Information on EC 1.10.2.2 - quinol-cytochrome-c reductase

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

EC NUMBER
COMMENTARY
1.10.2.2
-
RECOMMENDED NAME
GeneOntology No.
quinol-cytochrome-c reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. depending on the organism and the physiological conditions, either two or four protons are extruded from the cytoplasmic to the non-cytoplasmic compartment (cf.EC1.6.99.3 NADH2 dehydrogenase)
-
-
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
substrate binding site Qo structure, conformational changes upon inhibitor binding, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
2 reaction mechanism variants, a fully active enzyme mechanism and a half-of-the sites mechanism of ubiquinol oxidation, switching between the two variants may regulate the enzyme, Glu272 and His181 are involved
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
binding structure and mode of cytochrome c1 within the enzyme complex and cytochrome c during the catalytic reaction, direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c, half-of-the sites mechanism
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
substrate binding mechanism at the Qo site of the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
the Qo-cycle, overview, reaction mechanism involving cytochrome c, Glu295, and His161, electron transfer mechanism and formation of the ES complex involving a binding square, substrate binding mechanism at the Qo site of the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
alternating half-of-the-sites mechanism of ubiquinol oxidation, enzyme links electron transfer from ubiquinol to cytochrome c by a protonmotive Q cycle mechanism in which ubiquinol is oxidized at one center in the enzyme, referred to as center P, und ubiquinone is re-reduced at a second center, referred to as center N
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
reaction and substrate binding mechanism, overview, conformational changes at the binding site of inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole confirm the proton transfer pathway and reveal plasticity at the active site
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
alternating half-of-sites mechanism of ubiquinol oxidation
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
current competing models for the two-electron oxidation of quinol QH2 at the cytochrome bc1 complex and related complexes impose distinct requirements for the reaction intermediate, the initial and rate-limiting step in quinol oxidation, both in the biological and biomimetic systems, involves electron and proton transfer, probably via a proton-coupled electron-transfer mechanism, a neutral semiquinone intermediate is formed in the biomimetic system, and oxidation of the QH*/QH2 couple for UQH2-0, but not TMQH2-0, exhibits an unusual and unexpected primary deuterium kinetic isotope effect on its Arrhenius activation energy, DELTA GTS, where DELTA GTS for the protiated form is larger than that for the deuterated form, detailed reaction mechanism, molecular modeling, electrochemical and computational study, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
reaction mechanism, kinetic modeling
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
reaction mechanism, similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
aerobic respiration I (cytochrome c)
-
aerobic respiration II (cytochrome c) (yeast)
-
ammonia oxidation IV (autotrophic ammonia oxidizers)
-
Fe(II) oxidation
-
Oxidative phosphorylation
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
quinol:ferricytochrome-c oxidoreductase
The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
b6/f complex
-
-
bc1 complex
-
-
bc1 complex
Neurospora crassa SL 74OR23-1A FGSC No. 987
-
-
-
bc1 complex
Rhodobacter sphaeroides BC17
-
-
-
bc1 complex
-
-
coenzyme Q-cytochrome c reductase
-
-
-
-
coenzyme QH2-cytochrome c reductase
-
-
-
-
complex III
-
-
complex III
-
-
complex III
-
-
complex III
-
-
coQH2-cytochrome c oxidoreductase
-
-
-
-
cyt bc1
P05418
-
cyt bc1
Rhodobacter capsulatus pMTO-404/MTRKB1
-
-
-
Cyt bc1 complex
-
-
Cyt bc1 complex
-
-
Cyt bc1 complex
-
-
Cyt bc1 complex
-
-
cytochrome b-c1 complex
-
-
cytochrome b-c1 complex
Rhodobacter sphaeroides GA, Rhodobacter sphaeroides R-26
-
-
-
cytochrome b-c1 complex
-
-
cytochrome b-c2 complex
-
-
cytochrome b-c2 complex
Rhodobacter sphaeroides GA, Rhodobacter sphaeroides R-26
-
-
-
cytochrome bc1 complex
-
-
cytochrome bc1 complex
-
-
cytochrome bc1 complex
-
-
cytochrome bc1 complex
-
-
cytochrome bc1 complex
-
-
cytochrome bc1 complex
-
-
cytochrome bc1 complex
-
-
cytochrome c reductase
-
-
dihydrocoenzyme Q-cytochrome c reductase
-
-
-
-
f-b6 complex
-
-
hydroubiquinone c2 oxidoreductase
-
-
hydroubiquinone c2 oxidoreductase
Rhodobacter capsulatus pMTO-404/MTRKB1
-
-
-
mitochondrial electron transport complex III
-
-
-
-
plastoquinol-plastocyanin oxidoreductase
-
-
QH2:cyt c oxidoreductase
-
-
QH2:cytochrome c oxidoreductase
-
-
-
-
quinol cyt. c oxidoreductase (bc1)
-
-
quinol-cytochrome c oxidoreductase complex
-
-
quinol:cyt c Oxidoreductase
-
-
quinol:cytochrome c oxidoreductase
-
-
reduced coenzyme Q-cytochrome c reductase
-
-
-
-
reduced ubiquinone-cytochrome c oxidoreductase
-
-
-
-
reduced ubiquinone-cytochrome c reductase, complex III (mitochondrial electron transport)
-
-
-
-
respiratory complex III
-
-
ubihydroquinol:cytochrome c oxidoreductase
-
-
-
-
ubihydroquinone:cytochrome c oxidoreductase
-
-
ubiquinol cytochrome c oxidoreductase
-
-
ubiquinol cytochrome c oxidoreductase
-
-
ubiquinol cytochrome c oxidoreductase
-
-
ubiquinol cytochrome c oxidoreductase
-
-
ubiquinol-cytochrome c oxidoreductase
-
-
-
-
ubiquinol-cytochrome c reductase
-
-
ubiquinol-cytochrome c reductase
-
-
ubiquinol-cytochrome c reductase
-
-
ubiquinol-cytochrome c reductase
-
-
ubiquinol-cytochrome c reductase
-
-
ubiquinol-cytochrome c reductase
Saccharomyces cerevisiae KM91
-
-
-
ubiquinol-cytochrome c reductase complex
-
-
ubiquinol-cytochrome c-2 oxidoreductase
-
-
-
-
ubiquinol-cytochrome c1 oxidoreductase
-
-
-
-
ubiquinol-cytochrome c2 oxidoreductase
-
-
ubiquinol-cytochrome c2 reductase
-
-
-
-
ubiquinol-cytochrome-c oxidoreductase
-
-
ubiquinol-cytochrome-c reductase
-
-
ubiquinol:cytochrome c oxidoreductase
-
-
ubiquinol:cytochrome c oxidoreductase
-
-
ubiquinol:cytochrome c oxidoreductase
-
-
ubiquinol:cytochrome c reductase
-
-
ubiquinol:ferricytochrome c oxidoreductase
-
-
ubiquinone-cytochrome b-c1 oxidoreductase
-
-
-
-
ubiquinone-cytochrome c oxidoreductase
-
-
-
-
ubiquinone-cytochrome c reductase
-
-
-
-
UQH2
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-03-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
formerly Chromatium vinosum
-
-
Manually annotated by BRENDA team
hyperthermophile Knallgasbacterium
-
-
Manually annotated by BRENDA team
thermophilic strain PS3
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas viridis
-
-
Manually annotated by BRENDA team
enzyme is part of the cytochrome bc1 complex
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
Jerusalem artichoke
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
strain SL 74OR23-1A FGSC No. 987
-
-
Manually annotated by BRENDA team
wild-type 74A
-
-
Manually annotated by BRENDA team
Neurospora crassa 74A
wild-type 74A
-
-
Manually annotated by BRENDA team
Neurospora crassa SL 74OR23-1A FGSC No. 987
strain SL 74OR23-1A FGSC No. 987
-
-
Manually annotated by BRENDA team
strain PCC 7906
-
-
Manually annotated by BRENDA team
sheep
-
-
Manually annotated by BRENDA team
Tn5 mutant CFN4205
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas blastica
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas capsulata
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas capsulata; strain SB1003
-
-
Manually annotated by BRENDA team
strain pMTO-404/MTRKB1
-
-
Manually annotated by BRENDA team
strain tyrosine (Y) 147
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus pMTO-404/MTRKB1
strain pMTO-404/MTRKB1
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus SB1003
strain SB1003
-
-
Manually annotated by BRENDA team
basonym Rhodopseudomonas spheroides; formerly Rhodopseudomonas sphaeroides
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas sphaeroides
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas sphaeroides; strain GA
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas sphaeroides; strain GA; strain R-26, blue-green mutant
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas sphaeroides; strain R-26, blue-green mutant
-
-
Manually annotated by BRENDA team
formerly Rhodopseudomonas sphaeroides; wild-type strain NCIB 8253
-
-
Manually annotated by BRENDA team
strain BC17, BH6, CH6
-
-
Manually annotated by BRENDA team
wild-type strain NCIB8253
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides BC17
strain BC17, BH6, CH6
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides R-26
