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Information on EC 1.1.98.4 - F420H2:quinone oxidoreductase
for references in articles please use BRENDA:EC1.1.98.4
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.98 With other, known, physiological acceptors
1.1.98.4 F420H2:quinone oxidoreductase
IUBMB Comments
An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and Archaeoglobus fulgidus.
The expected taxonomic range for this enzyme is: Archaeoglobus fulgidus
- 1.1.98.4
-
heterodisulfide
- methanosarcina
-
methanogen
- methanophenazine
-
methanogenesis
- archaeon
- methane
-
f420h2-dependent
- ferredoxin
- mazei
- 2-hydroxyphenazine
- phenazines
- atmosphere
-
subcomplexes
- viologen
-
methanotrophic
- metronidazole
-
nadh-dependent
- hdrabc
-
greenhouse
-
h2-dependent
-
electron-transporting
- thermophila
- eukarya
- cob-s-s-com
- hydrogenases
showSynonyms
f420h2:quinone oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F420H2 dehydrogenase
F420H2 dehydrogenase
-
part of the energy-conserving F420H2:heterodisulfide oxidoreductase system (EC 1.8.98.1)
F420H2 dehydrogenase
-
part of the energy-conserving F420H2:heterodisulfide oxidoreductase system (EC 1.8.98.1)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a quinol + oxidized coenzyme F420 = a quinone + reduced coenzyme F420
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
quinol:coenzyme-F420 oxidoreductase
An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and Archaeoglobus fulgidus.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,4-naphthoquinone + reduced coenzyme F420
1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
?
2,3-dimethoxy-5-methyl-1,4-benzoquinone + reduced coenzyme F420
2,3-dimethoxy-5-methyl-1,4-benzoquinol + oxidized coenzyme F420
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Substrates: -
Products: -
Products: -
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2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + reduced coenzyme F420
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
?
2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420
2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420
2-hydroxy-1,4-naphthoquinone + reduced coenzyme F420
2-hydroxy-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
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2-methyl-1,4-naphthoquinone + reduced coenzyme F420
2-methyl-1,4-naphthoquinol + oxidized coenzyme F420
oxidized methyl viologen + reduced coenzyme F420
reduced methyl viologen + oxidized coenzyme F420
Substrates: the purified subunit oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole
Products: -
Products: -
?
tetramethyl-4-benzoquinone + reduced coenzyme F420
tetramethyl-1,4-benzoquinol + oxidized coenzyme F420
2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420
2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
?
2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420
2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
?
2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420
2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
?
2-methyl-1,4-naphthoquinone + reduced coenzyme F420
2-methyl-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: i.e. menadione
Products: -
Products: -
?
2-methyl-1,4-naphthoquinone + reduced coenzyme F420
2-methyl-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: i.e. menadione
Products: -
Products: -
?
2-methyl-1,4-naphthoquinone + reduced coenzyme F420
2-methyl-1,4-naphthoquinol + oxidized coenzyme F420
-
Substrates: i.e. menadione
Products: -
Products: -
?
menaquinone + reduced coenzyme F420
menaquinol + oxidized coenzyme F420
Substrates: the FqoF protein forms the input device of the protein complex which oxidizes coenzyme F420H2. Thus, this polypeptide replaces the NADH-oxidizing module of NADH dehydrogenases of bacteria which are not found in Archaeoglobus fulgidus. Then the electrons are channeled to the membrane-associated fragment composed of FqoBCDI, which is homologous to the corresponding module of complex I. As the subunits FqoAHJKLMN are highly hydrophobic and are related to polypeptides comprising the membrane fragment of complex I, they may form the membrane-integral module of the F420H2:quinone oxidoreductase that is responsible for the reduction of a special menaquinone found in the cytoplasmic membrane of Archaeoglobus fulgidus
Products: -
Products: -
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menaquinone + reduced coenzyme F420
menaquinol + oxidized coenzyme F420
-
Substrates: the physiological electron acceptor of the enzyme complex is most likely the menaquinone found in the membrane fraction of Archaeoglobus fulgidus. The reduction of menaquinone by F420H2 in Archaeoglobus fulgidus is catalyzed by a membrane-bound complex composed of at least seven different subunits. It contains 1-2 mol FAD and8 mol Fe-S/mol complex. The complex subunit composition indicates that the F420H2:quinone oxidoreductase complex from Archaeoglobus fulgidus is functionally analogous to the NADH:quinone oxidoreductase complex from mitochondria and bacteria
Products: -
Products: -
?
