-
-
?
succinate + oxidized 2,6-dichlorophenolindophenol
fumarate + reduced 2,6-dichloroindophenol
show the reaction diagram
-
in the presence of the artificial electron acceptor phenazine methosulfate and the ubiquinone analogue UQ1
-
-
?
succinate + oxidized benzyl viologen
fumarate + reduced benzyl viologen
show the reaction diagram
-
-
-
-
r
succinate + oxidized donor
?
show the reaction diagram
-
endogenous SDH activity results in blue diphormazan deposits from the nitroblue tetrazolium reduction through succinate oxidation
-
-
?
succinate + oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
fumarate + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
-
-
-
-
?
succinate + oxidized phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
?
succinate + phenazine ethosulfate
fumarate + reduced phenazine ethosulfate
show the reaction diagram
-
-
-
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
-
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
-
reaction catalyzed by preparations of complex II
-
?
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
-
enzyme catalyzes fumarate reduction as well as succinate oxidation with commensurate activities
-
-
r
succinate + phenazine methosulfate
fumarate + reduced phenazine methosulfate
show the reaction diagram
-
with 2,6-dichlorophenolindophenol, best substrate
-
-
?
succinate + phenazine methosulfate
fumarate + ?
show the reaction diagram
-
phenazine methosulfate as direct electron acceptor and 2,6-dichlorophenolindophenol as final acceptor
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
-
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
P0AC41
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
P21912, Q99643
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
the succinate dehydrogenase activity of mitochondria in adults and larvae are comparable
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
determination of quinol:fumarate reductase activity using 2,3-dimethyl-1,4-naphthoquinol
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
slow inactivation of the the enzyme in the substrate assay mixture containing different concentrations of substrates, succinate and 2,6-dichloroindophenol, the inactivation rate decreases with increasing concentration of succinate, the inactivation is 2,6-dichloroindophenol concentration independent
-
-
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
succinate dehydrogenase restores full activity to electron transport particles or complex II preparations whose succinate dehydrogenases have been selectively destroyed at pH 9.3
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
electron acceptor: menaquinone
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
complex II of the mitochondrial oxidative phosphorylating system
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol, role of Tyr-89 in the protonation of ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
a key membrane complex in the tricarboxylic acid cycle that catalyzes the oxidation of succinate to fumarate in the mitochondrial matrix as succinate dehydrogenase
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
complex II is the only membrane bound enzyme of the Krebs cycle, and it feeds electrons into the electron transport chain from the oxidation of succinate
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
SDH is a key enzyme that catalyses the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Functioning as mitochondrial complex II in the electron transport chain, it transfers electrons extracted from succinate to ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
SDH is an essential component of the electron transport chain and of the tricarboxylic acid cycle in the mitochondrial membrane
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
the enzyme is part of the tricarboxylic acid cycle, it is also a tumor suppressor. Succinate stabilizes and activates hypoxia-inducible factor HIFalpha and reversibly and competitively inhibits HIF-prolyl hydroxylase leading to induction of hypoxia in SDH-deficient cells, 2-oxoglutarate overcomes succinate-mediated inhibition of PHD in vitro, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
electrons are transferred from succinate to ubiquinone through the buried prosthetic groups FAD, [2Fe-2S] cluster, [4Fe-4S] cluster [3Fe-4S] cluster and heme, which form an integral part of the complex
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
electrons move from the FAD prosthetic group in SDH on to the two matrix subunits via a series of [Fe-S] redox clusters and possibly also via a heme group to end up at the terminal acceptor ubiquinone residing within the membrane subunits CybL and CybS
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
the enzyme does not generate a proton motive force during catalysis and are electroneutral, thus, the quinone reduction reaction must consume cytoplasmic protons which are released stoichiometrically during succinate oxidation. Residues SdhBG227, SdhCD95, and SdhCE101 are located at or near the entrance of a water channel that functions as a proton wire connecting the cytoplasm to the quinone binding site in vivo, while an alternative proton pathway exists in vitro only, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
Bacillus subtilis 3G18
-
-
-
-
?
succinate + ubiquinone-1
fumarate + ubiquinol-1
show the reaction diagram
Sulfolobus sp., Sulfolobus sp. 7
-
-
-
-
?
succinate + ubiquinone-1
fumarate + ubiquinol
show the reaction diagram
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
succinate + ubiquinone-2
fumarate + ubiquinol
show the reaction diagram
-
succinate:quinone reductase activity is determined as quinone-mediated succinate:2,4-dichlorophenolindophenol (DCIP) reductase
-
-
r
succinate + ubiquinone-8
fumarate + ubiquinol-8
show the reaction diagram
-
-
-
-
r
succinate + WST-1
fumarate + reduced WST-1
show the reaction diagram
-
-
-
-
?
ubiquinone-1 + L-malate
?
show the reaction diagram
-
-
-
-
?
ubiquinone-1 + L-malate
?
show the reaction diagram
-
-
-
-
-
ubiquinone-1 + succinate
ubiquinol + fumarate
show the reaction diagram
-
-
-
-
?
ubiquinone-1 + succinate
ubiquinol-1 + fumarate
show the reaction diagram
-
-
-
-
?
fumarate + reduced plumbagin
succinate + oxidized plumbagin
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
the complex can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone but acts with other electron acceptors
-
-
-
additional information
?
-
-
fumarate reductase activity of larval complex II is less than 3% of that of adult enzyme, complex II of adult nematode functions in the reverse direction as a fumarate reductase rather than as a succinate dehydrogenase
-
-
-
additional information
?
-
-
reduction of coenzyme Q and analogues, coenzyme Q2 is the most efficient electron acceptor, coenzyme Q10 in substrate quantities when supplemented with Triton X-100 and a lipid extract is about 75% as efficient as coenzyme Q2
-
-
-
additional information
?
-
-
L- or D-malate oxidation
-
-
-
additional information
?
-
-
catalytic mechanism
-
-
-
additional information
?
-
-
classification of fumarate reductases and succinate dehydrogenases based on voltammetric studies
-
-
-
additional information
?
-
-
pathway of electron transfer in complex II
-
-
-
additional information
?
-
-
study of potential dependecy and pH dependency of reaction, tunnel-diopde effect
-
-
-
additional information
?
-
-
dichlorophenolindophenol only acceptor when used together with phenazine methosulfate, no reaction with ubiquinones, see EC 1.3.5.1 for SDH- and FRD-complex
-
-
-
additional information
?
-
-
model of fumarate reductase electron-transport chain
-
-
-
additional information
?
-
-
the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
-
-
-
additional information
?
-
-
membrane-bound enzyme of the citric acid cycle and the respiratory chain
-
-
-
additional information
?
-
-
complex II of adult organism muscle exhibits high fumarate reductase activity and plays a key role in anaerobic electron-transport during adaptation to their microaerobic habitat, in contrast larval complex II shows a much lower fumarate reductase activity than the adult enzyme and functions as succinate dehydrogenase in aerobic respiration
-
-
-
additional information
?
-
-
complex II from mitochondria of the adult parasitic nematode exhibits a high fumarate reductase activity and plays a key role in the anaerobic electron transport observed in these organelles
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate
-
-
-
additional information
?
-
-
approximately 10% to 15% of paragangliomas are caused by mutations in the succinate dehydrogenase genes SDHB, SDHC, or SDHD
-
-
-
additional information
?
-
-
enzyme subunit mutations are involved in the Carney-Stratakis syndrome and in development of gastrointestinal stromal tumors, overview
-
-
-
additional information
?
-
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
-
additional information
?
-
-
germline mutations in the SDHB, SDHC or SDHD genes cause hereditary paraganglioma tumors which show constitutive activation of homeostatic mechanisms induced by oxygen deprivation/hypoxia, overview
-
-
-
additional information
?
-
-
germline mutations of the gene SDHB encoding succinate dehydrogenase subunit B predispose to malignant paraganglioma. Despite an autosomal dominant pattern of inheritance, penetrance of the disease is incomplete and age dependent, overview
-
-
-
additional information
?
-
-
germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
-
-
-
additional information
?
-
-
high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
-
-
-
additional information
?
-
-
inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: implications for the pathogenesis and treatment of mitochondrial encephalomyopathies, overview
-
-
-
additional information
?
-
-
mitochondrial dysfunction by complex II inhibition delays overall cell cycle progression via reactive oxygen species production, overview, complex II defects are involved in ageing and cancers such as hereditary paraganglioma and familial pheochromocytoma, overview
-
-
-
additional information
?
-
-
mutations of the enzyme can cause hereditary paraganglioma and/or pheochromocytoma, overview
-
-
-
additional information
?
-
-
subunit mutations are involved in development of malignant paragangliomas
-
-
-
additional information
?
-
-
succinate dehydrogenase enzyme subunit B gene mutations cause metastatic pheochromocytoma and paraganglioma, distribution of metastases in different tissues in correlation to the enzyme expression, sites of bone involvement, overview
-
-
-
additional information
?
-
-
succinate dehydrogenase flavoprotein subunit Sdh1p is bound by the mitochondrial FAD transporter, Flx1p, a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae, FLX1p controls SDH activity by regulating the amount of flavinylated Sdh1p, overview
-
-
-
additional information
?
-
-
the Cowden or Cowden-like syndromes are caused by PTEN mutations of the SDH-D gene, encoding the subunit D, the syndromes are associated with breast, thyroid and endometrial neoplasias, overview
-
-
-
additional information
?
-
-
the nuclear genes SDHD and SDHB encode two mitochondrial enzyme complex II subunits and are associated with the development of familial pheochromocytomas and paraganglioma, i.e. the hereditary pheochromocytoma/paraganglioma syndrome, HPPS, and the following metastasis, overview
-
-
-
additional information
?
-
-
vitamin E analogues bind to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
-
-
-
additional information
?
-
-
electronic communication between purified SQR and a surface modified gold capillary electrode, redox titrations, overview
-
-
-
additional information
?
-
-
enzyme assay using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide method
-
-
-
additional information
?
-
Q920L2
the flavoprotein of succinate dehydrogenase is an in vitro substrate of and phosphorylated at Tyr535 and Tyr596 by the Fgr tyrosine kinase, overview
-
-
-
additional information
?
-
Q09545
for enzymatic activity the succinate-dependent, phenazine methosulfate-mediated reduction of dichlorophenol indophenol of crude mitochondrial fractions prepared from the wild type and the P211 mutants is measured
-
-
-
additional information
?
-
-
fumarate reduction activity is measured by monitoring photometrically the oxidation of dithionite-reduced benzylviologen by fumarate, succinate oxidation activity is determined using either methylene blue, dichlorophenolindophenol, ferricenium hexafluorophosphate, dimethylnaphthoquinone or as electron acceptor. Strikingly, no succinate oxidation activity is be detected, independent of the electron acceptor
-
-
-
additional information
?
-
-
efficiency with different quinones, in decreasing order: phenazine methosulfate, decylubiquinone, duroquinone, menadione, 2,3-dimethyl-1,4-naphthoquinone
-
-
-
additional information
?
-
-
enzyme also accetps phenazine methosulfate, reaction of EC 1.3.5.4
-
-
-
additional information
?
-
-
enzyme operates with both natural quinones, ubiquinone and menaquinone, at a single quinone binding site. Residue Lys228 in subunit FrdB provides a strong hydrogen bond to menaquinone and is essential for reactions with both quinone types. There is similar hydrogen bonding of the C1 carbonyl of both MQ and UQ, whereas there is different hydrogen bonding for their C4 carbonyls
-
-
-
additional information
?
-
-
evidence for proton potential dependent catalysis of succinate oxidation by quinone as well as for proton potential generation upon catalysis of fumarate reduction by quinol
-
-
-
additional information
?
-
-
no activity with 1,4-benzoquinone
-
-
-
additional information
?
-
Bacillus subtilis 3G18
-
electronic communication between purified SQR and a surface modified gold capillary electrode, redox titrations, overview
-
-
-
additional information
?
-
Schistosoma japonicum Chinese
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
fumarate + menaquinol
succinate + menaquinone
show the reaction diagram
-
fumarate reductase acts as part of an anaerobic respiratory chain
-
-
r
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
-
-
-
-
?
succinate + acceptor
fumarate + reduced acceptor
show the reaction diagram
Q8LB02, Q8LBZ7
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-, O73937 and O73937 and O73939 and O73940
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
r
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
-
-
-
-
?
succinate + caldariellaquinone
fumarate + caldariellaquinol
show the reaction diagram
Sulfolobus sp. 7
-
-
-
-
?
succinate + electron acceptor
fumarate + reduced acceptor
show the reaction diagram
-
active in aerobic respiration, repressed during anaerobic respiration
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Q6DLZ2, Q6DLZ3
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Xanthomonas oryzae pv. oryzae ZJ173
Q6DLZ2, Q6DLZ3
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Staphylococcus aureus HG001
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
Staphylococcus aureus SA113
-
-
-
-
?
succinate + menaquinone
fumarate + menaquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
P0AC41
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
P21912, Q99643
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
r
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
complex II of the mitochondrial oxidative phosphorylating system
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
a key membrane complex in the tricarboxylic acid cycle that catalyzes the oxidation of succinate to fumarate in the mitochondrial matrix as succinate dehydrogenase
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
complex II is the only membrane bound enzyme of the Krebs cycle, and it feeds electrons into the electron transport chain from the oxidation of succinate
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
SDH is a key enzyme that catalyses the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Functioning as mitochondrial complex II in the electron transport chain, it transfers electrons extracted from succinate to ubiquinone
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
SDH is an essential component of the electron transport chain and of the tricarboxylic acid cycle in the mitochondrial membrane
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
the enzyme is part of the tricarboxylic acid cycle, it is also a tumor suppressor. Succinate stabilizes and activates hypoxia-inducible factor HIFalpha and reversibly and competitively inhibits HIF-prolyl hydroxylase leading to induction of hypoxia in SDH-deficient cells, 2-oxoglutarate overcomes succinate-mediated inhibition of PHD in vitro, overview
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
Bacillus subtilis 3G18
-
-
-
-
?
fumarate + reduced acceptor
succinate + acceptor
show the reaction diagram
-
FrdCAB functions in vivo as both the fumarate reductase and the succinate dehydrogenase, with an apparent energetic cost when catalyzing succinate oxidation
-
-
r
additional information
?
-
-
the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain
-
-
-
additional information
?
-
-
membrane-bound enzyme of the citric acid cycle and the respiratory chain
-
-
-
additional information
?
-
-
complex II of adult organism muscle exhibits high fumarate reductase activity and plays a key role in anaerobic electron-transport during adaptation to their microaerobic habitat, in contrast larval complex II shows a much lower fumarate reductase activity than the adult enzyme and functions as succinate dehydrogenase in aerobic respiration
-
-
-
additional information
?
-
-
complex II from mitochondria of the adult parasitic nematode exhibits a high fumarate reductase activity and plays a key role in the anaerobic electron transport observed in these organelles
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
-
-
-
additional information
?
-
-
succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate
-
-
-
additional information
?
-
-
approximately 10% to 15% of paragangliomas are caused by mutations in the succinate dehydrogenase genes SDHB, SDHC, or SDHD
-
-
-
additional information
?
-
-
enzyme subunit mutations are involved in the Carney-Stratakis syndrome and in development of gastrointestinal stromal tumors, overview
-
-
-
additional information
?
-
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
-
additional information
?