strain R-26, blue-green mutant
-
-
Manually annotated by BRENDA team
Rhodopseudomonas palustris Morita
strain Morita
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum S1
strain S1
-
-
Manually annotated by BRENDA team
ATCC No. 33942
-
-
Manually annotated by BRENDA team
wild-type starin S1, mutant strain SdeltaC2
-
-
Manually annotated by BRENDA team
strain NCYC74, derived from Saccharomyces cerevisiae KL14-4A
-
-
Manually annotated by BRENDA team
Saccharomyces carlsbergensis NCYC74
strain NCYC74, derived from Saccharomyces cerevisiae KL14-4A
-
-
Manually annotated by BRENDA team
bakers'yeast; commercial baker's yeast Red Star, strain D273-10B/A1
-
-
Manually annotated by BRENDA team
parental control diploid strain KM91 obtained by crossing the haploid strain 777-3A with the haploid KL14-4A/60
-
-
Manually annotated by BRENDA team
Red Star cake yeast
-
-
Manually annotated by BRENDA team
strain D 273-10B
-
-
Manually annotated by BRENDA team
strain FL100
-
-
Manually annotated by BRENDA team
strain Rp6, strain KL14-4A
-
-
Manually annotated by BRENDA team
wild-type strain W303-1B
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae D 273-10B
strain D 273-10B
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae DL1
strain DL1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae KM91
strain KM91
-
-
Manually annotated by BRENDA team
Scenedesmus obliquus
-
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
when the only supernumerary subunit (subunit IV) is deleted from the Rhodobaacter sphaeroides wild-type complex, the resulting three-subunit core complex has only a fraction of the electron transfer activity of the wild-type complex but has about four times the superoxide anions generating activity. When the three-subunit core complex is reconstituted with subunit IV, the electron transfer activity increases, and the O2 -.-generating activity decreases to the same level as those in the wild-type, four-subunit complex
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity, which is inactive in bovine cells, but can be activated through detergents treatment
physiological function
P05418
the respiratory cytochrome bc1 complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of protonmotive force which fuels ATP synthesis
physiological function
-
the cytochrome bc1 complex is an essential energy transduction electron transfer complex in photosynthetic bacteria. This complex catalyzes the electron transfer from ubiquinol to cytochrome c (or c2) with concomitant generation of a proton gradient and membrane potential for ATP synthesis by the ATP synthase complex
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
the bc1 complex, is the enzyme in the respiratory chain of mitochondria responsible for the transfer reducing potential from ubiquinol to cytochrome c coupled to the movement of charge against the electrostatic potential across the mitochondrial inner membrane. The complex is also implicated in the generation of reactive oxygen species under certain conditions and is thus a contributor to cellular oxidative stress
physiological function
-
reaction mechanism of superoxide generation by bc1, overview
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
additional information
P05418
structural diversity in the cytochrome c1 surface facing the iron-sulfur protein domain indicates low structural constraints on that surface for formation of a productive electron transfer complex. Modelling of the electron transfer complex with membrane-anchored cytochrome c552, the natural substrate
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
model of the bc1 complex for mammalian mitochondria incorporating the major redox centers near the Qo- and Qi-site of the enzyme, and including the pH-dependent redox reactions, overview. The model consists of six distinct states characterized by the mobile electron distribution in the enzyme
additional information
-
mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme complex from Phaeospirillum molischianum shows a more random organization and slower reaction center turnover compared to the enzyme complex from Rhodobacter sphaeroides
additional information
-
mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme shows a highly organized arrangement of light harvesting and reaction center complexes and fast reaction center electron transfer turnover. Cytochrome bc1 or ATPase complexes are localized in membrane domains distinct from the flat regions. Modeling of subunit IV into the cytochrome bc1 complex
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinol + cytochrome c
2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-decylbenzoquinol + cytochrome c
2,3-dimethoxy-5-methyl-6-decylbenzoquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
show the reaction diagram
-
-
-
-
?
2-[(7E,11E,15E,19E,23E,27E,31E,35E)-4-hydroxy-4,8,12,16,20,24,28,32,36,40-decamethyl-7,11,15,19,23,27,31,35,39-hentetracontanonaen-1-yl]-5,6-dimethoxy-3-methyl-1,4-benzenediol + oxidized cytochrome c
2-[(7E,11E,15E,19E,23E,27E,31E,35E)-4-hydroxy-4,8,12,16,20,24,28,32,36,40-decamethylhentetraconta-7,11,15,19,23,27,31,35,39-nonaen-1-yl]-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione + reduced cytochrome c
show the reaction diagram
-
ubiquinone-like compound with a hydroxyl-substituted side chain exhibits substrate efficiencies below that of native ubiquinone but significantly higher efficiency than alpha-tocopheryl quinone
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
show the reaction diagram
-
-
-
-
?
alpha-tocopheryl hydroquinone + cytochrome c
?
show the reaction diagram
-
-
-
-
?
coenzyme Q1H2 + 2 cytochrome c/ox
coenzyme Q1 + 2 cytochrome c/red + 2 H+
show the reaction diagram
-
-
-
-
?
coenzyme Q1H2 + 2 cytochrome c/ox
coenzyme Q1 + 2 cytochrome c/red + 2 H+
show the reaction diagram
-
-
-
-
?
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
Rhodospirillum rubrum S1
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
Rhodopseudomonas palustris Morita
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
Rhodobacter sphaeroides GA, Rhodobacter sphaeroides R-26
-
-
-
-
-
cytochrome b561 + ?
?
show the reaction diagram
-
cytochrome b561, reduced upon flash excitation, is re-oxidized slowly even in the absence of antimycin
-
-
?
cytochrome c551 + ?
?
show the reaction diagram
-
-
-
-
?
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
show the reaction diagram
-
-
-
-
r
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
show the reaction diagram
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
-
-
?
decylplastoquinol + cytochrome c
decylplastoquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
decylubiquinol + 2 ferricytochrome c
decylubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
show the reaction diagram
-
horse heart cytochrome c, half of the center N sites was insensitive to decylubiquinol
-
-
?
dihydroubiquinone + ferricytochrome c
ubiquinone + ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
?
naphthoquinol + ferricytochrome c
naphthoquinone + ferrocytochrome c
show the reaction diagram
-
-
-, naphthoquinone is the pool quinone of the organism
-
?
nonylubiquinol + cytochrome c
nonylubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
plastohydroquinol + cytochrome c
plastohydroquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
plastoquinol 1 + cytochrome c
plastoquinone 1 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
plastoquinol 9 + cytochrome c
plastoquinone 9 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
r
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
activity is highest near physiological ionic strength and decreases at higher concentrations
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
binding interaction of ubiquinone with cytochrome b, overview
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
rate-limiting is the transfer of the first electron from ubiquinol to the [2Fe-2S] cluster of the Rieske iron-sulfur-protein at the Qo-side, reaction energy profile
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
ubiquinol binds to the specific binding pocket of the cytochrome bc1 complex
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
rhodoquinol-3 + ferricytochrome c
rhodoquinone + ferrocytochrome c
show the reaction diagram
-
a substrate-induced wQ-cycle bypass reaction leading to production of superoxide
i.e. 2-amino-5-farnesyl-3-methoxy-6-methyl-1,4-benzoquinone
-
?
tetramethyl-p-benzoquinol + cytochrome c
tetramethyl-p-benzoquinone + reduced cytochrome c
show the reaction diagram
-
duroquinol
-
-
?
ubideuteroquinol + cytochrome c
ubideuteroquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubihydroquinol + cytochrome c
ubihydroquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricyanide
ubiquinone + 2 ferrocyanide + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
P05418
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
show the reaction diagram
P05418
-
-
-
?