tetramethyl-4-benzoquinone + reduced coenzyme F420
tetramethyl-1,4-benzoquinol + oxidized coenzyme F420
-
Substrates: i.e. menadione
Products: -
Products: -
?
tetramethyl-4-benzoquinone + reduced coenzyme F420
tetramethyl-1,4-benzoquinol + oxidized coenzyme F420
-
Substrates: i.e. menadione
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NADH and NADPH
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the reduction of heterodisulfide
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrogenase activity. No activity with NAD+ or NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the reduction of heterodisulfide
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrogenase activity. No activity with NAD+ or NADP+
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
menaquinone + reduced coenzyme F420
menaquinol + oxidized coenzyme F420
Substrates: the FqoF protein forms the input device of the protein complex which oxidizes coenzyme F420H2. Thus, this polypeptide replaces the NADH-oxidizing module of NADH dehydrogenases of bacteria which are not found in Archaeoglobus fulgidus. Then the electrons are channeled to the membrane-associated fragment composed of FqoBCDI, which is homologous to the corresponding module of complex I. As the subunits FqoAHJKLMN are highly hydrophobic and are related to polypeptides comprising the membrane fragment of complex I, they may form the membrane-integral module of the F420H2:quinone oxidoreductase that is responsible for the reduction of a special menaquinone found in the cytoplasmic membrane of Archaeoglobus fulgidus
Products: -
Products: -
?
menaquinone + reduced coenzyme F420
menaquinol + oxidized coenzyme F420
-
Substrates: the physiological electron acceptor of the enzyme complex is most likely the menaquinone found in the membrane fraction of Archaeoglobus fulgidus. The reduction of menaquinone by F420H2 in Archaeoglobus fulgidus is catalyzed by a membrane-bound complex composed of at least seven different subunits. It contains 1-2 mol FAD and8 mol Fe-S/mol complex. The complex subunit composition indicates that the F420H2:quinone oxidoreductase complex from Archaeoglobus fulgidus is functionally analogous to the NADH:quinone oxidoreductase complex from mitochondria and bacteria
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the reduction of heterodisulfide
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme is involved in the reduction of heterodisulfide
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
the purified fqoF polypeptide contains 0.7 mol FAD per mol protein
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
Iron-sulfur cluster
-
the purified complex contains 9 mol non-heme iron and 7 mol acid-labile sulfur per mol of complex
Iron-sulfur cluster
the purified fqoF polypeptide contains 10.6 mol non-heme iron and 7.2 mol acid-labile sulfur per mol protein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.21
pH 7, 22°C, crude extract, electron-acceptor system consisting of metronidazole and methyl viologen
136
-
activity with reduced coenzyme F420 as electron donor and 2,3-dimethyl-1,4-naphthoquinone as electron acceptors at pH 8.5 at a temperature of 39°C
17
-
activity with reduced coenzyme F420 as electron donor and methylviologen and metronidazole as electron acceptors at pH 8.5 at a temperature of 39°C
173
-
activity with reduced coenzyme F420 as electron donor and 2-methyl-1,4-naphthoquinone as electron acceptors at pH 8.5 at a temperature of 39°C
68
-
activity with reduced coenzyme F420 as electron donor and tetramethyl-4-benzoquinone as electron acceptors at pH 8.5 at a temperature of 39°C
9.3
pH 7, 22°C, purified enzyme, electron-acceptor system consisting of metronidazole and methyl viologen
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
-
20°C: about 40% of maximal activity, 80°C: about 55% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
FqoF subunit of the F420H2:quinone oxidoreductase
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme is involved in energy conservation during growth on lactate plus sulfate
physiological function
-
the enzyme is involved in the reduction of heterodisulfide
physiological function