-
-
germline mutations in the SDHB, SDHC or SDHD genes cause hereditary paraganglioma tumors which show constitutive activation of homeostatic mechanisms induced by oxygen deprivation/hypoxia, overview
-
-
-
additional information
?
-
-
germline mutations of the gene SDHB encoding succinate dehydrogenase subunit B predispose to malignant paraganglioma. Despite an autosomal dominant pattern of inheritance, penetrance of the disease is incomplete and age dependent, overview
-
-
-
additional information
?
-
-
germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
-
-
-
additional information
?
-
-
high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
-
-
-
additional information
?
-
-
inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: implications for the pathogenesis and treatment of mitochondrial encephalomyopathies, overview
-
-
-
additional information
?
-
-
mitochondrial dysfunction by complex II inhibition delays overall cell cycle progression via reactive oxygen species production, overview, complex II defects are involved in ageing and cancers such as hereditary paraganglioma and familial pheochromocytoma, overview
-
-
-
additional information
?
-
-
mutations of the enzyme can cause hereditary paraganglioma and/or pheochromocytoma, overview
-
-
-
additional information
?
-
-
subunit mutations are involved in development of malignant paragangliomas
-
-
-
additional information
?
-
-
succinate dehydrogenase enzyme subunit B gene mutations cause metastatic pheochromocytoma and paraganglioma, distribution of metastases in different tissues in correlation to the enzyme expression, sites of bone involvement, overview
-
-
-
additional information
?
-
-
succinate dehydrogenase flavoprotein subunit Sdh1p is bound by the mitochondrial FAD transporter, Flx1p, a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae, FLX1p controls SDH activity by regulating the amount of flavinylated Sdh1p, overview
-
-
-
additional information
?
-
-
the Cowden or Cowden-like syndromes are caused by PTEN mutations of the SDH-D gene, encoding the subunit D, the syndromes are associated with breast, thyroid and endometrial neoplasias, overview
-
-
-
additional information
?
-
-
the nuclear genes SDHD and SDHB encode two mitochondrial enzyme complex II subunits and are associated with the development of familial pheochromocytomas and paraganglioma, i.e. the hereditary pheochromocytoma/paraganglioma syndrome, HPPS, and the following metastasis, overview
-
-
-
additional information
?
-
-
vitamin E analogues bind to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
-
-
-
additional information
?
-
Schistosoma japonicum Chinese
-
female BALB/c mice vaccinated with recombinant Schistiosoma japonicum succinate dehydrogenase iron-sulfur protein all revealed high levels of specific antibody and significant reduction in worm burden, liver eggs per gram, fecal eggs per gram and intrauterine eggs, compared to non-vaccinated mice, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-methoxy-5-methylphenazinium methyl sulfate
-
-
-
2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone
-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
-
2,6-dichlorophenolindophenol
-
in presence of phenazine methosulfate
ATP
-
activation
benzyl viologen
-
-
cytochrome b
-
cytochrome b-558, 3.6 nmol per mg of protein, functions as electron carrier between NADH dehydrogenase and succinate dehydrogenase in the Ascaris NADH-fumarate reductase system
-
cytochrome b
-
cytochrome b-558, composed of two hydrophobic polypeptides with molecular masses of 17.2 and 12.5 kDa, which correspond to the two small subunits of complex II
-
cytochrome b
-
4.5-5 nmol cytochrome b per mg protein; cytochrome b-557.5
-
cytochrome b
-
cytochrome b-558, is the smallest protein of the complex with MW: 19000, it is a transmembrane protein and anchors succinate dehydrogenase to the cytoplasmic side of the membrane
-
cytochrome b
-
1 mol per mol of succinate dehydrogenase
-
cytochrome b
-
-
-
cytochrome b
-
-
-
cytochrome b
-
the isolated two-subunit membrane anchoring protein contains 35 nmol cytochrome b-556 per mg protein
-
cytochrome b
-
-
-
cytochrome b
-
-
-
cytochrome b
-
succinate dehydrogenase contains one heme b
-
cytochrome b
-
-
-
cytochrome b-560
-
-
-
cytochrome b-560
-
-
-
cytochrome b558
-
SdhC
-
FAD
-
covalently bound to flavoprotein subunit
FAD
-
; covalently bound to flavoprotein subunit
FAD
facultative anaerobic bacterium, Mammalia
-
-
FAD
-
covalently bound to flavoprotein subunit
FAD
-
1 mol of covalently bound flavin per 100,000 g of protein; covalently bound to flavoprotein subunit
FAD
-
covalently bound to flavoprotein subunit
FAD
-
role in succinate oxidation
FAD
-
1 mol flavin per mol succinate dehydrogenase
FAD
-
covalently bound to flavoprotein subunit
FAD
-
covalently linked to protein histidyl residue
FAD
-
covalently bound to FRDA subunit
FAD
-
covalently linked to larger subunit
FAD
-
amino acid sequence around FAD-binding site
FAD
-
localized in Sdh1, i.e. the flavoprotein subunit
FAD
-
flavoprotein subunit SdhA
FAD
-
in Sdh1 subunit
FAD
-
covalent FAD modification of flavoprotein subunit 1 from complex II
FAD
-
ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
FAD
-
flavoprotein, 41 pmol FAD per mg of protein in wild-type strain YPH499, possesses a flavoprotein subunit Sdh1p as part of the catalytic dimer of the tetrameric enzyme
FAD
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
FAD
-
FAD is non-covalently attached to SdhA. The reason for the lack of succinate oxidation activity might be explained by the absence of a covalently bound FAD which seems to be a prerequisite for succinate oxidation activity
FAD
-
covalently attached to the enzyme to enable succinate oxidation
FAD
-
stoichiometric ratio between covalently bound FAD and the iron-sulfur cluster is 1:1. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD
FAD
-
bound in the succinate dehydrogenase flavoprotein, SdhA, subunit
FAD
-
the enzyme complex contains one molecule of covalently bound FAD
FAD
-
SdhA is the FAD-containing subunit
Fe-S center
-
the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center
flavin
-
the enzyme complex contains non-extractable flavin. The purified complex contains 4.6 nmol/mg acid non-extractable flavin
flavin
-
quantitative determination of content in wild-type and mutant enzymes
flavin
Q920L2
flavoprotein of succinate dehydrogenase
flavin
-
covalently-bound flavin cofactor
flavin adenine dinucleotide
-
-
flavin adenine dinucleotide
-
-
fumarate
-
activation
heme
-
single heme localized between Sdh3 and Sdh4 subunits
heme
-
enzyme contains two heme molecules. Presence of protoheme IX, absence of the other heme types. The ratio of protoheme IX to the SQR protomer is 1.5, there are two protoheme IX-binding sites in SQR
heme
-
direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
heme
-
a single heme b moiety is incorporated into the membrane anchor and only the QP-site is functional
heme
-
in a di-heme membrane anchor protein harboring two putative quinone binding sites
heme
-
the residues required for heme-binding are harbored by SdhC
heme
-
proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV
heme
-
enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes. Protoheme IX is present in about 2:1 stoichiometry to covalently bound FAD
heme
-
the enzyme contains two heme b cofactors, a di-heme
heme b
-
heme bP und heme bD
heme b
-
the enzyme contains one hydrophobic subunit (C) with two haem b groups
heme b
-
the quinone binding site of succinate dehydrogenase is required for electron transfer to the heme b
heme b556
-
ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
-
heme b562
-
the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
IDP
-
activation
iron-sulfur centre
-
direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
iron-sulfur centre
-
ubiquinone reduction by an electron transfer relay comprising a flavin adenine dinucleotide cofactor, three iron-sulfur clusters, and possibly a heme b556. At the heart of the electron transport chain is a [4Fe-4S] cluster with a low midpoint potential that acts as an energy barrier against electron transfer
iron-sulfur centre
-
enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes. The purified mQFR complex has two iron-sulfur centers of the ferredoxin type that are paramagnetic in the reduced state, 2Fe-2S and 4Fe-4S, and one iron-sulfur center of the high potential type that is paramagnetic in the oxidized state, 3Fe-4S. Centers 2Fe-2S and 4Fe-4S exhibit a large difference in their redox midpoint potential, center 2Fe-2S is reducible with succinate, whereas the latter one can only be reduced by very low potential reductant such as dithionite
iron-sulfur centre
-
enzyme contains the canonical iron-sulfur centers S1, S2, and S3, as well as two B-type hemes. The S3 center has a high reduction potential of +130 mV and is present in two different conformations, one of which presents an EPR signal with g values at 2.035, 2.009, and 2.001. The apparent midpoint reduction potentials of the hemes, +75 and -65 mV at pH 7.5, are higher than those reported for other enzymes. The heme with the lower potential, heme bL, presents a considerable dependence of the reduction potential with pH, i.e. a redox-Bohr effect, having a pKox of 6.5 and a pKred of 8.7. This behavior is consistent with the proposal that in these enzymes menaquinone reduction occurs close to heme bL, near to the periplasmic side of the membrane, and involving dissipation of the proton transmembrane gradient
phenazine methosulfate
-
-
phenazine methosulfate
-
-
Plumbagin
-
a quinone analogue
quinone
-
with a periplasmically oriented quinone binding site of the enzyme
ubiquinone
-
-
ubiquinone
-
two putative binding sites in the di-heme membrane anchoring protein
ubiquinone
-
-
ubiquinone
-
the residues required for quinone-binding are harbored by SdhD
iron-sulfur centre
-
SdhB
additional information
-
the enzyme contains acid-labile sulfides
-
additional information
-
-
-
additional information
-
preparations of complex II contain 0.2 mg lipid per mg protein and 7-8 mol of acid-labile sulfide per 100,000 g of protein
-
additional information
-
the enzyme contains iron-sulfur centers; the iron-sulfur clusters are located in one or both of the hydrophilic subunits, centre 2 in fumarate reductase is a 4Fe-4S cluster
-
additional information
-
measurement of the redox potentials of the sulfur-centers; the enzyme contains iron-sulfur centers
-
additional information
-
measurement of the redox potentials of the sulfur-centers; the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains 18-20% lipid by weight protein
-
additional information
-
the enzyme contains acid-labile sulfides
-
additional information
-
analysis of the functional role of the trinuclear cluster S3 in the enzyme by introducing a fourth cysteine residue into the putative ligation motif to that cluster; the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers; the fumarate reductase of the parasitic adult and the succinate dehydrogenase of free-living larvae share a common iron-sulfur subunit, at least the flavoprotein subunit and the small subunit of cytochrome b of the larval complex II differ from those of adult
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
the enzyme contains iron-sulfur centers
-
additional information
-
two hydrophobic subunits (C and D) which bind either one haem b group
-
additional information
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3Fe-4S center
C4T9C3, -
sdhB gene encodes an ironsulfur subunit of succinate dehydrogenase
3Fe-4S center
-
the iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
4Fe-4S cluster
Q97W79 and Q97W78 and Q97W77 and Q97W76
the CCG-domain-containing subunit SdhE (formerly SdhC) contains a [4Fe4S] cluster in reduced (2+) and oxidized (3+) states. The reduced form of the [4Fe4S]2+ cluster is diamagnetic. The individual iron sites of the reduced cluster are noticeably heterogeneous and show partial valence localization, which is particularly strong for one unique ferrous site
Anions
-
required for activity
Br-
-
activation
ClO4-
-
activation
Fe
-
7-8 g-atoms of nonheme iron per 100000 g of protein
Fe
-
3Fe-4S, bound to Ip subunit; 4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits; non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
-
8 mol nonheme iron per mol of succinate dehydrogenase
Fe
-
3Fe-4S, bound to Ip subunit; non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
-
4Fe-4S, bound to Fp subunit or bridging between Ip and Fp subunits; non-heme iron, types of Fe-S clusters: 2Fe-2S, bound to Ip: iron-sulfur protein subunit, smaller subunit
Fe
-
Fe-S center. Direct role of the heme of succinate-ubiquinone oxidoreductase in transfer of electrons from the iron-sulfur cluster to the quinone
Fe-S cluster
-
two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol
Fe-S cluster
-
at least three distinct types of FeS cluster, at center S-1 a [2Fe-2S]2+,1+ cluster, at center S-2 a [4Fe-4S]2+,1+ cluster, and at center S-3 a [3Fe4S]1+,0 cluster
Fe-S-clusters
facultative anaerobic bacterium
-
-
Fe-S-clusters
-
3Fe-4S centre, bound to Ip subunit; 4Fe-4S centre, bound to Fp (Fp: flavoprotein subunit, larger) subunit or bridging between Ip and Fp subunits; types: 2Fe-2S-centre, bound to Ip (Ip: iron-sulfur protein subunit, smaller) subunit
Fe-S-clusters
-
types: 2Fe-2S-centre, bound to Ip (Ip: iron-sulfur protein subunit, smaller) subunit
Fe-S-clusters
-
electron magnetic resonance study of Fe-S-clusters
Fe-S-clusters
-
-
Fe-S-clusters
-
3Fe-4S centre, bound to Ip subunit
Fe-S-clusters
-
-
Fe-S-clusters
-
magnetic circular dichroism study of Fe-S-clusters S1-S3; types: 2Fe-2S-centre, bound to Ip (Ip: iron-sulfur protein subunit, smaller) subunit
Fe-S-clusters
-
-
Fe-S-clusters
-
-
Fe-S-clusters
-
electron magnetic resonance study of Fe-S-clusters
Fe-S-clusters
-
contains two 2Fe-2S-centers and one 4Fe-4S-center per mol of histidyl flavin
Fe2+
-
heme cofactor and [3Fe-4S] cluster, midpoint potentials of wild-type and mutant enzymes, overview
Fe2+
-
non-heme iron in the iron-sulfur protein in subunit Sdh2p as part of the catalytic dimer of the tetrameric enzyme, and heme iron in a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
Fe2+
-
in the heme cofactor
Fe2+
-
in the iron-sulfur protein SdhB and the cytochrome b558, SdhC
Fe2+
-
the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center, heme b
Fe2+
-
existence of [2Fe-2S], [4Fe-4S] and [3Fe-4S] iron-sulfur clusters within the purified protein, electron paramagnetic resonance spectroscopy, influence of the substrate on the signal corresponding to the [2Fe-2S] cluster, overview
Fe2+
-
the enzyme contains a [3Fe-4S] center
fumarate
-
activation
I-
-
activation
Iron
-
Sdh2 subunit contains [2Fe-2S], 4[Fe-4S] and [3Fe-4S] clusters
Iron
-
SdhB subunit contains [2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters
Iron
-
[2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters in SdhB subunit
Iron
-
contains [2Fe-2S], [4Fe-4S] and [3Fe-4S] clusters
Iron
-
[2Fe-2S], [3Fe-4S] and [4Fe-4S] clusters in Sdh2 subunit
Iron
-
the enzyme complex contains 102.4 nmol/mg iron
Iron
-
iron-sulfur subunit with 3 distinct [4Fe-4S], [3Fe-3S], and [2Fe-2S] clusters, i.e., organized in 2 domains, all participate in electron transfer, overview
Iron
-
enzyme contains about 11 iron atoms per complex, which is expected if the enzyme contains one [2Fe-2S] cluster, one [3Fe-4S] cluster, one [4Fe-4S] cluster and two type b hemes
Iron
-
the enzyme complex contains 10 Fe atoms. It contains the canonical centres S1 ([2Fe-2S]+2/+1) and S2 ([4Fe-4S]+2/+1) but lacks centre S3 ([3Fe-4S]+1/0). The iron-sulfur subunit contains an extra cysteine that may allow the binding of a new centre, most probably a tetranuclear one
Iron
-
SdhB is the iron-sulfur subunit
iron-sulfur centre