ubiquinol + 4-carboxy-2,6-dinitrophenyllysine27-cytochrome c
ubiquinone + ?
show the reaction diagram
-
cytochrome c from horse, modified at Lys27
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Scenedesmus obliquus
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
algal cytochrome c
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
under physiological conditions, the dimeric cytochrome bc1 complex is suggested to be continually primed by prompt oxidation of membrane ubiquinol via center N yielding a bound semiquinone in this center and a reduced, high-potential heme b in the other monomer of the enzyme. Then the oxidation of each ubiquinol molecule in center P is followed by ubiquinol formation in center N, proton translocation and generation of membrane voltage
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Rhodobacter sphaeroides BC17
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Neurospora crassa SL 74OR23-1A FGSC No. 987
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Rhodobacter capsulatus pMTO-404/MTRKB1
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Rhodospirillum rubrum S1
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Saccharomyces carlsbergensis NCYC74
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Rhodopseudomonas palustris Morita
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Saccharomyces cerevisiae D 273-10B
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Saccharomyces cerevisiae DL1
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Rhodobacter capsulatus SB1003
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Rhodobacter sphaeroides R-26
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
Neurospora crassa 74A
-
-
-
-
?
ubiquinol + cytochrome c
?
show the reaction diagram
-
-
-
-
?
ubiquinol + cytochrome c2
ubiquinone + reduced cytochrome c2
show the reaction diagram
Rhodopseudomonas palustris, Rhodopseudomonas palustris Morita
-
-
-
-
?
ubiquinol + ferricytochrome b-561
ubiquinone + ferrocytochrome b-561
show the reaction diagram
-
-
-
-
?
ubiquinol + ferricytochrome b-562
ubiquinone + ferrocytochrome b-562
show the reaction diagram
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
show the reaction diagram
-
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively
-
-
?
ubiquinol + horse heart cytochrome c
?
show the reaction diagram
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
show the reaction diagram
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
show the reaction diagram
Rhodopseudomonas palustris, Rhodopseudomonas palustris Morita
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
show the reaction diagram
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
show the reaction diagram
Rhodobacter sphaeroides R-26
-
-
-
-
?
ubiquinol + plastocyanin
?
show the reaction diagram
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
show the reaction diagram
-
-
-
-
-
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
show the reaction diagram
-
-
-
-
-
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
show the reaction diagram
Saccharomyces cerevisiae D 273-10B
-
-
-
-
?
ubiquinol 3 + cytochrome c
ubiquinone 3 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 4 + cytochrome c
ubiquinone 4 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
show the reaction diagram
-
-
-
-
-
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
show the reaction diagram
Saccharomyces cerevisiae D 273-10B
-
-
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
show the reaction diagram
-
the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria, substrate of chain length C5 to C10, ubiquinol binds transiently at the Qo site, only when both heme bL and the iron sulfur cluster are in the oxidized form, where it is oxidized
-
-
?
menaquinol + cytochrome c
menaquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
almost inert towards mammalian cytochrome c
-
-
-
additional information
?
-
-
dihydroubiquinone-1 is not a suitable substrate, as it reacts nonenzymically with cytochrome c at a rapid rate
-
-
-
additional information
?
-
-
activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation
-
-
-
additional information
?
-
-
enzyme complex III is part of the mitochondrial membrane electron transport chain
-
-
-
additional information
?
-
-
enzyme is a central component of cellular energy conservation machinery
-
-
-
additional information
?
-
-
enzyme is part of the Knallgas reaction pathway
-
-
-
additional information
?
-
-
the Qo-cycle, overview
-
-
-
additional information
?
-
-
electron transfer takes place between the 2 cytochrome b subunits
-
-
-
additional information
?
-
-
protonation reactions coupled to quinone binding, binding of 2.3-2.6 quinones per enzyme monomer at the Qo side, conformational changes
-
-
-
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
-
additional information
?
-
-
the physiological impact of a mixed Q pool in RQ-producing organisms, overview
-
-
-
additional information
?
-
-
model of half-of-the-sites activity in the dimeric cytochrome bc1 complex, overview
-
-
-
additional information
?
-
-
substrate synthesis and substrate specificity, overview
-
-
-
additional information
?
-
-
the cyt bc1 complex uses ubiquinol, but not plastoquinol, as a substrate, usage of a biomimetic oxidant, excited-state Ru(2,2'-dipyridyl)2(2-(2-pyridyl)benzimidazolate)+ in an aprotic medium to probe the oxidation of the ubiquinol analogue, 2,3-dimethoxy-5-methyl-1,4-benzoquinol, i.e. UQH2-0, and the plastoquinol analogue, trimethyl-1,4-benzoquinol, i.e. TMQH2-0, using time-resolved and steady-state spectroscopic techniques, comparison of isotope-dependent activation properties in the native and synthetic systems as well as analysis of the time-resolved direct-detection electron paramagnetic resonance signals in the synthetic system, overview
-
-
-
additional information
?
-
-
photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production
-
-
-
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
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
Rhodospirillum rubrum S1
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
Rhodopseudomonas palustris Morita
-
-
-
-
-
naphthoquinol + ferricytochrome c
naphthoquinone + ferrocytochrome c
show the reaction diagram
-
-
naphthoquinone is the pool quinone of the organism
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
show the reaction diagram
-
ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
P05418
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
show the reaction diagram
P05418
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
show the reaction diagram
-
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
show the reaction diagram
-
the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria
-
-
?
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
show the reaction diagram
Rhodobacter sphaeroides GA, Rhodobacter sphaeroides R-26
-
-
-
-
-
additional information
?
-
-
activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation
-
-
-
additional information
?
-
-
enzyme complex III is part of the mitochondrial membrane electron transport chain
-
-
-
additional information
?
-
-
enzyme is a central component of cellular energy conservation machinery
-
-
-
additional information
?
-
-
enzyme is part of the Knallgas reaction pathway
-
-
-
additional information
?
-
-
the Qo-cycle, overview
-
-
-
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
-
additional information
?
-
-
the physiological impact of a mixed Q pool in RQ-producing organisms, overview
-
-
-
additional information
?