the FqoF protein forms the input device of the protein complex which oxidizes coenzyme F420H2. Thus, this polypeptide replaces the NADH-oxidizing module of NADH dehydrogenases of bacteria which are not found in Archaeoglobus fulgidus. Then the electrons are channeled to the membrane-associated fragment composed of FqoBCDI, which is homologous to the corresponding module of complex I. As the subunits FqoAHJKLMN are highly hydrophobic and are related to polypeptides comprising the membrane fragment of complex I, they may form the membrane-integral module of the F420H2:quinone oxidoreductase that is responsible for the reduction of a special menaquinone found in the cytoplasmic membrane of Archaeoglobus fulgidus
physiological function
-
the enzyme is involved in the reduction of heterodisulfide
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). O28443_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
379
0
42687
TrEMBL
Secretory Pathway (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
20000
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
22000
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
32000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
33000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
37000
39000
40000
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
41000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
45000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
56000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
37000
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
37000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
39000
x * 39000 (subunit FqoF), SDS-PAGE. The F420H2:quinone oxidoreductase may be composed of three subcomplexes. The purified subunit FqoF oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole. The subunits FqoB, FqoCD and FqoI may form the membrane-associated module and transfer electrons to the membrane-integral modulemodule. It is most likely that the last subcomplex is composed of FqoA, FqoH, FqoJ, FqoK, FqoL, FqoM and FqoN. All subunits are highly hydrophobic and are probably involved in the reduction of a special menaquinone with a fully reduced isoprenoid side chain present in the cytoplasmic membrane of Archaeoglobus fulgidus
39000
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
oligomer
x * 39000 (subunit FqoF), SDS-PAGE. The F420H2:quinone oxidoreductase may be composed of three subcomplexes. The purified subunit FqoF oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole. The subunits FqoB, FqoCD and FqoI may form the membrane-associated module and transfer electrons to the membrane-integral modulemodule. It is most likely that the last subcomplex is composed of FqoA, FqoH, FqoJ, FqoK, FqoL, FqoM and FqoN. All subunits are highly hydrophobic and are probably involved in the reduction of a special menaquinone with a fully reduced isoprenoid side chain present in the cytoplasmic membrane of Archaeoglobus fulgidus
oligomer
-
x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
oligomer
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
oligomer
-
x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
-
1 h, stable in presence of 1 M (NH4)2SO4, in the presence of 1 M K2HPO (pH 8) only 60% activity is recovered
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is almost stable in aerobic solutions. No activity is lost when 2 mg purified protein in 1 ml 50 mM Tricine/KOH, pH 7.5, containing 0.2% dodecyl-/I-D-maltoside is stored at 4°C for 6 h under air as the gas phase
-
722162
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kunow, J.; Linder, D.; Stetter, K.O.; Thauer, R.K.
F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters
Eur. J. Biochem.
223
503-511
1994
Archaeoglobus fulgidus
brenda
Brueggemann, H.; Falinski, F.; Deppenmeier, U.
Structure of the F420H2:quinone oxidoreductase of Archaeoglobus fulgidus identification and overproduction of the F420H2-oxidizing subunit
Eur. J. Biochem.
267
5810-5814
2000
Archaeoglobus fulgidus (O28443), Archaeoglobus fulgidus
brenda
Abken, H.-J.; Deppenmeier, U.
Purification and properties of an F420H2 dehydrogenase from Methanosarcina mazei G1
FEMS Microbiol. Lett.
154
231-237
1997
Methanosarcina mazei G1, Methanosarcina mazei G1 DSM 3647
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.98.4)
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