F9VN10 and Q9C4L8 and F9VN12 and F9VN13, -
K-edge X-ray absorption spectroscopy is used to monitor the structural changes of their Fe sites in the irreversible [2Fe-2S] cluster degradation process. Regardless of the differences in the cluster-ligating cysteine motifs and the XAS-detectable [2Fe-2S]2+ cluster environments, a complete reductive breakdown of the [2Fe-2S] clusters results in the appearance of a new Fourier transform peak at about 3.3 A with a concomitant loss of the Fe-Fe interaction at ca. 2.7 A for both proteins. The results suggest that a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de novo biosynthesis and/or regulation of iron-binding enzymes in the cellular system
malonate
-
activation
NO3-
-
activation
phosphate
-
activation
SO42-
-
activation
succinate
-
activation
[2Fe-2S]-center
F9VN10 and Q9C4L8 and F9VN12 and F9VN13, -
the [2Fe-2S] cluster in SdhB-N and center C in SdhC are two succinate reducible high-potential centers detected in the archaeal succinate:caldariellaquinone oxidoreductase complex that differ in their arrangements of the cluster-binding cysteine motifs and the local cluster surroundings. a biological [2Fe-2S] cluster breakdown under reducing conditions generally releases Fe2+ from the polypeptide chain into the aqueous solution, and the Fe2+ might then be recruited as a secondary ferrous iron source for de noVo biosynthesis and/or regulation of iron-binding enzymes in the cellular system
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
-
-
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
-
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
-
-
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
potent inhibitor of fumarate reductase, not inhibitory for succinate dehydrogenase
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
potent inhibitor that affects both reduction and oxidation of quinone, the inhibitor binds close to heme bD
2-alkyl-4,6-dinitrophenol-17
-
-
2-alkyl-4,6-dinitrophenol-20
-
-
2-alkyl-4,6-dinitrophenols
-
derivatives of 2-alkyl-4,6-dinitrophenols, competitive inhibitors of both succinate dehydrogenase and fumarate reductase
2-alkyl-4,6-dinitrophenols
-
complete inhibition of the wild-type enzyme and of the mutants H106Y and H113Q
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
-
-
2-heptyl-4-hydroxyquinoline N-oxide
-
more than 0.1 mM, 50% inhibition
2-mercaptoethanol
-
-
2-n-heptyl-4 hydroxyquinoline N-oxide
-
a specific inhibitor, i.e. HQNO, which binds to quinone binding site Qd in SQR
2-n-heptyl-4-hydroxyquinoline
-
inhibition of succinate dehydrogenase activity using 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone or 2,6-dichlorophenolindophenol as electron acceptor
2-n-heptyl-4-hydroxyquinoline N-oxide
-
inhibitory to the succinate dehydrogenase activity assay using 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone and 2,6-dichloroindophenol as the electron acceptor, not inhibitory to the succinate dehydrogenase activity assay using phenazine methosulfate and 2,6-dichloroindophenol
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
-
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
-
2-n-heptyl-4-hydroxyquinolino-N-oxide
-
-
2-sec-butyl-4,6-dinitrophenol
-
non-competitive inhibition
2-thenoyltrifluoracetone
-
EC50 fumarate reductase 0.026 mM, EC50 succinate dehydrogenase 0.028 mM
2-Thenoyltrifluoroacetone
-
97% inhibition at 0.1 mM
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
15% inhibition of succinate dehydrogenase activity of larval and adult complex II at 0.1 mM
2-Thenoyltrifluoroacetone
-
50% inhibition at 3 mM
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
inhibits both wild-type and carboxin-resistant enzymes, competitive inhibition with respect to quinone
2-Thenoyltrifluoroacetone
-
slows down the inactivation of the enzyme in the substrate assay mixture
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
-
2-Thenoyltrifluoroacetone
-
-
3'-bromo-carboxin
-
not inhibitory
3'-bromo-carboxin
-
inhibits
3'-fluoro-carboxin
-
not inhibitory
3'-fluoro-carboxin
-
inhibits
3'-n-butyl-carboxin
-
not inhibitory
3'-n-butyl-carboxin
-
inhibits
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
-
-
3-nitropropionate
-
-
3-nitropropionic acid
-
irreversible inactivation, 0.00001 mM, 50% inhibition
3-nitropropionic acid
-
this study compares the effects of 3-nitropropionic acid in young and old mice. Treatment with 3-nitropropionic acid induces OD in young mice. Old mice present an increase in the basal level of orofacial movement that is not potentiated by any dose of 3-nitropropionic acid. Histochemical analyses show that old mice present an increase in the SDH activity. 3-Nitropropionic acid induces a decrease in SDH activity at both ages
3-nitropropionic acid
-
-
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
-
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
-
-
4,4,4-trifluoro-1-(2-thienyl)-1,3-butanedione
-
0.006 mM, 50% inhibition
4,4,4-trifluoro-1-(thiophen-2-yl)butane-1,3-dione
-
-
4-Chloromercuriphenyl sulfonate
-
-
4-Chloromercuriphenyl sulfonate
-
-
4-Chloromercuriphenyl sulfonate
-
inhibitor of the succinate-ubiquinone reductase reaction
4-Chloromercuriphenylsulfonate
-
0.003 mM/g protein 50% inhibition
5,5'-dithiobis(2-nitro-benzoic acid)
-
inactivates, conformation-change type inhibition, the presence of the substrate provides marked protection
5,5'-dithiobis(2-nitrobenzoate)
-
inhibition is reversed by addition of dithiothreitol or dithionite
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide
-
i.e., carboxin
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
-
-
5-(n-Undecyl)-6-hydroxy-4,7-oxobenzothiazole
-
UHDBT
5-Hydroxy-2-methyl-1,4-naphthoquinone
-
inhibition is only 50% even at 0.1 mM
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
acetoacetate
-
-
alpha-tocopheryl succinate
-
binds to the Qp site of the mitochondrial complex II causing the generation of superoxide triggering mitochondrial destabilisation and initiation of apoptotic pathways, mechanism, overview
amicarthiazol
Q6DLZ2, Q6DLZ3
i.e. 2-amino-4-methylthiazole -5-carboxanilide, a systemic fungicide. The wild-type enzyme is strongly inhibited by amicarthiazol, while that in resistant mutants is insensitive. A single amino acid substitution H229Y in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, molecular resistance mechanism, overview; i.e. 2-amino-4-methylthiazole-5-carboxanilide, a systemic fungicide. The wild-type enzyme is strongly inhibited by amicarthiazol, while that in resistant mutants is insensitive. A single amino acid substitution H229Y in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, molecular resistance mechanism, overview
-
atpenin A4
-
0.00001 mM, 50% inhibition
atpenin A4
-
0.000024 mM, 50% inhibition
atpenin A5
-
0.0000042 mM, 50% inhibition
atpenin A5
-
0.000004 mM, 50% inhibition
bicarbonate
-
-
carboxin
-
Q2-mediated Wurster's blue reduction: 90% inhibition at 0.02 mM, Q0-mediated Wurster's blue reduction: 75% inhibition at 0.02 mM, Q1-mediated Wurster's blue reduction: 88% inhibition at 0.02 mM, Q6-mediated Wurster's blue reduction: 50% inhibition at 0.02 mM
carboxin
-
15% inhibition of the succinate-ubiquinone reductase and of the quinol-fumarate reductase reaction, competitive inhibition with quinone or quinol
carboxin
-
15% inhibition of succinate dehydrogenase activity of larval and adult complex II at 0.001 mM
carboxin
-
not inhibitory
carboxin
-
more than 90% inhibition in isolated membranes at high concentrations, the mutant enzyme is less sensitive than wild-type enzyme
carboxin
-
inhibits the succinate dehydrogenase in the forward and reverse reaction
carboxin
-
not inhibitory
carboxin
-
interferes with electron transfer from the 3Fe-4S center to quinone, carboxin may bind to a quinone-binding site the Qp site, close to the 3Fe-4S center, amino acids involved in binding carboxin: a histidine residue in the B subunit and an aspartate residue in the D subunit
carboxin
-
0.001 mM, 50% inhibition
Cd2+
-
inhibits possibly due of interfering with energy transport mechanism
Chaotropic reagents
-
e.g. perchlorate, thiocyanate
-
clozapine
-
chronic administration of the antipsychotic agent, inhibit SDH activity only in the striatum
CN-
-
not inhibitory: when mixed with succinate or alone
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
D-Chlorosuccinate
-
-
D-Methylsuccinate
-
-
diethyl oxaloacetate
-
-
ferricyanide
-
at concentrations above 3 mM
formate
-
-
fumarate
-
-
fumarate
-
competitive
glycolate
-
-
glyoxylate
-
-
haloperidol
-
chronic administration of the antipsychotic agent, inhibits SDH activity in the hippocampus and striatum but not in the cerebellum, cortex, and prefrontal cortex
harzianopyridone
-
0.00002 mM, 50% inhibition
harzianopyridone
-
0.0002 mM, 50% inhibition
iodoacetamide
-
-
Maleate
-
-
-
Maleate
-
-
-
malonate
-
inhibits both succinate dehydrogenase and fumarate reductase
malonate
-
0.18 mM, 50% inhibition
malonate
-
competitive
menaquinone-1
-
competitive inhibitor of the succinate oxidation reaction of succinate dehydrogenase
Methylene succinate
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
nonyl-4-hydroxyquinoline-N-oxide
-
-
-
nonyl-4-hydroxyquinoline-N-oxide
-
the semiquinone analog and inhibitor of quinone reactions in complex II shows no influence on the redox behavior of the heme b moieties
-
olanzapine
-
chronic administration of the antipsychotic agent, inhibits SDH activity only in the cerebellum, but not in the hippocampus, striatum, cortex, and prefrontal cortex
oxaloacetate
-
-
oxaloacetate
-
competitive inhibitor
oxaloacetate
-
reactivation by reduction of enzyme with succinate; reactivation with anions
oxaloacetate
-
reactivation by reduction of enzyme with succinate
oxaloacetate
-
at 0.0006 mM: 20% inhibition of the succinate-ubiquinone reductase reaction and no inhibition of the fumarate reductase reaction, at 0.006 mM: 80% inhibition of fumarate reductase reaction
oxaloacetate
-
-
oxaloacetate
-
an inhibitor of the succinate binding site
p-benzoquinone
-
inhibition of succinate dehydrogenase activity using phenazone methosulfate or 2,6-dichlorophenolindophenol as electron acceptor; inhibitory to the succinate dehydrogenase activity assay using phenazine methosulfate and 2,6-dichloroindophenol
p-chloromercuribenzoate
-
-
papyriferic acid
-
papyriferic acid is a triterpene that is secreted by glands on twigs of the juvenile ontogenetic phase of resin producing tree birches. Papyriferic acid is a potent inhibitor of SDH. Kinetic analysis indicate that, unlike malonate, papyriferic acid acts by an uncompetitive mechanism, by binding to the enzyme-substrate complex. The hydrolysis product of papyriferic acid, betulafolienetriol oxide, is inactive on SDH. Papyriferic acid acts as an intact molecule and interacts at a site other than the succinate binding site, possibly binding to the ubiquinone sites on complex II
Pentachlorophenol
-
competitive inhibitor of both succinate dehydrogenase and fumarate reductase
rotenone
-
inhibits fumarate reductase, not succinate dehydrogenase
sec-butyl-4,6-dinitrophenol
-
non-competitive inhibition
sec-butyl-4,6-dinitrophenol
-
-
siccanin
-
residual activity: 7%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
-
residual activity: 13%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
-
residual activity: above 1%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
siccanin
-
residual activity: 19%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
sodium fumarate
-
EC50 fumarate reductase 0.6 mM and EC50 succinate dehydrogenase 4.8 mM
sodium malonate
-
EC50 fumarate reductase 19 mM and EC50 succinate dehydrogenase 0.68 mM
tetrachlorobenzoquinone
-
strong inhibition of succinate-phenazine methosulfate-(1,4-dichloroindophenol) oxidoreductase
thenoyltrifluoroacetate
-
inhibits a later step of the electron flow as it binds to the ubiquinone docking sites and abrogates the transfer of electrons to this molecule. It causes a time- and dose-dependent increase of apoptosis. 20% inhibition at 0.5 mM
thiabendazole
-
EC50 fumarate reductase 0.46 mM and EC50 succinate dehydrogenase 1 mM
thiol reagents
-
-
thiol reagents
-
-
trans-[RuCl2(3,4-pyridinedicarboxylic acid)4]
-
inhibits the enzyme of skeletal muscle and liver
trans-[RuCl2(3,5-pyridinedicarboxylic acid)4]
-
inhibits the enzyme of heart, skeletal muscle, liver, and kidney
trans-[RuCl2(3-pyridinecarboxylic acid)4]
-
inhibits the enzyme of hippocampus, cerebral cortex, heart and liver
trans-[RuCl2(4-pyridinecarboxylic acid)4]
-
inhibits the enzyme of heart and hippocampus
ubiquinol-2
-
competitive inhibitor of the fumarate reduction reaction of fumarate reductase
vitamin E analogues
-
epitomised by alpha-tocopheryl succinate affect the electron flow from complex II
-
Methylsuccinate
-
-
additional information
-
15-20% inhibition of complex II activity in striatum and hippocampus by methylmalonic acid at low concentrations of sucinate in the medium, but not in the peripheral tissue. the inhibitory property only occurs after exposing brain homogenates for at least 10 min with the acid, suggesting that this inhibition is mediated by indirect mechanisms
-
additional information
-
zidovudine, i.e. 3'-azido-3'-deoxythymidine or AZT, represses the enzyme content in mitochondria of cultured rat muscle cells by 13% via reducing the mitochondrial DNA content by 66% at 0.1 mg/ml, histochemic analysis, overview
-
additional information
-
residual activity: 97%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
-
additional information
-
residual activity: above 77%. Structure of siccanin is similar to ubiquinone-1. Siccanin, is effective against enzymes from Pseudomonas aeruginosa, Pseudomonas putida, rat and mouse mitochondria but ineffective or less effective against Escherichia coli, Corynebacterium glutamicum, and porcine mitochondria enzyme. Action mode is mixed-type for quinone-dependent activity and non-competitive for succinate-dependent activity, indicating the proximity of the inhibitor-binding site to the quinone-binding site
-
additional information
-
not inhibitory: heptyl 4-hydroxyquinoline N-oxide
-
additional information
-
transition from darkness to light causes a short transient increase in the SDH activity followed by a decrease to a half of the original activity
-
additional information
-
different pro-apoptotic agents responsible for complex II inhibition lead to mitochondrial matrix acidification
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-Dinitrophenol
-
activation
2,4-Dinitrophenol
-
activation
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
slightly activates
antimycin A
-
activates
aripiprazole
-
chronic administration of the antipsychotic agent, increases SDH activity in the prefrontal cortex at high doses of 20 mg/kg body weight
ATP
-
activation
ATP
-
activation
cardiolipin
-
stimulation in presence of detergent
Chaotropic anions
-
activation
-
cytochrome b-558
-
-
-
cytochrome b-558
-
-
-
diphosphate
-
activation
dithiothreitol
-
required for activity
flavin
-
the 66000 Da subunit is the flavoprotein subunit containing a covalently bound flavin
FMNH2
-
activation
FMNH2
-
activation
fumarate
-
activation
fumarate
-
activation
IDP
-
activation
IDP
-
activation
Iron-sulfur cluster
-
the cluster is fixed by cysteines of two cysteine-rich CCG domain sequence motifs (CX31-39CCX35-36CXXC) of subunit Sdh of the Sulfolobus solfataricus succinate:quinone reductase
ITP
-
activation
ITP
-
activation
KCN
-
activation at 6.7 mM up to 10 mM when both alternative pathways to oxygen are inhibited
malonate
-
activation
malonate
-
activation
malonate
-
activation
medium-chain triglycerides ketogenic diet
-