-
-
photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
bacteriochlorophyll
-
-
cytochrome b
-
-
-
cytochrome b
-
-
-
cytochrome b
-
protoheme
-
cytochrome b
-
-
-
cytochrome b
P05418
two cyt b subunits form the hydrophobic core of the complex, overview
-
cytochrome b
-
the cytochrome b subunit contains two b-type hemes, bL and bH
-
cytochrome b-561
-
-
-
cytochrome b-562
-
-
-
cytochrome b-562
-
-
-
cytochrome b-565
-
-
-
cytochrome c-552
Euglena gracilis, Scenedesmus obliquus
-
-
-
cytochrome c-553
-
-
-
cytochrome c1
-
heme c
cytochrome c1
P05418
the domain houses the cofactor heme c1 which is bound by the characteristic CXXCH motif with residues Cys82, Cys85, His86 (Cys245cyt c1, Cys248cyt c1, His249cyt c1) and with Met210 (Met373cyt c1) as the sixth heme ligand, structure of the subunit, overview
cytochrome c1
-
the cytochrome c1 subunit carries a c-type heme (c1)
heme b
-
prosthetic group
Phospholipid
-
prosthetic group
semiquinone
-
antimycin-sensitive prosthetic group
ubiquinone
-
prosthetic group
Heme c
-
prosthetic group
additional information
-
all the bc1 complexes contain three redox prosthetic group bearing subunits (cytochrome b, cytochrome c1, and Rieske iron-sulfur protein) with varying numbers (ranging from 0 to 8) of non-redox prosthetic group bearing (supernumerary) subunits
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
P05418
Rieske protein, the subunit iron-sulfur protein is made up of three domains. The membrane anchor is an N-terminal TMH (Asp17-Gln41) with pronounced tilt which brings the catalytic domain in contact with the second monomer providing the structural basis for the functional dimer. The catalytic domain is interconnected with the TMH by the hinge region, Met42-Leu51, which harbours the ADV motif, Ala46-Val48
Fe2+
-
Rieske iron-sulfur protein possessing a high potential [2Fe-2S] cluster
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
-
Rieske iron-sulfur protein
Fe2+
-
Rieske ironsulfur protein
Fe2+
-
Rieske iron-sulfur protein
Iron
-
enzyme contains a Rieske [2Fe-2S] cluster
Iron
-
enzyme contains 2 cytochromes with heme groups, enzyme contains a Rieske [2Fe-2S] cluster, structure analysis of the Rieske ISP and of soluble fragments thereof
Iron
-
enzyme complex contains a Rieske Fe-S protein which controls the rate of reduction of the cytochrome b
Iron
-
enzyme complex contains a [2Fe-2S] cluster
Iron
-
enzyme contains a Rieske [2Fe-2S] cluster required for activity
Iron
-
enzyme complex contains an iron-sulfur protein, and heme groups in the cytochrome molecules
Iron
-
enzyme contains a Rieske [2Fe-2S] cluster
Iron
-
contains [2Fe2S] cluster
Iron-sulfur cluster
-
-
Iron-sulfur cluster
-
-
Iron-sulfur cluster
-
-
Iron-sulfur cluster
-
-
Sr2+
-
conserved binding site in photosynthetic bacteria is on cyt c1
Sr2+
-
crystals of Rsbc1 grown in the presence of strontium ions reveal several Sr2+ binding sites. One site that is not present in mitochondrial bc1 but appears to be conserved in photosynthetic bacteria is on cyt c1
Mg2+
-
lowers the substrate binding affinities
additional information
-
no Zn2+ in the native enzyme structure. No Sr2+ binding sites in mitochondrial bc1
additional information
-
no Zn2+ in the native enzyme structure
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,3,4-trimethoxy-5-decyl-6-methyl-phenol
-
competitive inhibitor, binds stably to the Qo site of the cytochrome bc1 complex, binding structure, inhibitory potency depends on the chain length of the ubiquinol substrate and is higher with Q0C5 than with Q0C10, inhibition is pH-dependent
2,3,4-trimethoxy-5-methyl-6-decyl-phenol
-
competitive inhibitor, binds stably to the Qo site of the cytochrome bc1 complex, binding structure, inhibition is pH-dependent
2,5-dibromo-3-methyl-6-isopropylbenzoquinone
-
-
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2-alkyl-3-hydroxy-1,4-naphthoquinone
-
-
2-heptyl-4-hydroxyquinoline N-oxide
-
-
2-Heptyl-4-hydroxyquinoline-N-oxide
-
-
2-Heptyl-4-hydroxyquinoline-N-oxide
-
-
2-Iodo-6-isopropyl-3-methyl-2',2,4'-trinitrodiphenyl ether
-
-
2-nonyl-4-hydroxyquinoline N-oxide
-
binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview
2-nonyl-4-hydroxyquinoline-N-oxide
-
-
3-[(2,4-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(2,6-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(2-bromo-4-fluorophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
-
3-[(2-bromo-4-fluorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-bromophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-chlorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-methoxyphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[3H]azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone
-
azidoQ
3-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
-
4-[[5-(6-bromopyridin-3-yl)-5-methyl-2,4-dioxo-1,3-oxazolidin-3-yl]amino]benzonitrile
-
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzonitrile
-
-
5-(6-bromopyridin-3-yl)-3-[(2,4-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(2,6-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(4-chlorophenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(4-methoxyphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-(phenylamino)-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(2-methyl-4-nitrophenyl)amino]-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(4-methylphenyl)amino]-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
-
5-methyl-3-[(4-methylphenyl)amino]-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
i.e. famoxadone, noncompetitive inhibitor with respect to the substrate of cytochrome c, but is a competitive inhibitor with respect to the substrate of decylubiquinol
-
5-methyl-5-(6-phenoxypyridin-3-yl)-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
-
5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole
-
competitive, structure of the enzyme with the hydroxyquinone anion Qo site inhibitor bound, binding mechanism
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
-
-
5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
-
-
5-Undecyl-6-hydroxy-4,7-dioxobenzothiazole
-
-
Antimycin
-
inhibits ubiquinone reduction at the Qc site of the enzyme
Antimycin
-
highly reduces the rate of cytochrome c1
Antimycin
-
due to half-of-sites mechanism of the enzyme, 1 inhibitor molecule per enzyme complex dimer is sufficient for inhibition, center N inhibitor
Antimycin
-
center N inhibitor, acts at the Qn site of the bc1 complex, binding mode differing from ilicicolin
Antimycin
-
a Qn site inhibitor
Antimycin
-
with one equivalent of antimycin more than 90% of activity is inhibited
Antimycin
-
effective inhibitor
Antimycin
-
with one equivalent of antimycin more than 90% of activity is inhibited
Antimycin
-
-
antimycin A
-
most potent inhibitor
antimycin A
-
inhibits the enzyme complex and blocks the cell differentiation, inhibition mechanism
antimycin A
-
binds to center N sites, irreversible conformational change occurrs upon SQ formation in the active monomer
antimycin A1
-
binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview
antimycin-A
-
strong inhibition of Q-cycle bypass reactions
atovaquone
-
an anti-malarial agent that specifically targets the cytochrome bc1 complex and inhibits parasite respiration in vivo, mutants Y279S, Y279C, and L282V are resistant to the inhibition, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes
azoxystrobin
-
noncompetitive inhibitor with respect to the substrate of cytochrome c, but is a competitive inhibitor with respect to the substrate of decylubiquinol
famoxadone
-
reversible, tight-binding, non-competitive inhibitor, proximal Qo-site inhibitor, binding and inhibition mechanism, overview
funiculosin
-
similar to ilicicolin
funiculosin
-
a Qn site inhibitor
hydroxyapatite
-
-
ilicicolin H
-
center N inhibitor
ilicicolin H
-
center N inhibitor, the antibiotic substance acts at the Qn site of the bc1 complex, isolated from the fungus Cylindrocladium iliciola strain MFC-870, binding mode differing from antimycin, effects on kinetics
ilicicolin H
-
a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM
ilicicolin H
-
weak inhibitor, IC50 is above 100 nM
ilicicolin H
-
weak inhibitor
ilicicolin H
-
potent inhibitor. S20T, Q22E, Q22T and L198F mutations in the yeast bc1 complex conferr resistance to ilicicolin H
menaquinol
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
methoxyacrylate stilbene
-
reversible, tight-binding, mixed-competitive inhibitor, proximal Qo-site inhibitor, binding and inhibition mechanism, overview
methoxyacrylate stilbene
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
methoxyacrylate stilbene
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
methoxyacrylate stilbene
-
-
Myxothiazol
-
inhibits ubiquinone reduction at the Qz site of the enzyme
Myxothiazol
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
N,N'-dicyclohexylcarbodiimide
-
-
n-2-heptyl-1-hydroxyquinoline N-oxide
-
-
n-alkyl-6-hydroxy-4,7-dioxobenzothiazole
-
length of side chain 7-15 carbon atoms
n-heptyl-4-hydroxyquinoline-N-oxide
-
-
Phospholipase A2
-
-
-
Stigmatellin
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
Stigmatellin
-
binding involves conformational change of Glu295, molecular dynamic simulation, mutants E295G, E295D, and E295Q are resistant to inhibition
Stigmatellin
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
Stigmatellin
-
binds to center P sites
Stigmatellin
P05418
species-specific binding of the inhibitor, binding structure and mechanism, overview
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
undecyl-hydroxy-dioxobenzoxythiazole
-
-
undecyl-hydroxy-dioxobenzoxythiazole
-
-
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Ligands are His121, His267, Lys269, and Asp254
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Ligands are His121, His268, Lys270, and Asp253
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Zinc binds five to six N or O atoms
Zn2+
-
crystalline chicken bc1 complex specifically binds Zn2+ ions at two identical sites or one per monomer in the dimer. Zinc binding occurs close to the QP site and is likely to be the reason for the inhibitory effect on the activity of bc1 observable during zinc titration. The Zn2+ ion binds to a hydrophilic area between cytochromes b and c1 and is coordinated by GgH212 of cyt c1, GgH268, GgD253, and GgE255 of cyt b, and might interfere with the egress of protons from the QP site to the intermembrane aqueous medium. No Zn2+ is bound at the zinc binding motif of the putative MPP active site of core-1 and core-2 for chicken bc1 after prolonged soaking
methoxyacrylate-stilbene
-
-
additional information
-
insensitive to N',N'-dicyclohexylcarbodiimide
-
additional information
-
-
-
additional information
-
resistant to classical inhibitors like myxothiazol, stigmatellin and antimycin
-
additional information
-
structure determination of the inhibitor binding site Qi, located near the matrix side of the membrane bilayer
-
additional information
-
the rate of cytochrome c1 is highly reduced in absence of ubiquinone
-
additional information
-
inhibitor binding at the quinone reduction Qi side or the quinol oxidation Qo side
-
additional information
-
inhibition and inhibitor binding mechanisms
-
additional information
-
ubiquinol cannot act as inhibitor
-
additional information
-
design, synthesis, and kinetic evaluation of 3-(phenylamino)oxazolidine-2,4-diones as potent cytochrome bc1 complex inhibitors, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Antimycin
-
stimulation at low inhibitor/enzyme ratio
asolectin
-
stimulates superoxide anion production, overview
-
Dodecyl maltoside
-
-
ilicicolin
-
stimulation at low inhibitor/enzyme ratio
O2
-
molecular oxygen increases the activity of Rhodobacter sphaeroides bc1 complex up to 82%, depending on the intactness of the complex. Since oxygen enhances the reduction rate of heme bL, but shows no effect on the reduction rate of heme bH, the effect of oxygen in the electron transfer sequence of the cytochrome bc1 complex is at the step of heme bL reduction during bifurcated oxidation of ubiquinol. Free superoxide anion is not involved in the oxygen enhanced reduction of heme bL
Sucrose
-
required for full in vitro activity, at 250 mM
Tween 20
-
required for full in vitro activity, at 0.01%
additional information
-
cardiolipin is essential for the function of bc1
-
additional information
-
cardiolipin is essential for the function of bc1. Two phosphatidylethanolamines, one phosphatidylcholine, one phosphatidyinositol, and one cardiolipin are bound to the enzyme cmplex
-
additional information
-
cardiolipin is essential for the function of bc1
-
additional information
-
detergents stimulate superoxide anion production, overview
-
additional information
-
detergents stimulates superoxide anion production, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0046
-
coenzyme Q1H2
-
estimated value of KM, descriptive of rotenone-dicumarol-insensitive CoQ1 reduction and CoQ1H2 oxidation on passage through normoxic lungs
0.004
-
cytochrome c
-
mammalian cytochrome c
0.004
-
cytochrome c
-
patient with cytochrome b mutation
0.0055
-
cytochrome c
-
wild-type protein
0.00714
-
cytochrome c
-
mutant with truncated cytochrome c1
0.009
-
cytochrome c
-
-
0.01
-
cytochrome c
-
solubilized in presence of 0.1% bovine serum albumin
0.013
-
cytochrome c
-
reconstituted into proteoliposomes
0.025
-
cytochrome c
-
-
0.001
-
cytochrome c2
-
-
-
0.023
-
cytochrome c2
-
MgCl2 20 mM
-
0.03
-
cytochrome c2
-
MgCl2 5 mM
-
0.01
-
decylubiquinol
-
pH 8.0, 23C
4.3
-
decylubiquinol
-
pH 8.0, mutant S183A
4.5
-
decylubiquinol
-
pH 8.0, wild-type enzyme
9.2
-
decylubiquinol
-
pH 8.0, mutant Y185F
12.4
-
decylubiquinol
-
pH 8.0, mutant S183T
0.006
-
horse heart cytochrome c
-
-
-
0.008
-
QH2
-
pH 7.0, 23C, mutant I269M
0.013
-
QH2
-
pH 7.0, 23C, wild-type enzyme and mutant F278I
0.072
-
QH2
-
pH 7.2, 25C
0.005
-
rhodoquinol-3
-
pH 8.0, 23C
0.001
-
ubiquinol
-
-
0.0015
-
ubiquinol
-
-
0.02
-
ubiquinol
-
pH 7.4, 25C
0.0064
-
ubiquinol-1
-
-
0.08
-
ubiquinol-1
-
-
0.004
-
ubiquinol-10
-
-
0.006
-
ubiquinol-10
-
-
0.038
-
ubiquinol-10
-
-
0.002
-
ubiquinol-2
-
-
0.0054
-
ubiquinol-2
-
-
0.025
-
horse heart cytochrome c
-
MgCl2 5 mM
-
additional information
-
additional information
-
steady-state kinetics
-
additional information
-
additional information
-
kinetics of the enzyme complex activity dependent on pH and on the Rieske iron-sulfur protein midpoint potential, thermodynamic profile of the Q cycle
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
reaction kinetics of oxidation and electron transfer, complex formation kinetics, pH-dependence
-
additional information
-
additional information
-
pre-steady-state kinetics
-
additional information
-
additional information
-
pre-steady-state and steady-state kinetics, kinetic modeling, kinetics of interactions between monomers of the dimeric enzyme complex, pH 7.0 and pH 8.8
-
additional information
-
additional information
-
pre-steady-state kinetics of cytochrome b reduction
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics, the extent of cyt b reduction in the steady state, measurement of the reduction state of both cyt b hemes during steady state turnover, thermodynamic characterization of ubiquinol-3 and rhodoquinol-3, overview
-
additional information
-
additional information
-
kinetic modeling
-
additional information
-
additional information
-
pre-steady-state reduction of cyt b and cyt c1, steady-state kinetics and Arrhenius activation energies of wild-type and mutant enzymes, overview
-
additional information
-
additional information
-
pre-steady state reduction rate of cytochrome bL in bc1 complex by ubiquinol and effect of oxygen on the kinetics, overview
-
additional information
-
additional information
-
steady-state equation for the six-state system model, substrate binding affinities under different conditions, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
66.7
-
2,3-Dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinol
-
-
7.83
-
cytochrome c
-
-
8.33
11.7
cytochrome c
-
-
10.2
-
cytochrome c
-
reconstituted into proteoliposomes
10.3
-
cytochrome c
-
solubilized in presence of 0.1% bovine serum albumin
13.3
-
cytochrome c
-
-
25
35
cytochrome c
-
-
25
66.7
cytochrome c
-
-
25
-
cytochrome c
-
-
82
-
cytochrome c
-
purified enzyme
165
-
cytochrome c
-
mutant with truncated cytochrome c1, membrane fraction
170
-
cytochrome c
-
wild type, membrane fraction
517
-
cytochrome c
-
mutant with truncated cytochrome c1, purified bc1 complex
919
-
cytochrome c
-
wild type, purified bc1 complex
0.133
-
cytochrome c1
-
-
0.333
-
cytochrome c1
-
-
0.333
-
cytochrome c1
-
-
0.833
-
cytochrome c1
-
-
1.07
1.17
cytochrome c1
-
-
1.25
-
cytochrome c1
-
-
2.13
3
cytochrome c1
-
-
3.33
-
cytochrome c1
-
-
3.67
5.08
cytochrome c1
-
-
3.9
-
cytochrome c1
-
-
66.7
-
cytochrome c1
-
-
65
-
decylubiquinol
-
pH 7.0, wild-type enzyme
143
-
decylubiquinol
-
pH 8.0, 23C
10
-
QH2
-
pH 7.0, 23C, mutant Y279C
15
-
QH2
-
pH 7.0, 23C, mutant L282V
20
-
QH2
-
pH 7.0, 23C, mutant Y279S
30
-
QH2
-
pH 7.0, 23C, mutant I269M
220
-
QH2
-
pH 7.0, 23C, wild-type enzyme and mutant F278I
76
-
rhodoquinol-3
-
pH 8.0, 23C
28.3
-
ubihydroquinone
-
-
140
160
ubiquinol
-
pH 7.0, 22C
4.17
5
horse heart cytochrome c1
-
-
-
additional information
-
additional information
-
rate of direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0068
-
2,3,4-trimethoxy-5-decyl-6-methyl-phenol
-
pH 7.4, 25C
0.0716
-
2,3,4-trimethoxy-5-methyl-6-decyl-phenol
-
pH 7.4, 25C
0.000329
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.00000362
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
noncompetitive versus cytochrome c, pH 7.4, 23C
-
0.00005143
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
competitive versus decylubiquinol, pH 7.4, 23C
-
0.0000025
-
Antimycin
-
pH 7.0, 22C
0.000195
-
famoxadone
-
pH 7.2, 25C
0.0000025
0.00005
ilicicolin H
-
pH 7.0, 22C
0.0000025
0.000005
methoxyacrylate stilbene
-
-
0.0000025
-
methoxyacrylate stilbene
-
pH 7.0, 22C
0.000022
-
methoxyacrylate stilbene
-
pH 7.2, 25C
additional information
-