cytochemical investigation of SDH activity in cardiomyocytes of late adult rats fed for 8 weeks with a medium-chain triglycerides ketogenic diet is performed. Young, age-matched and old animals fed with a standard chow are used as controls. It is shown that the medium-chain triglycerides ketogenic diet intake partially recovers age-related decrease of SDH activity and increases the myocardial area occupied by metabolically active mitochondria. These effects might counteract metabolic alterations leading to apoptosis-induced myocardial atrophy and failure during aging
-
Na2SO4
-
activation
NaN3
-
activation
phenazine methosulfate
-
-
phosphate
-
activation
phosphate
-
activation
Phospholipids
-
activation
Phospholipids
-
activation
reduced ubiquinone-10
-
activation
Sodium citrate
-
activation
succinate
-
activation
succinate
-
activation
succinate
-
activation
succinyl coenzyme A
-
activation
succinyl-CoA
-
activation
Tcm62
-
importance in SDH assembly
-
menaquinone-9(2H)
-
-
additional information
-
overview
-
additional information
-
stimulation of SIRT3 expression decreases the level of acetylation of the SdhA subunit and increases Complex II activity in kaempherol-treated cells compared to control and nicotinamide-treated cells
-
additional information
-
transition from darkness to light causes a short transient increase in the SDH activity followed by a decrease to a half of the original activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
value below
0.0034
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22C
0.0037
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22C
0.0048
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
wild-type
0.007
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
H106Y mutant
0.0073
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
H106L/D117V mutant
0.01
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
F103V mutant
0.011
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
L122stop mutant
0.015
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
H113Q mutant
0.018
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
W116R mutant
0.003
-
2,6-dichlorophenol indophenol
-
22C, wild-type strain YPH499
0.007
-
2,6-dichlorophenol indophenol
-
22C, Sdh3p/Sdh4p double mutant strain H106A/C78A
0.06
-
caldariellaquinone
-
pH 6.8, 50C
0.18
-
caldariellaquinone
-
pH 6.5, 55C
1.5
-
D-malate
-
-
0.011
-
decylubiquinone
-
pH 7.6, 30C
0.3
-
ferricyanide
Escherichia coli, facultative anaerobic bacterium, Mammalia
-
-
0.3
-
ferricyanide
-
-
0.3
-
ferricyanide
-
-
0.005
-
fumarate
-
succinate oxidation, pH 7.8, 30C
0.0149
-
fumarate
-
-
0.025
-
fumarate
-
fumarate reduction, Km of fumarate does not depend on concentration of quinol
0.06
-
fumarate
-
pH 6.5, 70C, determined for activity in membranes from aerobic growth
0.1
-
fumarate
-
65C, pH 6.5
0.143
-
fumarate
-
complex II from adult nematode
0.15
-
fumarate
-
succinate oxidation
0.35
-
fumarate
-
donor menadiol
0.4
0.7
fumarate
-
-
0.455
-
fumarate
-
complex II from larvae
0.0654
-
oxidized 1,4-dichloroindophenol
-
pH 6.5, 55C
-
0.089
-
oxidized 2,6-dichlorophenolindophenol
-
pH 6.8, 50C
0.0991
-
oxidized N,N,N',N'-tetramethyl-4-phenylenediamine
-
pH 6.5, 55C
-
0.295
-
oxidized phenazine methosulfate
-
pH 6.5, 55C
-
0.11
-
phenazine methosulfate
-
-
0.48
-
phenazine methosulfate
-
-
0.48
-
phenazine methosulfate
-
-
0.11
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101L; pH 8.0, 25C, recombinant subunit SDHD mutant Q78L
0.124
-
reduced plumbagin
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95L
0.128
-
reduced plumbagin
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95E
0.13
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHB mutant G227L
0.14
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101D
0.16
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95L
0.17
-
reduced plumbagin
-
pH 8.0, 25C, recombinant wild-type enzyme
0.19
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95E
0.002
-
succinate
-
fumarate reduction, pH 7.8, 30C
0.0025
-
succinate
-
30C, pH 7.8
0.02
-
succinate
-
-
0.02
-
succinate
-
-
0.023
-
succinate
-
-
0.03
-
succinate
-
fumarate reduction
0.04
-
succinate
-
30C, pH 7.8, H84L mutant
0.049
-
succinate
-
-
0.1
-
succinate
-
-
0.12
-
succinate
-
-
0.13
-
succinate
-
succinate oxidation, determined at 0.01 mM ubiquinone-2
0.138
-
succinate
-
succinate with papyriferic acid 0.04 mM, pH 7.4, 25C
0.153
-
succinate
-
complex II from larvae
0.165
-
succinate
-
succinate with papyriferic acid 0.04 mM, pH 7.4, 25C
0.165
-
succinate
-
65C, pH 6.5
0.167
-
succinate
-
succinate with papyriferic acid 0.08 mM, pH 7.4, 25C
0.21
-
succinate
-
pH 7.6, 30C
0.23
-
succinate
-
-
0.25
-
succinate
-
30C, pH 7.0
0.27
-
succinate
-
for both membrane fragments and mitochondrial enzyme
0.28
-
succinate
-
pH 6.8, 50C
0.29
-
succinate
-
-
0.3
-
succinate
-
-
0.303
-
succinate
-
succinate alone, pH 7.4, 25C
0.339
-
succinate
-
succinate alone, pH 7.4, 25C
0.414
-
succinate
-
succinate alone, pH 7.4, 25C
0.5
-
succinate
-
pH 6.5, 70C, determined for activity in membranes from aerobic growth
0.608
-
succinate
-
complex II from adult nematode
0.7
-
succinate
-
membrane bound enzyme
1.42
-
succinate
-
pH 6.5, 55C
1.5
-
succinate
-
-
2.3
-
succinate
-
soluble enzyme
0.0025
-
ubiquinone
-
wild-type SQR
0.01
-
ubiquinone
-
mutant E29F, pH 7.9, 30C
0.01
-
ubiquinone
-
mutant H71Y
0.012
-
ubiquinone
-
mutant H71Y
0.013
-
ubiquinone
-
mutant H71Y/A72C
0.014
-
ubiquinone
-
mutant enzyme
0.017
-
ubiquinone
-
wild-type enzyme
0.027
-
ubiquinone
-
mutant E29L, pH 7.9, 30C
0.06
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHD mutant Q78L
0.07
-
ubiquinone
-
wild-type, pH 7.9, 30C
0.07
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95L
0.09
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHB mutant G227L; pH 8.0, 25C, recombinant subunit SDHC mutant E101L
0.1
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101D
0.13
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95E
0.15
-
ubiquinone
-
pH 8.0, 25C, recombinant wild-type enzyme
0.16
-
ubiquinone
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95L
0.2
-
ubiquinone
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95E
0.0016
-
ubiquinone-1
-
-
0.003
-
ubiquinone-1
-
larval and adult complex II
0.02
-
ubiquinone-1
-
pH 6.8, 50C
0.00017
-
ubiquinone-2
-
differences in Km value (9fold) and Vmax/Km ratio (19fold) between Q1 and Q2 indicate that the 6-polyprenyl tail of the ubiquinone ring contributes to the binding affinity and that Q2 is better substrate than Q1
0.0005
-
ubiquinone-2
-
-
0.0089
-
ubiquinone-2
-
S33C mutant
0.009
-
ubiquinone-2
-
R19A and F20L mutants
0.01
-
ubiquinone-2
-
S33T mutant
0.0102
-
ubiquinone-2
-
T17A mutant
0.0106
-
ubiquinone-2
-
H30A mutant
0.0108
-
ubiquinone-2
-
wild-type and T23A mutant
0.0114
-
ubiquinone-2
-
S33A mutant
1.14
-
ferrocyanide
-
pH 6.5, 55C
additional information
-
fumarate
-
with menaquinone EC 1.3.5.4, succinate oxidation: 0.003 mM, pH 7.8, 30C
2.2
-
L-Malate
-
-
additional information
-
additional information
-
overview mammalian enzyme
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
succinate-quinone and quinol-fumarate reductase reaction of succinate dehydrogenase and fumarate reductase
-
additional information
-
additional information
-
no effect of phosphate on fumarate reductase, but increase of Km of succinate dehydrogenase
-
additional information
-
additional information
-
midpoint potentials of [3Fe-4S] cluster and heme b, kinetics and kinetic isotope effects of recombinant wild-type and mutant enzymes at different pH in both reaction directions, overview
-
additional information
-
additional information
-
steady-state kinetic measurements show that the enzyme displays standard Michaelis-Menten kinetics at a low temperature of 30C but exhibits deviation from it at a higher temperature of 70C, the enzyme shows positive cooperativity at higher temperatures
-
additional information
-
additional information
-
interprotomer temperature-dependent positive cooperativity in the trimeric complex. Only the trimer, not the monomer, exhibits positive cooperativity at high temperatures
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.67
-
1,4-Naphthoquinone
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30C
35
-
2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
isolated complex
182
-
2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
membrane preparation
3.6
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22C
60
-
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
22C
1.83
-
2,6-dichlorophenolindophenol
-
pH 7.6, 30C
9.4
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95L
-
12.6
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101L
-
15.9
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant subunit SDHB mutant G227L
-
17.4
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95L
-
18
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101D
-
19.9
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95E
-
20.8
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant subunit SDHD mutant Q78L
-
20.9
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant wild-type enzyme
-
29.6
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95E
-
0.283
-
D-malate
-
-
1.7
-
fumarate
-
succinate oxidation, pH 7.8, 30C
79.6
-
fumarate
-
65C, pH 6.5
0.142
-
L-Malate
-
-
0.2
-
naphthoquinol
-
mutant enzyme
2
-
naphthoquinol
-
wild-type enzyme
8.33
-
phenazine methosulfate
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30C
7.7
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101L
8.6
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95L
9.1
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHB mutant G227L
9.3
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHD mutant Q78L
10.4
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101D
12.7
-
reduced plumbagin
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95E
15.9
-
reduced plumbagin
-
pH 8.0, 25C, recombinant wild-type enzyme
21.5
-
reduced plumbagin
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95L
23
-
reduced plumbagin
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95E
0.1
-
succinate
-
mutant K228R, cosubstrate ubiquinone, pH 7.9, 30C
0.3
-
succinate
-
mutant K228L, cosubstrate ubiquinone, pH 7.9, 30C
10
-
succinate
-
mutant enzyme
20.4
-
succinate
-
mutant E49F, cosubstrate ubiquinone, pH 7.9, 30C
23
-
succinate
-
mutant E49L, cosubstrate ubiquinone, pH 7.9, 30C
24
-
succinate
-
wild-type, cosubstrate ubiquinone, pH 7.9, 30C
28.3
-
succinate
-
-
66.7
-
succinate
-
-
78
-
succinate
-
30C, pH 7.8
83.3
150
succinate
-
based on FAD content, dependency on assay temperature
85
-
succinate
-
fumarate reduction, pH 7.8, 30C
90
100
succinate
-
-
167
217
succinate
-
-
167
217
succinate
-
-
167
217
succinate
-
-
167
217
succinate
-
-
260
-
succinate
-
wild-type enzyme
82
-
succinate-phenazine ethosulfate
-
30C, pH 7.8
11.6
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHB mutant G227L
15.6
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101L
16.2
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95L
17.4
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHD mutant Q78L
18.6
-
ubiquinone
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95E
20.9
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant E101D
22.3
-
ubiquinone
-
pH 8.0, 25C, recombinant subunit SDHC mutant D95E
24.8
-
ubiquinone
-
pH 7.0, 25C, recombinant subunit SDHB/C mutant G227L/D95L
37.9
-
ubiquinone
-
pH 8.0, 25C, recombinant wild-type enzyme
167
-
ubiquinone
-
-
2.167
-
duroquinone
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30C
additional information
-
fumarate
-
with menaquinone EC 1.3.5.4: , succinate oxidation: 3.4 s-1, pH 7.8, 30C
1.67
-
menadione
-
with 2,6-dichlorophenolindophenol, pH 7.6, 30C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
succinate-quinone and quinol-fumarate reductase reaction of succinate dehydrogenase and fumarate reductase
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.5e-05
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
fumarate reductase, succinate oxidation reaction
0.0002
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
fumarate reductase, fumarate reduction reaction
0.0002
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
-
0.0004
-
2-(n-heptyl)-4-hydroxy-quinoline N-oxide
-
inhibitor of the activity of mutant and wild-type enzyme
0.0013
-
2-alkyl-4,6-dinitrophenol-17
-
fumarate reductase, succinate oxidation reaction
0.002
-
2-alkyl-4,6-dinitrophenol-17
-
fumarate reductase, fumarate reduction reaction
0.017
-
2-alkyl-4,6-dinitrophenol-17
-
succinate dehydrogenase, succinate oxidation reaction
0.0015
-
2-alkyl-4,6-dinitrophenol-20
-
fumarate reductase, succinate oxidation reaction
0.002
-
2-alkyl-4,6-dinitrophenol-20
-
fumarate reductase, fumarate reduction reaction
0.019
-
2-alkyl-4,6-dinitrophenol-20
-
succinate dehydrogenase, succinate oxidation reaction
0.0009
-
2-n-heptyl-4-hydroxyquinoline
-
purified enzyme
3e-05
-
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
mutant E29L, pH 7.9, 30C
5e-05
-
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
wild-type, pH 7.0, 30C
0.00062
-
2-n-heptyl-4-hydroxyquinolino-N-oxide
-
pH 7.6, 30C
7e-06
-
atpenin A4
-
25C, pH 7.5
1e-06
-
atpenin A5
-
25C, pH 7.5
0.001
-
carboxin
-
-
0.002
-
carboxin
-
succinate oxidation
0.003
-
carboxin
-
fumarate reduction
0.03
-
carboxin
-
succinate dehydrogenase, succinate oxidation reaction
0.035
-
carboxin
-
succinate dehydrogenase, fumarate reduction reaction
0.04
-
fumarate
-
-
0.15
-
fumarate
-
-
0.35
-
fumarate
-
-
1.3
-
fumarate
-
-
7e-06
-
harzianopyridone
-
25C, pH 7.5
6.2
-
Maleate
-
-
-
0.00025
-
malonate
-
-
0.018
-
malonate
-
-
0.0218
-
malonate
-
-
0.0246
-
malonate
-
-
0.088
-
malonate
-
pH 7.6, 30C
0.012
-
menaquinone-1
-
succinate dehydrogenase, succinate oxidation reaction
1.8
-
Methylene succinate
-
-
0.00034
-
oxaloacetate
-
-
0.00115
-
oxaloacetate
-
-
0.0015
-
oxaloacetate
-
-
0.0015
-
oxaloacetate
-
-
0.02567
-
papyriferic acid
-
pH 7.4, 25C
0.03573
-
papyriferic acid
-
pH 7.4, 25C
0.013
-
Pentachlorophenol
-
succinate dehydrogenase, succinate oxidation reaction
0.017
-
Pentachlorophenol
-
succinate dehydrogenase, fumarate reduction reaction
0.017
-
Pentachlorophenol
-
30C, pH 7.8
0.023
-
Pentachlorophenol
-
fumarate reductase, succinate oxidation reaction
0.037
-
Pentachlorophenol
-
fumarate reductase, fumarate reduction reaction
0.083
-
Pentachlorophenol
-
30C, pH 7.8, H84L mutant
0.015
-
ubiquinol-2
-
fumarate reductase, fumarate reduction reaction
0.008
-
2-Thenoyltrifluoroacetone
-
-
additional information
-
5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide
-
with menaquinone EC 1.3.5.4, fumarate reduction: 0.030 mM, pH 7.8, 30C; with menaquinone EC 1.3.5.4, succinate oxidation: 0.035 mM, pH 7.8, 30C
0.04527
-
papyriferic acid
-
pH 7.4, 25C
additional information
-
Pentachlorophenol
-
with menaquinone EC 1.3.5.4, fumarate reduction: 0.013 mM, pH 7.8, 30C; with menaquinone EC 1.3.5.4, succinate oxidation: 0.017 mM, pH 7.8, 30C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00011
-
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
-
-
0.00233
-
(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)(3-phenoxyphenyl)methanone
-
-
0.00033
-
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
0.03
-
(4-chlorophenyl)(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
value above
0.00063
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
-
-
0.03
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,2-diphenylethanone
-
value above
1e-05
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
-
-
5.1e-05
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2,6-dimethylhept-5-en-1-one
-
-
0.00013
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
-
-
0.000234
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-ethylhexan-1-one
-
-
0.0001
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
-
-
0.00258
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylbutan-1-one
-
-
2e-05
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
-
-
0.000122
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylhexan-1-one
-
-
3e-06
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
-
-
4e-06
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylundecan-1-one
-
-
1e-05
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
-
-
0.000299
-
1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-phenylpropan-1-one
-
-
0.03
-
2,3-dimethoxy-5-(2-methylbutanoyl)pyridin-4(1H)-one
-
value above
0.0128
-
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
-
-
0.0207
-
2,3-dimethoxy-5-(naphthalen-2-ylcarbonyl)pyridin-4(1H)-one
-
-
0.03
-
2,3-dimethoxy-5-[(2-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
value above
0.00045
-
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
0.00298
-
2,3-dimethoxy-5-[(3-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
0.03
-
2,3-dimethoxy-5-[(4-methoxyphenyl)carbonyl]pyridin-4(1H)-one
-
value above
0.00049
-
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
0.00408
-
2,3-dimethoxy-5-[(4-phenoxyphenyl)carbonyl]pyridin-4(1H)-one
-
-
0.00127
-
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
-
-
0.00194
-
2-bromo-3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridin-4(1H)-one
-
-
1e-05
-
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
-
-
2.4e-05
-
3-(4-tert-butylphenyl)-1-(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)-2-methylpropan-1-one
-
-
0.03
-
3-[(4-chlorophenyl)carbonyl]-2,5,6-trimethoxypyridin-4(1H)-one
-
value above
0.0138
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
-
-
0.0139
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxy-2-methylpyridin-4(1H)-one
-
-
0.03
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl diacetate
-
value above
0.03
-
3-[(4-chlorophenyl)carbonyl]-5,6-dimethoxypyridine-2,4-diyl dimethanesulfonate
-
value above
0.0008
-
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
-
-
0.00275
-
5-(biphenyl-4-ylcarbonyl)-2,3-dimethoxypyridin-4(1H)-one
-
-
0.03
-
5-[(2-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
value above
0.00656
-
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
0.03
-
5-[(3-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
value above
0.0034
-
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
0.0267
-
5-[(4-chlorophenyl)carbonyl]-2,3-dimethoxypyridin-4(1H)-one
-
-
4e-06
-
atpenin A5
-
-
1.1e-05
-
atpenin A5
-
-
0.0046
-
atpenin A5
-
-
0.000245
-
boscalid
-
-
0.00179
-
boscalid
-
-
0.0036
-
carboxin
-
-
0.00013
-
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
0.00178
-
cyclohexyl(2,4-dihydroxy-5,6-dimethoxypyridin-3-yl)methanone
-
-
0.0009
-
siccanin
-
pH 7.4, 25C
0.009
-
siccanin
-
pH 7.4, 25C
0.21
-
siccanin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0007
0.0011
-
liver SDH in presence of Cd2+, pH not specified in the publication, temperature not specified in the publication
0.0076
-
-
electron accepotr 2,6-dichlorophenolindophenol, pH 7.6, 30C
0.01
-
-
measured by the rate of dichloroindophenol reduction
0.024
-
-
SQR activity in raji cells
0.026
-
-
liver SDH, pH not specified in the publication, temperature not specified in the publication
0.039
-
-
SQR activity in HT-29 cells
0.05
0.095
-
pH 7.4, 37C, SDH activity for each metabolic state, i.e. torpor, early arousal, late arousal, interbout euthermia and summer-active, overview
0.0547
-
-
egg mitochondria
0.135
-
-
heart mitochondria
0.136
-
-
muscle mitochondria
0.154
-
-
liver mitochondria
0.706
-
-
complex II from larvae, fumarate reductase activity
1.2
-
-
-
2.04
-
-
isolated complex II
3.53
-
-
complex II from adult nematode, succinate dehydrogenase activity
4.28
-
-
complex II from larvae, succinate dehydrogenase activity
6.1
-
-
cosubstrate 2,3-dimethyl-1,4-naphthoquinol, pH not specified in the publication, temperature not specified in the publication
7.5
-
-
pH 6.5, 55C
28
54
-
depending on assay temperature
28.9
-
-
complex II from adult nematode, fumarate reductase activity
29
-
-
-
56
-
-
-
57.5
-
-
; pH 7.0, 30C
67
78
-
-
additional information
-
Rhodospirillum sp.
-
fumarate reductase with methyl viologen and succinate dehydrogenase activities in cell-free extracts of members of the family with different quinone types
additional information
-
-
-
additional information
-
-
distribution of 2,3-dimethoxy-5-methyl-1,4-benzoquinone reductase activity in cells transformed with fumarate reductase plasmids
additional information
-
-
activities of wild-type and mutants, expressed in micromol of succinate oxidized/min/nmol of cytochrome b556
additional information
-
-
comparison of assay methods
additional information
-
-
catalytic efficiencies of recombinant wild-type and mutant enzymes at different pH in both reaction directions, overview
additional information
-
-
activities in hyperadrenergic newborn or adult rat leukocytes, overview
additional information
-
-
-
additional information
-
-
substrate specificities of wild-type and mutant enzymes, overview
additional information
-
-
enzyme activity in motoneurons of soleus and tibialis anterior muscles, overview
additional information
-
-
mean initial reaction velocities in four areas of lateral pterygoid muscle from rat brain, overview
additional information
-
-
when comparing with rat liver mitochondria, succinate-quinone reductase activity of Plasmodium yoelii yoelii, is 1.4% of rat liver succinate-quinone reductase
additional information
-
-
the succinate-dependent reactive oxygen species production from the complex II of the Ascaris suum adult worm is significantly higher than that from the complex II of the L3 larvae
additional information
-
-
enzyme shows no succinate oxidation activity but strong fumarate reduction activity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
-
6.5
-
-
assay at
6.6
6.8
-
-
6.6
6.8
-
assay at
7
7.2
-
phosphate buffer
7.2
-
-
assay at
7.3
-
-
Tris-acetate buffer
7.4
7.8
-
for both succinate dehydrogenase and fumarate reductase
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
assay at
7.6
-
-
assay at
7.8
-
-
assay at
7.8
-
-
with decylubiquinone-dichlorophenylindophenyl as electron acceptor
7.8
-
-
assay at
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
pH 5.5: about 40% of maximal activity, pH 7.5: about 55% of maximal activity
6
7.5
-
slow decline of activity at acidic pH, fast decline in alkaline range
6.5
-
-
decrease of activity below
8.5
-
-
80% of maximal activity
additional information
-
-
pH profile analysis, both EC 1.3.5.1 and 1.3.5.4 show a similar profile, suggesting that similar amino acid residues may be involved in quinol deprotonation and oxidation in Escherichia coli enzymes
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
Q09545
assay at
30
-
-
assay at
30
-
-
oxidation of succinate, assay at; reduction of fumarate, assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
38
-
-
assay at
50
-
-
assay at
70
-
-
assay at
75
81
-
from 30C to 75C the activity increases 45fold, with an optimum temperature between 75C and 81C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
75
-
from 30C to 75C the activity increases 45fold, with an optimum temperature between 75C and 81C
60
87
-
60C: about 40% of maximal activity, 87C: about 55% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
-
-
calculated from sequence, subunit 1
7.8
-
-
calculated from sequence, subunit 4
8.5
-
-
calculated from sequence, subunit 2
9.2
-
-
calculated from sequence, subunit 3
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
succinate dehydrogenase activity is suppressed in the muscle tissue after exposure to pesticides
Manually annotated by BRENDA team
-
significant decrease in activity following aluminium exposure. Post-treatment with centrophenoxine restores the altered enzyme activity
Manually annotated by BRENDA team
-
significant decrease in activity following aluminium exposure. Post-treatment with centrophenoxine restores the altered enzyme activity
Manually annotated by BRENDA team
-
15-20% inhibition of complex II activity in striatum and hippocampus by methylmalonic acid at low concentrations of sucinate in the medium, but not in the peripheral tissue. the inhibitory property only occurs after exposing brain homogenates for at least 10 min with the acid, suggesting that this inhibition is mediated by indirect mechanisms
Manually annotated by BRENDA team
Q8LB02, Q8LBZ7
highest expression
Manually annotated by BRENDA team
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
decreased complex II activity in diabetic hearts compared to control
Manually annotated by BRENDA team
-
15-20% inhibition of complex II activity in striatum and hippocampus by methylmalonic acid at low concentrations of sucinate in the medium, but not in the peripheral tissue. the inhibitory property only occurs after exposing brain homogenates for at least 10 min with the acid, suggesting that this inhibition is mediated by indirect mechanisms
Manually annotated by BRENDA team
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
; expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
after treatment with Bonny Light Crude Oil the specific activity of succinic dehydrogenase increases markedly at 5.0 ml/kg body weight Bonny Light Crude Oil over untreated controls
Manually annotated by BRENDA team
-
chlorpyrifos intoxication causes significant inhibition in the level of succinate dehydrogenase
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
soleus and tibialis anterior muscles
Manually annotated by BRENDA team
-
lateral pterygoid muscle in the head, activity in single muscle fibers in situ, the activity is higher in the upper and lateral areas than in the medial and lower areas, overview
Manually annotated by BRENDA team
-
muscle from adult stage
Manually annotated by BRENDA team
-
submitochondrial particles are prepared from frozen muscles of Ascaris suum adult female worms
Manually annotated by BRENDA team
-
pressure stimulus enhances SDH activity approx. 3fold
Manually annotated by BRENDA team
-
express only type II Fp subunit of SQR complex
Manually annotated by BRENDA team
Q8LB02, Q8LBZ7
-
Manually annotated by BRENDA team
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
Q8LB02, Q8LBZ7
-
Manually annotated by BRENDA team
-
from newborn and adult rats both in hyperadrenergic status, the activity in newborn rats is 3-8fold higher than in adult rats
Manually annotated by BRENDA team
additional information
-
loss of SDH activity in chief cells is found in the majority, i.e. 90%, of head and neck paragaliomas
Manually annotated by BRENDA team
additional information
-
aerobic growth on succinate and anaerobic growth on glycerol-fumarate
Manually annotated by BRENDA team
additional information
-
the pattern of SDH activity is consistent in general with the pattern of expression of the genes sdh2-3 and to a lesser extent of sdh1-2
Manually annotated by BRENDA team
additional information
-
differing pH profile in cells and growth of strains SA113 and HG001, overview. Various tricarboxylic acid (TCA) cycle genes, particularly the succinate dehydrogenase genes sdhCAB, are upregulated in Staphylococcus aureus biofilms
Manually annotated by BRENDA team
additional information
Staphylococcus aureus HG001, Staphylococcus aureus SA113
-
differing pH profile in cells and growth of strains SA113 and HG001, overview. Various tricarboxylic acid (TCA) cycle genes, particularly the succinate dehydrogenase genes sdhCAB, are upregulated in Staphylococcus aureus biofilms
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
succinate-quinone oxidoreductase is solubilized and purified from Escherichia coli inner membranes
-
Manually annotated by BRENDA team
-
SDH is attached to the membrane through Sdh3 and Sdh4 subunits
Manually annotated by BRENDA team
-
presence of 2 B type haem in the membrane anchoring subunits
Manually annotated by BRENDA team
-
membrane-bound SDH is used
Manually annotated by BRENDA team
-
membrane-bound enzyme is used
Manually annotated by BRENDA team
-
membrane-bound SDH is used
Manually annotated by BRENDA team
-
membrane-bound enzyme is used
Manually annotated by BRENDA team
-
membrane-bound, the catalytic domain is bound to the cytoplasmic membrane by 2 hydrophobic membrane anchor subunits that also form the sites of interaction with quinones
Manually annotated by BRENDA team
-
membrane anchoring based on the amphipathic nature of the putative helices found in subunit SdhC, is suggested
Manually annotated by BRENDA team
-
the membrane part of the enzyme is functionally connected to the active site
Manually annotated by BRENDA team
Bacillus subtilis 3G18
-
-
-
Manually annotated by BRENDA team
-
the membrane domain consists of two subunits SdhC and SdhD. The membrane domain contains a bound heme b moiety at the subunit interface with SdhC and SdhD each providing one of the two axial His ligands
Manually annotated by BRENDA team
Xanthomonas oryzae pv. oryzae ZJ173
-
;
-
Manually annotated by BRENDA team
-
the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
Manually annotated by BRENDA team
facultative anaerobic bacterium
-
-
Manually annotated by BRENDA team
-
inner membrane
Manually annotated by BRENDA team
-
of the adult parasitic nematode and of free living second stage larvae
Manually annotated by BRENDA team
-
; of the adult parasitic nematode and of free living second stage larvae
Manually annotated by BRENDA team
-
cytoplasmic side of inner membrane
Manually annotated by BRENDA team
-
mitochondria from L3 larvae and adult Ascaris suum muscle are prepared
Manually annotated by BRENDA team
-
mitochondrion from bovine heart are prepared
Manually annotated by BRENDA team
-
mitochondria from Septoria nodorum are prepared
Manually annotated by BRENDA team
-
; based on the presence of a predicted mitochondrial targeting peptides the protein is imported into mitochondria
Manually annotated by BRENDA team
-
enzyme isolated from mitochondria
Manually annotated by BRENDA team
-
the effect of papyriferic acid on the oxidation of succinate by SDH is examined in mitochondrial preparations from livers
Manually annotated by BRENDA team
-
submitochondrial particles are prepared from frozen muscles of Ascaris suum adult female worms
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
in contrast to all other members of this superfamily, the enzyme is exported into the periplasm via the twin-arginine translocation (tat)-pathway
-
Manually annotated by BRENDA team
Shewanella putrefaciens MR-1
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
-
-
sum of molecular weights of membrane anchor subunits is about 30 kDa
35000
-
-
iron-sulphur subunit
70000
-
-
flavoprotein subunit, identified by Western blot analysis
90000
100000
-
soluble enzyme, gel filtration, ultracentrifugation
90000
100000
-
monomeric form, gel filtration
97000
105000
facultative anaerobic bacterium, Mammalia
-
overview
97000
105000
-
sedimentation
97000
105000
-
heart, sedimentation, chromatography on agarose, calculation from FAD content
100000
-
-
succinate dehydrogenase
100000
-
-
SDS-PAGE after cross-linkage with dimethylsuberimidate, sedimentation equilibrium centrifugation
100000
-
-
gel filtration
110000
-
-
PAGE
118000
-
-
calculation from subunit composition
119800
-
-
monomeric recombinant C-terminally His6-tagged enzyme, gel filtration
120000
-
-
larval and adult complex II, non-denaturating PAGE
120000
-
-
-
135000
-
-
high resolution clear-native electrophoresis
141000
-
-
gel filtration
147000
-
-
calculation from Stokes radius and sedimentation coefficient
150000
-
-
blue native gel electrophoresis
170000
-
-
sedimentation equilibrium centrifugation of preparation containing Triton X-100
180000
-
-
dimeric form, gel filtration
260000
-
-
Blue-native PAGE
360000
-
P0AC41
trimer
410000
-
-
non-denaturing PAGE; PAGE
500000
-
-
native PAGE
500000
-
-
wild-type enzyme, consisting of 360 kDa from protein and an unknown contribution of detergent and lipid, native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
?