additional information
-
inhibition mechanism and kinetics
-
additional information
-
additional information
-
inhibitor binding and inhibition kinetics
-
additional information
-
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00001593
-
3-[(2,4-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.001517
-
3-[(2,6-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.001
-
3-[(2-bromo-4-fluorophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.00005998
-
3-[(2-bromo-4-fluorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.001
-
3-[(4-bromophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.00000944
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.000337
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23C
0.001049
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23C
0.00001879
-
3-[(4-chlorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.00005792
-
3-[(4-methoxyphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.00002404
-
3-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
pH 7.4, 23C
0.001
-
4-[[5-(6-bromopyridin-3-yl)-5-methyl-2,4-dioxo-1,3-oxazolidin-3-yl]amino]benzonitrile
-
above, pH 7.4, 23C
0.005312
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
pH 7.4, 23C
0.0002752
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzonitrile
-
pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-3-[(2,4-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-3-[(2,6-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-3-[(4-chlorophenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-3-[(4-methoxyphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-5-methyl-3-(phenylamino)-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(2-methyl-4-nitrophenyl)amino]-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(4-methylphenyl)amino]-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.001
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
above, pH 7.4, 23C
0.00002376
-
5-methyl-3-[(4-methylphenyl)amino]-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.0000482
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23C
-
0.000142
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23C
-
0.00006326
-
5-methyl-5-(6-phenoxypyridin-3-yl)-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23C
0.00004
-
antimycin A
-
-
0.0004347
-
azoxystrobin
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23C
0.000527
-
azoxystrobin
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23C
0.000012
-
ilicicolin H
-
a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM
0.00004
-
Myxothiazol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.29
-
-
mutant with truncated cytochrome c1, membrane fraction
1.35
-
-
wild type, membrane fraction
65
-
-
-
160
-
-
-
308
-
-
mutant with truncated cytochrome c1, purified bc1 complex
469
-
-
wild type, purified bc1 complex
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
8
-
-
2,3-dimethoxy-5-methyl-6-decylbenzoquinol as substrate
8
-
-
cytochrome bc1 complex
additional information
-
-
below 10.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
9.2
-
-
6.5
8
-
activity increases with increasing pH
6.5
9
-
cytochrome bc1 complex
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
room temperature, assay at
22
-
-
assay at room temperature
23
-
-
assay at
25
-
-
assay at
25
-
-
assay at, cytochrome bc1 complex
25
-
-
assay at
additional information
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
temperature dependent activity of complex III in preparations with phospholipids replaced by dimyristoylglycerophosphocholine
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
enzyme expression pattern during cell development
Manually annotated by BRENDA team
-
transgenic embryonic stem cell line with expression of the green fliuorescent protein under control of the alpha-myosin heavy chain promotor, enzyme expression pattern during cell development
Manually annotated by BRENDA team
-
heart muscle
Manually annotated by BRENDA team
-
Keilin-Hartree muscle preparation
Manually annotated by BRENDA team
-
highly expressed in heart, the expression increases in hearts of 4-, 10-, and 28-week-old spontaneously hypertensive rats. UCCR7.2 expression is reduced in the absence of ovarian hormones, but is not directly regulated by estrogen in the heart. UCCR7.2 is a steroid hormone-responsive gene in the heart, with expression increased in cardiac hypertrophy and in response to hypertension
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
inner surface of the chromatophore membrane
-
Manually annotated by BRENDA team
-
inner surface of the chromatophore membrane
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides BC17, Rhodobacter sphaeroides GA
-
-
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides R-26, Rhodopseudomonas palustris Morita
-
inner surface of the chromatophore membrane
-
-
Manually annotated by BRENDA team
-
subunits specified by nuclear genes and sythesized in the cytoplasm
Manually annotated by BRENDA team
-
intracytoplasmic membrane
Manually annotated by BRENDA team
-
cytoplasmic membrane
Manually annotated by BRENDA team
Rhodobacter capsulatus pMTO-404/MTRKB1
-
cytoplasmic membrane
-
Manually annotated by BRENDA team
-
inner membrane
Manually annotated by BRENDA team
-
integral multisubunit membrane protein
Manually annotated by BRENDA team
-
analysis of the localization and orientation of the enzyme complex in the membrane bilayer
Manually annotated by BRENDA team
-
membrane localization and organization of enzyme complex domains, overview
Manually annotated by BRENDA team
Neurospora crassa 74A, Neurospora crassa SL 74OR23-1A FGSC No. 987, Rhodobacter capsulatus pMTO-404/MTRKB1
-
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus SB1003
-
membrane-bound
-
Manually annotated by BRENDA team
Rhodopseudomonas palustris Morita, Rhodospirillum rubrum S1
-
-
-
Manually annotated by BRENDA team
-
mitochondrial membrane, transmembranous subunit QPc-9.5 kDa, more mass on the matrix side of the membrane
Manually annotated by BRENDA team
-
matrix space of mitochondria and intermembrane space
Manually annotated by BRENDA team
-
mitochondrial membrane, transmembranous subunit QPc-9.5 kDa, more mass on the matrix side of the membrane
Manually annotated by BRENDA team
Saccharomyces cerevisiae D 273-10B
-
-
-
-
Manually annotated by BRENDA team
Neurospora crassa SL 74OR23-1A FGSC No. 987, Saccharomyces cerevisiae D 273-10B, Saccharomyces cerevisiae FL100
-
-
-
Manually annotated by BRENDA team
additional information
-
architecture of the intracytoplasmic membrane, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6400
-
-
-
6400
-
-
ISP-associated protein, SDS-PAGE
7200
-
-
-
7200
-
-
cytochrome c1-associated protein, SDS-PAGE
8000
-
-
DCCD-binding protein, SDS-PAGE
8000
-
-
-
8000
-
-
subunit IX, SDS-PAGE
9175
-
-
heme-not containing protein, amino acid sequence
9175
-
-
-
9200
-
-
hinge protein, SDS-PAGE
9500
-
-
-
9500
-
-
subunit ubiquinone-binding protein QPc, SDS-PAGE
9507
-
-
amino acid sequence
12300
-
-
subunit VI, SDS-PAGE
13400
-
-
Q-binding protein, SDS-PAGE
14000
-
-
QP-C, ubiquinone binding protein, amino acid sequence
19000
-
-
FeS-protein, SDS-PAGE
20000
-
-
Rieske iron sulfur protein
21540
-
-
Rieske iron sulfur protein, apoprotein, amino acid sequence
21710
-
-
Rieske iron sulfur protein, holoprotein, including [Fe2-S2] cluster, amino acid sequence
25000
-
-
iron-sulfur protein [Fe2-S2], SDS-PAGE
25000
-
-
iron-sulfur protein [Fe2-S2], SDS-PAGE
26000
-
-
iron-sulfur protein, SDS-PAGE
26000
-
-
gel filtration
27000
-
-
cytochrome b, SDS-PAGE
27900
-
-
cytochrome c1, SDS-PAGE
29000
-
-
cytochrome c1, SDS-PAGE
30000
-
-
cytochrome c, SDS-PAGE
31000
-
-
cytochrome b monomer, SDS-PAGE
31000
-
-
cytochrome c1, SDS-PAGE
31000
-
-
cytochrome c and cytochrome b, SDS-PAGE
32000
-
-
cytochrome b, SDS-PAGE
34100
-
-
His-tagged cyt c1, SDS-PAGE
39000
-
-
cytochrome b
40000
-
-
core II protein
40000
-
-
subunit II, SDS-PAGE
40800
-
-
His-tagged cyt b, SDS-PAGE
42500
-
-
cytochrome b, calculated from amino acid sequence
43700
-
-
cytochrome b, SDS-PAGE
44000
48000
-
core protein, SDS-PAGE
44000
-
-
core protein, SDS-PAGE
44000
-
-
c1 subcomplex, SDS-PAGE
44000
-
-
core protein, SDS-PAGE
47000
-
-
core protein 2, SDS-PAGE
47000
-
-
core II, SDS-PAGE
47000
-
-
core protein I, SDS-PAGE
48000
-
-
cytochrome b, SDS-PAGE
49000
-
-
core I, SDS-PAGE
49200
-
-
core protein I, amino acid sequence
50000
-
-
core protein 1, SDS-PAGE
50240
-
-
core protein, calculated from amino acid composition
60000
68000
-
cytochrome c1
62000
-
-
dimeric cytochrome b
62000
-
-
-
62000
-
-
cytochrome c1
88400
-
-
calculation from subunit composition, assuming stoechiometry of 1:1:1
114000
-
-
calculated from subunit composition
121000
-
-
calculation from cytochrome content
134000
-
-
sedimentation equilibrium
139000
-
-
diffusion coefficient/sedimentation coefficient
200000
-
-
minimum molecular weight, calculated from heme contents
200000
-
-
protein determination
207500
-
-
summation of protein components
216000
-
-
bc1 subcomplex, SDS-PAGE
238000
-
-