-
two different stage specific forms of complex II (EC 1.3.5.1) share a comme iron-sulfur subunit
?
-
? * 62000 + ? * 26000
?
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
?
-
x * 68000 (subunit 1) + x * 28400 (subunit 2) + x * 15300 (subunit 3) + x * 11100 (subunit 4), calculated from sequence
?
-
complex II is comprised of two hydrophilic proteins, flavoprotein (Fp) and iron-sulfur protein (Ip), and two transmembrane proteins (CybL and CybS), as well as prosthetic groups required for electron transfer from succinate to ubiquinone
?
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
?
-
x * 70000, about, HA-tagged Sdh1p, SDS-PAGE, x * 66000, cleaved HA-tagged Sdh1p, SDS-PAGE
?
Q920L2
x * 70000, flavoprotein of succinate dehydrogenase, SDS-PAGE
?
-
x * 32000, recombinant SDISP, SDS-PAGE
?
-
1 * 73234 + 1 * 28064 + 1 * 27097 Da calculated for flavoprotein, iron-sulfur protein, and cytochrome subunit, respectively. Complex is composed of three subunits, a 74 kDa flavoprotein that contains a covalently bound flavin adenine dinucleotide, a 28 kDa iron-sulfur cluster-containing polypeptide, and a 27 kDa transmembrane polypeptide, which is also the binding site of two b-type hemes and two menaquinones
?
-
enzyme consists of a 65000 Da flavoprotein SdhA, a 29000 Da iron-sulfur protein SdhB, and a 19000 Da subunit SdhC containing two b-type cytochromes, SDS-PAGE
?
-
1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
?
-
x * 67000 + x * 33000 + x * 28000 + x * 14000, SDS-PAGE
?
Schistosoma japonicum Chinese
-
x * 32000, recombinant SDISP, SDS-PAGE
-
?
-
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
-
?
Sulfolobus sp. 7
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
-
dimer
-
1 * 79000 + 1 * 31000, SDS-PAGE
dimer
-
calculation from gene sequence
dimer
-
1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
dimer
-
two additional polypeptides of 14000 and 15000 are necessary for the two large subunits to associate with the membrane
dimer
-
1 * 65000 (flavoprotein) + 1 * 28000 (ironprotein) + 19000 (cytochrome protein, membrane anchor), precipitation of radiolabeled protein with specific antibody and SDS-PAGE
dimer
-
1 * 7000 + 1* 27000, SDS-PAGE
dimer
-
1 * 65000 + 1 * 26000, large subunit is a flavoprotein, small subunit is an iron-sulfur protein
dimer
-
1 * 60000-79000 + 1 * 24000-31000, SDS-PAGE
dimer
-
1 * 60000 + 1* 25000, SDS-PAGE; amino acid composition of subunits
dimer
-
1 * 60000 + 1* 25000, SDS-PAGE
dimer
-
amino acid sequence around the flavin site
dimer
-
-
dimer
-
biosynthesis and processing
tetramer
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
tetramer
-
secondary structure
tetramer
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
tetramer
-
1 * 67000 + 1 * 30000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
-
heart, succinate dehydrogenase, SDS-PAGE
tetramer
-
amino acid sequence of Ip subunit
tetramer
-
1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
tetramer
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
tetramer
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
tetramer
-
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
tetramer
-
composed of a catalytic dimer, comprising a flavoprotein subunit Sdh1p and an iron-sulfur protein Sdh2p, and a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview
tetramer
-
subunits SdhA, SdhB, SdhC, and SdhD
tetramer
-
determined by high resolution clear-native electrophoresis and Western blot analysis. Enzyme consists of four subunits: a flavoprotein subunit (Fp, SDH1) and an iron-sulphur subunit (Ip, SDH2) form a soluble heterodimer, which binds to a membrane anchor b-type cytochrome (SDH3)/CybS (SDH4) heterodimer
tetramer
-
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
tetramer
-
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
-
trimer
-
1 * 65000-68700, Fp-subunit, FAD-binding, 1 * 27500-28000, Ip-subunit, Fe-S cluster containing, 1 * 19000-22000, membrane binding and cytochrome b containing subunit, SDS-PAGE
trimer
-
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
trimer
-
1 * 72000, 1 * 28000, 1 * 14000
trimer
P0AC41
3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis
trimer
-
trimer of the heterotrimeric protomer. 67000, subunit SdhA, 29000, subunit SdhB, 23000, subunit SdhC, SDS-PAGE
trimer
-
homotrimeric complex of the heterotrimeric protomer
trimer
-
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE
trimer
-
3 * 120000, about, wild-type enzyme, SDS-PAGE
trimer
Neurospora crassa 74A
-
1 * 72000, 1 * 28000, 1 * 14000
-
monomer
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
additional information
-
overview on structure, orientation in membranes and genetics
additional information
-
structure molecular dynamic simulations using the crystal structure with PDB ID 1PB4
additional information
-
the enzyme from Bacillus subtilis consists of two hydrophilic protein subunits comprising succinate dehydrogenase, and a di-heme membrane anchor protein harboring two putative quinone binding sites, overview
additional information
-
SdhC and SdhD form an active complex
additional information
-
structure-function relationships of SDH based on the porcine heart enzyme crystal structure, modeling at 2.4 A resolution, PDB ID 1ZOY
additional information
-
it is shown that lung stage L3 larvae mitochondria contain larval flavoprotein subunit (Fp) and adult flavoprotein subunit at a ratio of 1:0.56, and that most lung stage L3 larvae cytochrome b containing subunits CybS are of the adult form. This clearly indicates that the rearrangement of complex II begins with a change in the isoform of the anchor CybS subunit, followed by a similar change in the Fp subunit
additional information
-
cf. EC 1.3.5.1, both complexes contain a catalytic domain, composed of a subunit with a covalently bound flavin cofactor, the dicarboxlyate binding site, and an iron-sulfur subunit, which contains three distince iron-sulfur clusters. The catalytic domain is bound to the cytoplasmic membrane by two hydrophobic membrane anchor subunits that also form the sites for interaction with quinones. The catalytic domain is highly conserved and reflect the biochemical and structural similarity of EC 1.3.5.1 (SQR) and 1.3.5.4 (QFR). SQR, in addition to differences in the type of quinones it uses as compared to QFR, is known to contain a single B556 heme moiety, showing to have bis-histidine axial ligation
additional information
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
additional information
-
the catalytic core SdhA and SdhB subunits contain the redox cofactors that participate in electron transfer to ubiquinone. Sdh1 contains the covalently bound FAD cofactor and the binding site for succinate. Sdh2 contains the three Fe-S centers that mediate electron transfer to ubiquinone in the complex of succinate-ubiquinone dehydrogenase, EC 1.3.5.1, regulation of SDH, overview.The membrane domain consists of two subunits SdhC and SdhD. The membrane domain contains a bound heme b moiety at the subunit interface with SdhC and SdhD each providing one of the two axial His ligands
additional information
Q6DLZ2, Q6DLZ3
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB; succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
additional information
-
circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview
additional information
Bacillus subtilis 3G18
-
the enzyme from Bacillus subtilis consists of two hydrophilic protein subunits comprising succinate dehydrogenase, and a di-heme membrane anchor protein harboring two putative quinone binding sites, overview
-
additional information
Staphylococcus aureus HG001, Staphylococcus aureus SA113
-
SDH consists of three subunits: membrane-bound cytochrome b558, SdhC, a flavoprotein containing an FAD binding site, SdhA, and an iron-sulfur protein showing a binding region signature of the 4Fe-4S type, SdhB
-
additional information
Xanthomonas oryzae pv. oryzae ZJ173
-
succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB; succinate dehydrogenase forms the peripheral part of the succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
lipoprotein
-
-
side-chain modification
-
reversible acetylation of SdhA reduces the enzyme activity, activation by deacetylation by SIRT3
flavoprotein
-
covalent FAD modification of flavoprotein subunit 1 from complex II
side-chain modification
-
reversible acetylation of SdhA reduces the enzyme activity, activation by deacetylation by SIRT3. Acetylation of SdhA at conserved K179, K485, K498, and K538 residues, structure model, overview. Hyperacetylation of SdhA decreases Complex II activity in SIRT3 knockout mice
phosphoprotein
Q920L2
the flavoprotein of succinate dehydrogenase is an in vitro substrate of and phosphorylated at Tyr535 and Tyr596 by the Fgr tyrosine kinase, mass spectrometric analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
structure of subunits, binding sites, structure of complex II, pathway of electron transfer
-
X-ray diffraction data up to 3.2 resolution
-
by the hanging-drop vapour-diffusion technique
-
crystallization conditions are screened for succinate-quinone oxidoreductase that is solubilized and purified using 2.5% (w/v) sucrose monolaurate and 0.5% (w/v) Lubrol PX, respectively, and two different crystal forms are obtained in the presence of detergent mixtures composed of n-alkyl-oligoethylene glycol monoether and n-alkyl-maltoside. Crystallization takes place before detergent phase separation occurrs and the type of detergent mixture affects the crystal form
-
fumarate reductase, determined at 3.3 A, belongs to the type D enzymes: contains two hydrophobic subunits and no heme group
-
hanging-drop vapour-diffusion method, the enzyme is cocrystallized with the ubiquinone binding-site inhibitor Atpenin A5 (AA5) to confirm the binding position of the inhibitor and reveal additional structural details of the Q-site
-
hanging-drop vapour-diffusion, SQR in 20 mM Tris-HCl, pH 7.6, 0.05% THESIT is mixed with an equal volume of reservoir solution containing 100 mM Na-HEPES, pH 7.5, 200 mM, CaCl2 and 28% polyethylene glycol 400, crystals diffract to 2.6 A resolution
-
structure of SQR at 2.6 A resolution; structure of SQR is reported at 2.6 A resolution. The SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of reactive oxygen species
P0AC41
structure of subunits, binding sites, structure of complex II, pathway of electron transfer
-
three new structures of Escherichia coli succinate-quinone oxidoreductase are solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present is solved at 2.4 A resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. Comparison of the new succinate-quinone oxidoreductase structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone
-
sitting-drop vapour diffusion method. the crystals have the potential to diffract at least 2.0 A with optimization of post-crystal-growth treatment and cryoprotection. The most common form of crystals is the space group P2(1)2(1)2(1) with approximate unit-cell parameters a = 70 A, b = 84 A, c = 290 A. On a few occasions using slightly different conditions a second form has been obtained with space group P2(1) and unit cell parameters a = 120 A, b = 201 A, c = 68 A, alpha = beta = gamma = 90
-
structure of complex II in presence of oxaloacetate or with the endogenous inhibitor bound, structure of the malonate-bound complex
-
hanging drop method, crystal structure of complex II from porcine heart at 2.4 A resolution and its complex structure with inhibitors 3-nitropropionate and 2-thenoyltrifluoroacetone at 3.5 A resolution
-
partially purified enzyme, crystal growth in ammonium sulfate preparation precipitate, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
fumarate reductase, refined at 2.2-A resolution, belongs to the type B enzymes: contains one hydrophobic subunit and two heme groups
-
structure of subunits, binding sites, structure of complex II, pathway of electron transfer
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
inactivation below pH 5, stable for about 20 h without loss of activity at pH 6.0 in the presence of 0.1% Triton X-100
7.5
-
-
enzyme activity falls abruptly
8.5
-
-
fumarate reductase activity decreases to 80%
8.8
-
-
labile at alkaline pH
9
-
-
20 min, 50% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
enzyme activity remains constant for up to 5 h
25
-
-
62% loss of activity within 1 h
40
-
-
no loss of activity after 10 min
45
-
-
10 min, 50% loss of activity
45
-
-
inactivation
45
-
-
anions protect against thermoinactivation
55
-
-
1 h, stable
65
-
-
almost complete loss of activity after 10 min
68
-
-
approx. 50% loss of activity after 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
anions required for optimal stability
-
dithiothreitol required for optimal stability
-
dithiothreitol stabilizes during storage
-
extremely labile
-
stable during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
O2, 22% loss of activity during solublization period, only 3% loss if solubilization is performed under Ar
-
391114
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 1-2 weeks
-
-70C, as ammonium sulfate precipitate, or 50 mM phosphate buffer, pH 7.5, 20 mM succinate, 5 mM dithiothreitol, several months or several days at -20C
-
liquid N2 or -20C, pH 6.0, presence of 0.1% Triton X-100
-
room temperature, no loss of activity, for about 24 h
-
-20C in crude extract, soluble enzyme, 24 h, 50% loss of activity, membrane bound form no loss of activity
-
-70C, 0.2 mM dithiothreitol, 1 month
-
4C, N2-atmosphere
-
-80C, anaerobic conditions
-
-20C, in 10 mM MOPS-HCl, pH 7.4, 2-4% Thesit, 50% glycerol, stable for at least a few weeks
-
-70C or liquid N2
-
4C, N2-atmosphere
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
O73937 and O73937 and O73939 and O73940
of larval and adult complex II, using DEAE-cellulofine column chromatography in the presence of 0.1% w/v sucrose monolaurate
-
using detergent solubilization, ammonium sulfate fractionation and gel filtration on Sephadex G-200
-
using solubilization with sucrose monolaurate and column chromatography on DEAE-cellulose
-
and reconstitution into proteoliposomes
-
enzyme from membranes of strain 3G18, expressed from low copy plasmid
-
by selective resolution of complex II with chaotropic salts
-
from complex II, i.e. EC 1.3.5.1
-
isolation from the soluble cytochrome b-c1 complex of the mitochondrial protein, which converts soluble succinate dehydrogenase into succinate-ubiquinone oxidoreductase using two different methods, method 1: treatment with Triton X-100 in the presence of urea, column chromatography on calcium phosphate and ammonium sulfate fractionation, method 2: ammonium acetate fractionation in the presence of deoxycholate, ammonium sulfate fractionation in the presence of urea, and differential centrifugation
-
succinate-ubiquinone reductase obtained from resolution of succinate-cytochrome c reductase using hydroxyapatite and ammonium sulfate fractionation
-
using ammonium sulfate fractionation, solvent extraction and deoxycholate-ammonium sulfate extraction
-
using urea washing, Triton X-100 extraction, cholate-ammonium sulfate extraction, calcium phosphate gel and ammonium sulfate precipitation
-
using solubilization with Triton X-100 and column chromatography on DEAE and Ultrogel ACA
-
from EC 1.3.5.1
-
of both succinate dehydrogenase and fumarate reductase using solubilization with Thesit and DEAE fast-flow chromatography
-
recombinant SQR
-
recombinant SQR, Q-Sepharose, Poros 50HQ, Sephacryl S-300
-
recombinant wild-type and mutant enzymes partially from strain DW35 by membrane preparation
-
succinate-quinone oxidoreductase is solubilized and purified using detergents 2.5% (w/v) sucrose monolaurate and 0.5% (w/v) Lubrol PX
-
using solubilization with polyoxyethylene-9-lauryl ether and column chromatography on DEAE-Sepharose CL-6B
-
using treatment with detergent Thesit and chromatography on DEAE-Sepharose FF column, Poros 50HQ column and Sephacryl S-300 gel filtration column
-
partial, complex II preparation, using Triton X-100 extraction followed by ammonium sulfate precipitation
-
two forms, differing in protein charges
-
comparison of methods
-
from complex II, i.e. EC 1.3.5.1
-
using solubilization with Thesit, column chromatography on HiLoad 26/10 Q-Sepharose and gel filtration on a Sephacryl S-300 column
-
native enzyme from brain mitochondria by anion and cation exchange chromatography followed by heparin affinity chromatography
Q920L2
subunit SdhE (formerly SdhC) expressed in Escherichia coli
Q97W79 and Q97W78 and Q97W77 and Q97W76
native enzyme complex from heart partially by ammonium sulfate fractionation
-
recombinant His6- or His8-tagged enzyme from Thermus thermophilus by nickel affinity chromatography and gel filtration, untagged enzyme by anion exchange chromatography and gel filtration
-
wild-type enzyme by gel filtration to remove Triton X-100, and anion exchange chromatography, followed by hydroxylapatite chromatography, and again anion exchange chromatography and gel filtration
-
partial, complex II preparation, using Triton X-100 extraction followed by ammonium sulfate precipitation
-
a purification procedure is established to enrich the protein 24fold via a combination of anion exchange and gel filtration chromatography with a yield of 36% of the initial activity in the periplasm extract
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
genes sdhC and sdhD, DNA and amino acid sequence determination and analysis, the genes form an operon with the pep1 gene, genetic organization, transcriptional mapping, sdh gene phylogenetic analysis, overview
-
cDNA of iron-sulfur subunit; cloning of the complete cDNAs for the iron-sulfur protein of complex II from anaerobic adult
-
description of succinate dehydrogenase operon
-
site directed mutagenesis at substrate binding site
-
cDNA of iron-sulfur subunit; cloning of the complete cDNAs for the iron-sulfur protein of complex II
-
cell membranes transformed with plasmid which codes for all four subunits of the fumarate reductase complex
-
expressed in Escherichia coli K12 strain
-
expressed in Escherichia coli strain DW35
-
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in strain DW35
-
gene cluster sdhCDAB encoding 4 subunits, DNA and amino acid sequence analysis, overepression
-
overview succinate dehydogenase and fumarate reductase
-
transformed strain DW35 used for expression of membrane-bound enzyme
-
bovine cDNA for the CII-3 subunit of complex II cloned into pUC118, cloning of complete cDNA using sequence information from the bovine clone, mapping of the succinate dehydrogenase C gene
-
cloning of 2 distinct cDNAs of flavoprotein subunit of SQR
-
DNA and amino acid sequence determination of mutated genes SDHB and SDHD from a Chinese family with the familial paraganglioma syndrome, pedigree of the family, overview
-
DNA and amino acid sequence determinatis of wild-type and germline mutants of the genes coding for the enzyme subunits SDHB, SDHC, and SDHD
-
gene SDHB ecoding the subunit B, genotype-phenotype correlations among patients with SDHB mutations in different exons do not reveal obvious differences for age at presentation, biochemical phenotype, primary tumor size and location, distribution of metastatic lesions, or presence of additional head and neck paragangliomas, overview
-
gene SDHB, chromoslomal location at 1p36.13, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes
-
gene SDHD, DNA and amino acid sequence determination and analysis of wild-type and mutant genes
-
gene SDHD, encoding the cybS subunit of the succinate dehydrogenase, mapps to chromosome 11q23, genotyping of native wild-type and mutant genes, overview
-
genes encoding subunits SdhC, SdhD, and SdhB are located at 1q21,11q23, and 1p35-36.1
-
genes SDHB, SDHC, and SDHD, DNA and amino acid sequence determination and analysis, genotyping
-
genes SDHC, SDHD, and SDHB, DNA and amino acid sequence determination and analysis, expression analysis in healthy individuals and in patients with Cowden and Cowden-like syndromes, the latter show PTEN mutations, overview
-
genes SDHD and SDHB, DNA and amino acid sequence determination of healthy individuals and patients with paraganglioma and phaeochromocytomas, several samples, overview; genes SDHD and SDHB, DNA and amino acid sequence determination of healthy individuals and patients with paraganglioma and phaeochromocytomas, several smaples, overview
-
subunit B encoding gene SDHB, DNA and amino acid sequence determination, genotyping, overview; subunit C encoding gene SDHC, DNA and amino acid sequence determination, genotyping, overview; subunit encoding genes SDHA, and SDHD, DNA and amino acid sequence determination, genotyping, overview
-, P21912, Q99643
expressed in Mortierella alpina 1S-4
C4T9C3, -
cloning of the succinate dehydrogenase CDAB operon from KTA4 mutant on plasmid in Escherichia coli
-
description of succinate dehydrogenase operon
-
cloning of the fumarate reductase operon
-
complementation of a commercially available SDH3/SDH4 double knockout mutant yeast strain, subcloning of SDH genes in Escherichia coli strain DH5alpha
-
expression of HA-tagged Sdh1p coupled to the Escherichia coli lacZ reporter gene
-
genes SDHA, SDHB, SDHC, and SDHD
-
targeted gene diruption of iron-sulfur protein
-
cDNA encoding succinate dehydrogenase iron-sulfur protein SDISP, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strains M15 and Y1090
-
expression of subunit SdhE (formerly SdhC) in Escherichia coli
Q97W79 and Q97W78 and Q97W77 and Q97W76
SdhC and the N-terminal domain fragment of SdhB of respiratory complex II are overproduced in Escherichia coli
F9VN10 and Q9C4L8 and F9VN12 and F9VN13, -
recombinant expression of C-terminally His6-tagged or N-termminally His8-tagged enzyme in Thermus thermophilus under the control of a constitutive promoter
-
the encoding plasmid is transformed in Wolinella succinogenes
-
sdhB from mutant H229Y is ligated into a cosmid, pUFR034, to generate pUFR034RAX, which confers resistance to amicarthiazol when transformed into the wild-type sensitive strain; sdhB from mutant H229Y is ligated into a cosmid, pUFR034, to generate pUFR034RAX, which confers resistance to amicarthiazol when transformed into the wild-type sensitive strain
Q6DLZ2, Q6DLZ3
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview
-
both succinate dehydrogenase, SDH, and succinate:ubiquinone oxidoreductase, SQR, activity are markedly and equally downregulated when subunits SDHA and SDHB are targeted, and also when SDHC and SDHD are inhibited
-
Dhh1, a DEAD box protein, is required for the degradation of SDH4 mRNA in iron-deficient conditions. Furthermore, Cth2, an RNA-binding protein responsible for binding to AU-rich elements (ARE), promotes the 5' to 3' degradation of SDH4 mRNA. The final results suggest that Cth2 protein recruits the Dhh1 helicase to promote SDH4 mRNA decay in response to iron-deficiency
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H277R
-
the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
H277Y
-
the molecular basis of boscalid-resistant phenotypes in Alternaria alternata is elucidated. Furthermore, the cross-resistance pattern between boscalid and carboxin in these isolates is investigated. The iron-sulfur subunit of SDHB is targeted for analysis. Sequence comparison of resistant isolates with those of the wild-type isolates show that a single point mutation exist in fungicide-resistant isolates. This mutation leads to a substitution of a highly conserved histidine residue, located in a region associated with the (3Fe-4S) high-potential non-heme iron sulphur-redox (S3) center to either H277Y or H277R
G168D
-
enzyme not assembled, properties of heme bP and heme bD seem normal
H113L
-
enzyme not assembled
H113M
-
assembled enzyme, low enzyme activity, altered properties of heme bD compared to wild-type
H113Y
-
enzyme not assembled, contains heme
H13Y
-
assembles enzyme with about 50% of normal activity, alters properties of heme bP and heme bD compared to wild-type, the isolated enzyme is not stable in the presence of succinate
H155L
-
assembled enzyme, the enzyme has some activity but apparently is unstable
H155Y
-
enzyme not assembled, contains heme
H28L
-
assembles succinate dehydrogenase, active succinate dehydrogenase but inactive succinate: quinone reductase, contains heme bP but lacks low potential heme
H28Y
-
enzyme not assembled, contains heme
H47Y
-
assembles fully active enzyme
H70L
-
enzyme not assembled
H70Y
-
enzyme not assembled
H70Y/Y73S
-
assembled enzyme, enzyme activity is 30% of normal
S214C/Q215G
-
substitution in the IP subunit, mutant is enzymatically impaired and less stable than wild-type
P211F
Q09545
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211H
Q09545
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211L
Q09545
mutant shows the weakest SDH activity, mutant shows a significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate in P211L mutant is increased compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211N
Q09545
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211Q
Q09545
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211R
Q09545
mutant shows significant reduced SDH activity, life span of mutant is not reduced compared to wild-type, embryogenesis is impaired in mutant, in P211R mutant are twice as many dead embryos compared to wild-type (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
C247
-
mutation in flavoprotein subunit FrdA. Increase in fumarate reduction rate, slight increase in succinate oxidation. Residue C247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate
D95E
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
D95L
-
site-directed mutagenesis of subunit C, the mutant shows a shifted pH-optimum but similar activity compared to the wild-type enzyme
E101D
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
E101L
-
site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
E29F
-
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione, the succinate-ubiquinone reductase reaction remains unaffected. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E29L
-
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione, the succinate-ubiquinone reductase reaction remains unaffected. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
F20L
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Phe-20 is not involved in the Q binding
G227L
-
site-directed mutagenesis of subunit B, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
G227L/D95E
-
site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0
G227L/D95L
-
site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0
H232S
-
mutation in flavoprotein subunit FrdA. Decrease in fumarate reduction, strong decrease in succinate oxidation. Residue H232 is the general acid-base catalyst
H30A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, His-30 is not involved in the Q binding
H44C
-
the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 38% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H44R
-
the mutation does not allow cells to grow anaerobically on glycerol and fumarate, the substitution produces an inactive complex
H44S
-
the mutation allows cell growth in glycerol/fumarate medium at a 4fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 32% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H44Y
-
the mutation allows cell growth in glycerol/fumarate medium at a 7fold slower rate than control cells, fumarate reductase activity: the mutant oxidizes reduced benzyl viologen with 17% of the efficiency of wild-type, succinate dehydrogenase activity: the mutant membrane complex is inactive as compared to the wild-type complex
H71C
-
role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Mutant H71C results in a protein that retains penta-coordinated heme b indicating that Cys is not able to provide coordination for the heme in Escherichia coli SQR even in its optimal structural position. Km (ubiquinone): 0.012 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. Mutant H71C retains 43% of ubiquinone reductase activity compared to wild-type SQR, quinone reductase activity is impaired to a greater extent than its succinate-oxidase activity measured with phenazine ethosulfate
H71L
-
mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme
H71Q
-
mutation in SdhC subunit, 82% and 69% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively
H71Y
-
mutant lacks heme. Km (ubiquinone): 0.01 mM compared to 0.0025 mM wild-type, lower ubiquinone or phenazine ethosulfate reductase activity compared to mutant H71C or double mutant H71Y/A72C
H71Y/A72C
-
role of a Cys residue in Escherichia coli SdhD for heme b coordination is examined. H71C mutant is created to mimic the TyrCys motif found in yeast Sdh4p. Double mutant assembles within the membrane but without heme, and it retains the ability to reduce quinone. Km (ubiquinone): 0.013 mM compared to 0.0025 mM wild-type. H71C and Y71C72 mutants show higher phenazine ethosulfate or ubiquinone reductase activities than mutant H71Y. The Y71C72 double mutant shows significant improvement in its activity compared to H71Y or H71C
H84L
-
mutation in SdhC subunit, 54% and 23% of wild-type kcat with succinate-phenazine ethosulfate and succinate, respectively
H91L
-
mutant enzyme produces more superoxide than the wild-type enzyme
I150E
-
mutation lowers the midpoint potential of the [4Fe-4S] cluster
I150H
-
mutation lowers the midpoint potential of the [4Fe-4S] cluster
I28E
-
mutation significantly reduces the succinate-ubiquinone reductase activity of the enzyme, mutant enzyme produces more superoxide than the wild-type enzyme
K228L
-
mutation in subunit FrdB. Residue K228 provides a strong hydrogen bond to menaquinone and is essential for reactions with both menaquinone and ubiquinone
K228R
-
mutation in subunit FrdB. Residue K228 provides a strong hydrogen bond to menaquinone and is essential for reactions with both menaquinone and ubiquinone
L220S
-
mutation does not alter the redox behavior of the [4Fe-4S] cluster but instead lowers the midpoint potential of the [3Fe-4S] cluster
Q78L
-
site-directed mutagenesis of subunit D, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme
R19A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Arg-19 is not involved in the Q binding
R248H
-
mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation
R248L
-
mutation in flavoprotein subunit FrdA. Strong decrease both in fumarate reduction and in succinate oxidation
R31A
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Arg-31 is a critical residue for succinate-Q-reductase
R31H
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity
R31K
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the guanidino group of arginine is critical for succinate-Q reductase activity, it occupies a much larger space than the primary amine of lysine, extends a longer distance, and may provide more chance for hydrogen bond formation, it may stabilize Q binding through pi-pi interactions between the guanidino group and the benzoquinone ring
S27A
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, Ser-27 is a critical residue for succinate-Q-reductase, it participates in a hydrogen bond at the Q-binding site of the C subunit
S27C
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding
S27T
-
the mutation yield cells unable to grow aerobically in M9/succinate medium, the mutant has no activity, the size of the amino acid side chain at position 27 of C subunit is critical for Q binding
S33A
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 35% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase, the mutation of Ser-33 to alanine may greatly reduce enzyme turnover without affecting the affinity for Q
S33C
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 44% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase
S33T
-
the mutant has retarded aerobic growth rate in succinate/M9 medium and it has 88% of the succinate-Q-reducase activity of complement enzyme, the apparent Km value of this mutant for Q2 is about the same as wild-type, the purified mutant protein has azido-Q uptake comparable with that of complement reductase
T17A
-
growth on succinate is essentially the same as the wild-type, electron transfer activity, the apparent Km value for Q2 and the amount of azido-Q incorporated into the succinate dehydrogenase C subunit are comparable with those of the complement reductase, Thr-17 is not involved in the Q binding
T23A
-
the mutation yields cells capable of aerobic growth on M9/succinate medium at a rate slightly slower than that of complement strain, 40% decrease in the specific activity of the mutant to catalyze electron transfer from succinate to Q, apparent Km for Q2 is the same as that of complement reductase, Thr-23 may not be involved in Q binding
A3G
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
C191Y
-
a novel germline missense SDHB mutation (C191Y) in a patient affected by a glomus tumor is reported. The missense mutation hits an amino acid residue conserved from mammals to the yeast Saccharomyces cerevisiae. Histochemistry demonstrates that SDH activity is selectively absent in the patient tumor tissue
D92Y
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
D92Y
-
the naturally occurring mutation of gene SDHD encoding subunit Sdh4p is involved in development of malignant paragangliomas with paraganglioma bone metastases, intrathoracic paraganglioma with lymph node metastases, locally invasive head-and-neck paraganglioma with destruction of the petrosal bone, and locally invasive paraganglioma of the bladder with lymph node metastases, phenotypes, overview
G12S
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
G148D
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H145N
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
H50R
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
L157X
-
the case of a novel SDHB mutation (L157X) in a Japanese patient with abdominal paraganglioma following malignant lung metastasis is reported. Novel mutation is a nonsense mutation, resulting in a truncated protein. In addition, an asymptomatic carrier of the SDHB mutation in this family is identified
R17X
-
naturally occuring mutation in the SDHD gene of a 29-year-old man showing metastases in both lungs and the liver, but no increased hormone production by the tumor, phenotype, overview
R46Q
-
a naturally occuring mutation in gene SDHB in a Japanese family with both abdominal and thoracic paraganglioma following metastasis
R46X
-
naturally ocurring mutations, the recurrent stop-codon mutation in succinate dehydrogenase subunit B gene might play a role in cellular pre-adaptation to hypoxia in normal peripheral blood and childhood T-cell acute leukemia, overview
S163P
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
W43X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
W43X
-
a naturally occurring mutation of the enzyme leads to hypermethylation of the seventh CTCF binding site in the germline and causes paragnaglioma after maternal transmission, study of a three-generation comprising mutation in the germline, phenotype and molecular analysis, overview
W61X
-
an unusual naturally occurring SDHC gene non-sense mutation in a case of laryngeal paraganglioma, phenotype with an additional thyroid papillary carcinoma, overview