estimated from a specific cytochrome c1 content of 4.2 nmol/mg protein
240000
250000
-
from concentration of prosthetic groups
241100
-
-
total mass of protein moiety
242000
-
-
minimum molecular weight calculated from stoichiometry
243300
-
-
complete enzyme monomer, amino acid composition
248000
-
-
bc1 complex, SDS-PAGE
250000
-
-
from subunit composition
250000
-
-
sedimentation velocity
250000
-
-
ultracentrifugation
262000
288000
-
light-scattering measurement
268000
-
-
cytochrome c1 content
285000
-
-
-
285000
-
-
from concentration of prosthetic groups
290000
-
-
from subunit composition
400000
-
-
ultracentrifugation sedimentation velocity
440000
-
-
from hydrodynamic measurements
480000
-
-
-
500000
-
-
analytical ultracentrifugation
550000
-
-
from hydrodynamic measurements
550000
-
-
-
550000
-
-
gel filtration
640000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
dimer
-
each monomeric unit consists of 9 different subunits; subunit I: 50000 Da, subunit II: 45000 Da, Rieske iron-sulfur protein 22000 Da and for subunits from 14000-8000 Da
dimer
-
2 * 270000
dimer
-
each monomeric unit consists of 9 different subunits
dimer
-
enzyme complex
dimer
-
cytochrome bc1 complex, electron transfer complex structure
dimer
-
complex composition, binding structure of cytochromes, crystal structure, overview
dimer
-
2 * 250000, SDS-PAGE
dimer
-
dimeric cytochrome bc1 complex, structure overview
dimer
P05418
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer
dimer
Neurospora crassa 74A
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
-
dimer
Rhodobacter sphaeroides BC17
-
-
-
dodecamer
-
subunits I, II, III, IV, V, VI, VIIA, VIIB, VIII, IX, X and XI
heptamer
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
heptamer
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
heptamer
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
heptamer
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
nonamer
-
-
nonamer
-
9 subunits range in size from 7200-44000 Da
octamer
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
octamer
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
octamer
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination; 1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
octamer
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
octamer
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
octamer
-
composed of 8 different subunits with molecular weights ranging from 11-44 kDa
octamer
-
-
octamer
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
oligomer
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
oligomer
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
oligomer
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
oligomer
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE; 1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
oligomer
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
pentamer
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
tetramer
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
tetramer
-
1 * 40000 + 1 * 34000 + 1 * 24000 + 1 * 14000, SDS-PAGE
tetramer
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
tetramer
Rhodobacter sphaeroides BC17
-
1 * 40100 + 1 * 32600 + 1 * 19000 + 1 * 14000, SDS-PAGE
-
tetramer
Rhodobacter sphaeroides R-26
-
1 * 48000 + 1 * 30000 + 1 * 24000 + 1 * 12000, SDS-PAGE
-
trimer
-
1 * 40000 + 1 * 34000 + 1 * 25000
trimer
-
1 * 62000 + 1 * 39000 + 1 * 20000; 1 * 62000 + 1 * 39000 + 1 * 20000, cytochrome c1, cytochrome b, Rieske-type iron-sulfur protein, SDS-PAGE
trimer
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
trimer
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
trimer
Rhodobacter capsulatus pMTO-404/MTRKB1
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
-
trimer
-
1 * 40000 + 1 * 34000 + 1 * 25000
-
undecamer
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
undecamer
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
undecamer
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
additional information
-
enzyme complex subunit composition and stoichiometry, subunits of 14, 21, 25, 32, 40, and 55 kDa, overview
additional information
-
spectroscopic enzyme complex composition analysis, structural changes upon cofactor or substrate binding, overview
additional information
-
enzyme is part of the mitochondrial cytochrome bc1 complex
additional information
-
interaction analysis between monomers of the dimeric enzyme complex
additional information
-
enzyme complex is a dimer of oligomeric complexes with 11 subunits, composition analysis by mass spectrometry, overview
additional information
-
separation of multienzyme complex III components, mass spectrometral analysis, complex composition, overview
additional information
-
structure modeling and analysis, overview
additional information
-
modeling the variations in cytochrome b structure with the mutated bc1 complexes
additional information
-
secondary structure of yeast cytochrome b and a view of center N, overview
additional information
-
3 catalytic subunits
additional information
-
blue-native PAGE analysis: supercomplex composed of dimeric complex III and two copies of monomeric complex IV, supercomplex composed of dimeric complex III and one copy of monomeric complex IV, dimeric complex III
additional information
-
all the bc1 complexes contain three redox prosthetic group bearing subunits (cytochrome b, cytochrome c1, and Rieske iron-sulfur protein) with varying numbers (ranging from 0 to 8) of non-redox prosthetic group bearing (supernumerary) subunits
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
the Rhodobacter sphaeroides complex contains four protein subunits: three core subunits and one supernumerary subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospholipoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bc1 crystal structure analysis
-
purified cytochrome bc1 complex with bound inhibitors 2,3,4-trimethoxy-5-decyl-6-methyl-phenol or 2,3,4-trimethoxy-5-methyl-6-decyl-phenol, the latter in a 4fold molar excess, 2-4 weeks, X-ray diffraction structure determination and analysis
-
purified native oxidized enzyme complex or enzyme bound to antimycin A1 or 2-nonyl-4-hydroxyquinoline N-oxide, hanging drop vapour diffusion method, 20 mg/ml protein in 50 mM MOPS, pH 7.2, 20 mM ammonium acetate, 20% w/v glycerol, and either 0.1% decanoyl-N-methylglucamide or 0.1% diheptanoyl phosphatidylcholine, or 0.16% sucrose monocaprate, mixed with precipitant solution, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution, modeling
-
bc1 crystal structure analysis
-
multilayer membrane crystals of cytochrome reductase formed by the dialysis method at pH 5.5
-
bc1 crystal structure analysis
-
purified recombinant fully functional complex, hanging drop vapour diffusion method, 20 mg/ml protein in 25 mM sodium phosphate, pH 7.5, 250 mM NaCl and 0.02% beta-ddodecyl-malto-pyranoside is mixed with reservoir solution, containing 100 mM sodium acetate, pH 4.6, 50 mM NaCl, 33% 2-methyl-2,4-pentandiol, in a 1:2 ratio, 18C, 4 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement
P05418
bc1 crystal structure analysis
-
bc1 from Rhodobacter sphaeroides can only be crystallized bound to certain types of inhibitors such as stigmatellin and famoxadone, bc1 crystal structure analysis
-
crystallization of the enzyme cytochrome bc1 complex with mitochondrial cytochrome c and the antibody fragment FV18E11, protein solution with 120 mM ionic strength is rapidly mixed with precipitation solution containing 12% PEG 4000, 20 mM Tris-HCl, pH 7.5, hanging drop vapour diffusion method, 3 weeks at 4C, X-ray diffraction structure determination and analysis, modeling
-
crystallized in the presence of stigmatellin or hexahydrodibenzothiophene, bc1 crystal structure analysis
-
modelling of three-dimensional structure of cytochrome b
-
purified enzyme with inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole bound, microseeding and vapour diffusion method, protein solution contains 50 mg/ml protein, mixing with precipitant solution containing 5% PEG 4000, Tris-HCl, pH 7.5, 0.05% n-undecyl-beta-D-maltopyranoside, 0.01 mM 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole, room temperature, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
bc1 crystal structure analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9.5
-
irreversibly denatured at pH lower than 5.0, stable at neutral pH, at pH 9.5 40% of the enzyme is irreversibly denatured after 19h
5.5
9
-
activity decreases drastically if pH is higher than 9.0 or lower than 5.5
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
half-life about 12 h in 10 mM Tris-acetate, pH 7.8
0
-
-
stable for several hours
37
-
-
stable at lower temperatures, becomes less stable when incubation temperature is raised, half-life time at 37C is 15 min
37
-
-
stable at 37C, progressively decreases at 4C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
slight loss of activity during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% w/v glycerol, spectral properties and reductase activity unaltered after 2 months, but decrease in electron transfer ratio