Y114X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H243L
C4T9C3, -
an amino-acid substitution of a highly conserved histidine residue within the third cysteine-rich cluster of SdhB replaced by a leucine residue confers carboxin resistance to the organism
B89G
-
succinate dehydrogenase D polypeptide, the mutation conferrs resistance to carboxin but not to thenoyltrifluoroacetone
C184Y
-
SDH2C184Y mutant allele equivalent to human SDHBC191Y does not restore the OXPHOS phenotype of the DELTAsdh2 null mutant. In the C184Y mutant, SDH activity is abolished along with a reduction in respiration. Sensitivity to oxidative stress is increased in the mutant, as revealed by reduced growth in the presence of menadione. The frequency of petite colony formation is increased in the C184Y mutant, indicating an increased mtDNA mutability
C78A
-
mutation in Sdh4 subunit, 94% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
C78A
-
site-directed mutagenesis of the subunit Sdh4p residue an axial ligand of heme binding, leads to highly reduced to undetectable levels of heme b562 compared to the wild-type enzyme
C78A/H106A
-
site-directed mutagenesis of the subunits Sdh3p and Sdh4p, leads to highly reduced to undetectable levels of heme b562 and reduced cell growth compared to the wild-type enzyme
C78H
-
mutation in Sdh4 subunit, 53% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
C85A
-
mutation in Sdh4 subunit, 94% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
D117V
-
reduced covalent FAD content
D88E
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
D88K
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity and FAD content
D88N
-
site-directed mutagenesis of a subunit Sdh4p residue, the mutant shows reduced activity and FAD content, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
F103V
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Phe-103 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase, the enzyme is thermolabile at temperatures above 25C
F69V
-
mutation in anchor subunit Sdh4, 56% of wild-type kcat
H106A
-
mutation in Sdh3 subunit, 78% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H106A
-
site-directed mutagenesis of the subunit Sdh3p residue, an axial ligand of heme binding, leads to highly reduced to undetectable levels of heme b562 compared to the wild-type enzyme
H106L/D117V
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25C
H106Y
-
the covalent FAD level is reduced, indicating some impairment of enzyme assembly, the quinone reductase activity is not greatly impaired, the enzyme is thermolabile at temperatures above 25C
H113A
-
mutation in Sdh3 subunit, 61% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H113Q
-
the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, His-113 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase
H30A
-
mutation in Sdh3 subunit, 97% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H37A
-
mutation in Sdh4 subunit, 100% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H46A
-
mutation in Sdh3 subunit, 45% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H46D
-
mutation in Sdh3 subunit, 47% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H84A
-
mutation in Sdh3 subunit, 97% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H99A
-
mutation in Sdh4 subunit, 75% of wild-type kcat for 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone reduction
H99L
-
reduced covalent FAD content
H99L
-
mutation in anchor subunit Sdh4, 29% of wild-type kcat
K132E
-
mutation in Sdh4 subunit affects heme assembly
K132G
-
mutation in Sdh4 subunit affects heme assembly
K132Q
-
mutation in Sdh4 subunit, reduced heme content
K132V
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mutation in Sdh4 subunit affects heme assembly
P190Q
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mutation in Sdh2 subunit, mutants have reduced succinate-ubiquinone oxidoreductase activity and are hypersensitive to oxygen and paraquat
R47C
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site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity
R47E
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site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity and FAD content
R47K
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site-directed mutagenesis of a subunit Sdh3p residue, the mutant shows reduced activity, as well as accumulation and secretion of succinate, the mutant is sensitive to hyperoxia and paraquate and shows enhanced superoxide production in vivo and in vitro
S71A
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mutation in anchor subunit Sdh4, 43% of wild-type kcat
S94E
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mutation in Sdh4 subunit, mutants have reduced succinate-ubiquinone oxidoreductase activity and are hypersensitive to oxygen and paraquat
W116R
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the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Trp-116 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase
A86H
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FAD is non-covalently attached to SdhA. This is prooved by mutant A86H: in contrast to wild-tpye mutant A86H shows an additional fluorescent band which can be detected after SDS-PAGE
L85X
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naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
additional information
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germline mutations and variants in the succinate dehydrogenase gene SDHD, encoding the subunit D, in Cowden and Cowden-like syndromes, overview, mutations of the SDH genes can cause diverse pathologies, overview
additional information
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splicing defect mutant IVS2+5GA is a naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
additional information
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clinical manifestations of familial paraganglioma and phaeochromocytomas, that may include papillary renal cell carcinoma and macrovascular disease, in succinate dehydrogenase B gene mutation carriers, SDH-B mutation carriers develop disease early and predominantly in extra-adrenal locations, disease penetrance is incomplete, phenoypes, overview
additional information
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clinical and molecular genetics of patients with the Carney-Stratakis syndrome and germline mutations of the genes coding for the succinate dehydrogenase subunits SDHB, SDHC, and SDHD, causing gastrointestinal stromal tumors, phenotypes, overview
additional information
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mutations of genes SDHb and SDHDencoding subunits of SDH are involved in development of carcinoid tumours and bilateral phaeochromocytoma, phenotype, overview
additional information
-, P21912, Q99643
single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, especially mutation c.456+32G>A of gene SDHA showing significant genotype association with impairment of sperm production, overview; single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, overview; single nucleotide polymorphisms in succinate dehydrogenase subunits genes are involved in impaired spermatogenesis, overview
additional information
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germline mutations of the SDHB gene are correlated to an elevated risk of malignant, extradrenal tumor development, overview
additional information
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high frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain, determiunation of sequence variants, overview, mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations, genotype-phenotype correlations, overview
additional information
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inactivation of SDHD by scrambled and SDHD-targeting small interfering RNA short hairpins, Sc and Di3, expression, succinate dehydrogenase-deficient cells show cell-permeating alpha-ketoglutarate derivatives alleviate pseudohypoxia, overview
additional information
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determination of distinct heterozygous SDHB missense DNA mutations, the mutational mechanism targeting SDHB is operational in T-cell acute leukemia, overview
L122stop
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the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25C
additional information
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construction of a gene SDH3 disruption mutant by gene replacement, effects of mutations of the enzyme subunits on the electron transfer activities in mitochondrial membranes of mutant yeast cells compared to the wild-type strain, overview
additional information
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the amount of Sdh1p decreases in an FAD transporter flx1D mutant strain, SDH1 coding sequence and the regulatory sequences located downstream of the SDH1 coding region, as well as protein import and cofactor attachment, seem to be not involved in the decrease in the amount of protein, FLX1 deletion or mutation results in a respiration-deficient phenotype, in which the activities of the mitochondrial FAD dependent-enzymes, lipoamide dehydrogenase and succinate dehydrogenase, are reduced, overview
additional information
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ubiquinone-binding site mutations in the succinate dehydrogenase generate superoxide and lead to the accumulation of succinate
Y89OCH
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substitution with stop codon truncates Sdh4 by removing the third predicted transmembrane segment, 22% of wild-type activity
additional information
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construction of a sdhCAB deletion mutant DELTAsdh
additional information
Staphylococcus aureus HG001, Staphylococcus aureus SA113
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construction of a sdhCAB deletion mutant DELTAsdh
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H229Y
Q6DLZ2, Q6DLZ3
the single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, the mutant is insensitive to the fungicide; the single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, the mutant is insensitive to the fungicide
additional information
Q6DLZ2, Q6DLZ3
several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview; several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview
H229Y
Xanthomonas oryzae pv. oryzae ZJ173
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the single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, the mutant is insensitive to the fungicide; the single amino acid substitution in the SdhB protein of succinate dehydrogenase determines resistance to amicarthiazol, the mutant is insensitive to the fungicide
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additional information
Xanthomonas oryzae pv. oryzae ZJ173
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several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview; several resistant mutant strains, the SDH activity of mutant strain XRUVI is clearly lower than that of wild-type strain ZJ173 in the absence of amicarthiazol, overview
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
reconstitution from partially purified succinate dehydrogenase, cytochrome b and phospholipids, reconstitution by the reversal of chaotrope-induced resolution of complex II
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reconstitution with partially purified components or reversible resolution of complex II by ammonium sulfate treatment or by removal of ClO4- by precipitation as KClO4
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succinate dehydrogenase restores succinate-coenzyme Q reductase activity to alkali-treated complex II particles
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the isolated enzyme is resolved into a reconstitutively active, two-subunit succinate dehydrogenase and a two-subunit membrane anchoring protein fraction by alkaline treatment in the presence of urea followed by DEAE-Sepharose CL-6B column chromatography, maximum reconstitution is obtained when the weight ratio of succinate dehydrogenase to the two-subunit membrane anchoring protein reaches 5.26
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
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the relevance of modifications in Alternaria alternata AaSdhB sequence in conferring boscalid resistance is discussed
molecular biology
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considering the conservation of amino acids crucial for the SQR activity and the high levels of ROS production from the mitochondrial complex II of the Ascaris suum adult worm together with the absence of complexes III and IV activities in its respiratory chain, it is a good model to examine the reactive oxygen species production from the mitochondrial complex II
medicine
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species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics
molecular biology
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the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria. The discovery of this unique molecular marker provides evidence for the monophyly of Euglenozoa that is independent of evolutionary models; the splitting of sdhB in Euglena and trypanosomatids is an example of a unique molecular character that specifically unites these two phylogenetic groups
diagnostics
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succinate dehydrogenase subunits may be candidate susceptibility genes for some phosphatase and tensin homolog (PTEN, tumor suppressor) mutation-negative individuals with Cowden syndrome-like cancers. To address this hypothesis, germline succinate dehydrogenase subunits SDHB-D mutation analysis in 375 PTEN mutation-negative Cowden syndrome /Cowden syndrome -like individuals is performed, followed by functional analysis of identified SDH mutations/variants. Germline SDH mutations/variants occur in a subset of PTEN mutation-negative Cowden syndrome /Cowden syndrome -like individuals and are associated with increased frequencies of breast, thyroid, and renal cancers beyond those conferred by germline PTEN mutations. SDH testing should be considered for germline PTEN mutation-negative Cowden syndrome /Cowden syndrome -like -like individuals, especially in the setting of breast, thyroid, and/or renal cancers
diagnostics
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SDHB mutations are a marker for a prognostic risk of patients with pheochromocytomas or paragangliomas
diagnostics
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mutations of SDH subunit encoding genes are good markers for paraganglioma
medicine
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no DNA methylation is identified in the promoter regions of the succinate dehydrogenase A, B, C, D and fumarate hydratase genes in 72 breast carcinomas and 10 breast cancer cell lines using methylation sensitive high resolution melting which detects both homogeneous and heterogeneous methylation, implying that that inactivation via DNA methylation of the promoter CpG islands of SDH and fumarate hydratase is unlikely to play a major role in sporadic breast carcinomas
medicine
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an SDHB-related pheochromocytoma/paragangliomas patient is presented bearing a SDHB gene mutation with extensive tumor burden, numerous organ lesions, and rapidly growing tumors, which responded extremely well to cyclophosphamide, vincristine, and dacarbazine combination chemotherapy
medicine
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mutations in the genes encoding succinate dehydrogenase are associated with hereditary predisposition to pheochromocytoma and paraganglioma. The results support the notion that loss of mitochondrial function alters epigenetic processes and might provide a signature methylation mark for paraganglioma
biotechnology
C4T9C3, -
a new host-vector system for Mortierella alpina 1S-4, zygomycetes, on the basis of self-cloning for the industrial application of Mortierella transformants is developed. Transformants expressing the Escherichia coli uidA gene encoding beta-glucuronidase by using the mutant H243L as the selectable marker (leading to to carboxin resistance)
medicine
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species-selective inhibition by siccanin is unique among succinate dehydrogenase inhibitors, and thus siccanin is a potential lead compound for new chemotherapeutics
molecular biology
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the splitting of sdhB in Euglena and trypanosomatids is an example of a unique molecular character that specifically unites these two phylogenetic groups
medicine
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the succinate dehydrogenase iron-sulfur protein is a promising candidate for a partially protective vaccination against Schistosoma, SjSDISP vaccine may primarily play a role in anti-embryonation or anti-fecundity immunity
medicine
Schistosoma japonicum Chinese
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the succinate dehydrogenase iron-sulfur protein is a promising candidate for a partially protective vaccination against Schistosoma, SjSDISP vaccine may primarily play a role in anti-embryonation or anti-fecundity immunity
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molecular biology
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the splitting of sdhB in Euglena and trypanosomatids is an example of a unique molecular character that specifically unites these two phylogenetic groups