-
-20C, isolated complex III is stored in presence of 50% glycerol, can be used for functional studies up to a month, for preparation of subunits only freshly prepared bc1 complex, because storage leads to partial degradation of some subunits by proteases
-
-70C, complex III stable to storage and to repeated freeze-thawing
-
-20C, 50% w/v glycerol, spectral properties and reductase activity unaltered after 2 months, but decrease in electron transfer ratio
-
-20C, glycerol, completely stable for 6 months
-
-20C, stored in 50% glycerol
-
-20C, stable in organic solvent
-
-70C, 50 mM Tris-HCl buffer, pH 8.0, 200 mM NaCl, 0.1 mg/ml dodecylmaltoside, 50% glycerol
-
-70C, stable for several weeks
-
-80C, lyophilized in 50% v/v glycerol
-
0C, stable for several hours
-
20C loses 13% of its activity after 1 h
-
4C, 0.003 mM purified enzyme, 0.01% Tween 20, 250 mM sucrose, 1 week, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme complex from membranes, recombinant membraneous and soluble [2Fe-2S] proteins from Escherichia coli to homogeneity
-
cytochrome c1
-
fully oxidized enzyme complex to homogeneity
-
separation of multienzyme complex III components from heart mitochondria
-
to homogeneity from heart mitochondria
-
ubiquinone-binding protein QPc-9.5 kDa
-
separation of multienzyme complex III components from heart mitochondria
-
cytochrome b polypeptide
-
differential centrifugation
-
purification of cytochrome c1, and the Rieske ISP with soluble fragments
-
purification of the active enzyme complex III from mitochondria
-
active enzyme to homogeneity
-
isolation of mitochondria, solubilizatioin of membranes, sucrose gradient ultracentrifugation
-
Rieske-type iron-sulfur protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of the Rieske [2Fe-2S] cluster from gene petA in Escherichia coli as full length membraneous protein or as truncated soluble protein, phylogenetic analysis of Rieske ISPs, genes petA and petB
-
cDNA encoding the Rieske iron-sulfur protein QPc-9.5 kDa isolated and sequenced
-
complete sequence of bovine mitochondrial DNA in a clone library in multicopy plasmid vectors
-
operon encoding the bc1 complex cloned and sequenced, operon disrupted by transposon insertion
-
cloning of human mitochondrial genes, comparison with bovine mitochondrial genes
-
cDNA encoding subunit I of the cytochrome reductase cloned and sequenced
-
genes encoding the four subunits of the bf complex cloned and sequenced
-
DNA sequence of the Rieske ISP determined
-
expressed in Paracoccus denitrificans
-
operon encoding the bc1 complex cloned and sequenced
-
recombinant expression of cyt bc1DELTAac complex fused with a C-terminal deca-histidine-tag at cyt b
P05418
DNA sequence of the Rieske ISP determined
-
fbc operon cloned and sequenced
-
nucleotide sequence of the pet operon determined
-
strain pMTO-404/MTRKB1 constructed by deletion of the chromosomal copy of the pet operon from green strain MT1131 and genetic complementation with a plasmid pMTO-404 containing the operon and a tetracycline resistance gene
-
structural genes petA for the Rieske FeS protein, petB for cytochrome b and petC for cytochrome c1 cloned by complementation, using a mutant defective in this complex
-
fbcB and fbcC genes cloned using PCR amplification
-
gene fbcF cloned and expressed in Escherichia coli
-
petABC operon encoding the subunits of the cytochrome bc1 complex sequenced, petB gene cloned
-
DNA sequence of the Rieske ISP determined
-
all of the genes for the subunits of the yeast including QCR6, the nuclear gene encoding subunit 6 have been cloned and sequenced
-
CBP3 gene cloned by transformation of a mutant from complementation group G28 with a yeast genomic library
-
cloning and mapping of the yeast nuclear genes for the core II and Rieske iron-sulphur protein, reintroduced into yeast cells on multi-copy plasmids
-
cloning of the COR1 gene for 44 kDa core subunit
-
cloning of the structural gene for the 40-kDa subunit II in pEMBL and M13 vectors and DNA sequence analysis
-
cytochrome b gene, DNA sequence determination of wild-type and mutant strains
-
expressed in Saccharomyces cerevisiae
-
genes encoding all of the subunits cloned and sequenced
-
nuclear genes coding for the 17000 kDa, 14000 kDa and 11000 kDa subunits isolated from a clone bank of yeast nuclear DNA
-
segment of the iron-sulfur protein gene from Neurospora crassa used to detect the yeast gene by Southern analysis, yeast gene, which contains no introns, expressed in Escherichia coli
-
DNA sequence of the Rieske ISP determined
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E295D
-
site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type
E295G
-
site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type
E295Q
-
site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type
Y156W
-
site-directed mutagenesis, mutant enzyme shows altered pH-dependence compared to the wild-type enzyme
E272Q
-
mutation in cytochrome b, elimination of the proton acceptor in cytochrome b, decreased rate of quinol oxidation
F278I
-
site-directed mutagenesis, the mutation does not affect the residues of the EF helix of cytochrome b, the mutant shows similar ubiquinol-binding as the wild-type complex
G37D
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows normal growth
G37S
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows impaired growth
I269M
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex
L198F
-
site-directed mutagenesis, the mutation is located on exon 4, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows normal growth
L198F
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
Q22E
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth
Q22E
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
Q22T
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth
Q22T
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
S183A
-
site-directed mutagenesis, kinetic parameters compared to the wild-type enzyme
S183T
-
site-directed mutagenesis, kinetic parameters compared to the wild-type enzyme
S20L
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows impaired growth
S20T
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth
S20T
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
Y185F
-
iron-sulfur protein mutant, pre-steady-state and steady-state kinetic analysis in comparison to the wild-type enzyme
Y185F
-
site-directed mutagenesis, kinetic parameters compared to the wild-type enzyme
Y185F
-
mutation in the Rieske protein, decreased redox potential of the FeS cluster, decreased rate of quinol oxidation
Y185F/E272Q
-
mutation (185) in the Rieske protein, mutation (272) in cytochrome b, decreased rate of quinol oxidation
Y279C
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone
Y279S
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone
additional information
-
a functional cyt bc1 complex with a truncated cyt c1: the coding region of the fbcC gene between triplet 39 and 202, specifying the complete highly acidic domain of the Paracoccus denitrificans cyt c1, is deleted in frame (removing nucleotides 2279 to 2766)
additional information
P05418
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer
H111N
-
site-directed mutagenesis, the rate of heme bL reduction in the H111N mutant complex increases in the presence of oxygen, no altered effect of superoxide dismutase on the oxygen increased rate of heme bL reduction in the H111N mutant complex compaired to the wild-type enzyme, overview
additional information
-
when the only supernumerary subunit (subunit IV) is deleted from the Rhodobaacter sphaeroides wild-type complex, the resulting three-subunit core complex has only a fraction of the electron transfer activity of the wild-type complex but has about four times the superoxide anions generating activity. When the three-subunit core complex is reconstituted with subunit IV, the electron transfer activity increases, and the O2 -.-generating activity decreases to the same level as those in the wild-type, four-subunit complex
L282V
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone
additional information
-
cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes, overview
additional information
-
construction of several mutants, some of which are resistant to center N site enzyme inhibitors, such as ilicicolin H or antimycin, genomic structure of mutants, effects of the cytochrome b mutations on respiratory growth and cross-resistance to other Qn site inhibitors, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
reconstitution
-
reconstitution of the solubilized membrane-protein complex in phospholipid vesicles
-
reconstitution
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
test of respiratory-chain dysfunction in human mitochondrial myopathies
medicine
-
complex III deficiency in the muscle mitochondria
medicine
-
peripheral arterial disease
additional information
P05418
the complex from the alpha-proteobacterium Paracoccus denitrificans is a model for the medically relevant mitochondrial complexes