1.12.1.2: hydrogen dehydrogenase
This is an abbreviated version!
For detailed information about hydrogen dehydrogenase, go to the full flat file.
Word Map on EC 1.12.1.2
-
1.12.1.2
-
alcaligenes
-
eutrophus
-
hydrogenases
-
ralstonia
-
hydrogen-oxidizing
-
h2-dependent
-
lithoautotrophic
-
thiocapsa
-
roseopersicina
-
h2-oxidizing
-
oxygen-tolerant
-
synthesis
- 1.12.1.2
- alcaligenes
- eutrophus
- hydrogenases
-
ralstonia
-
hydrogen-oxidizing
-
h2-dependent
-
lithoautotrophic
-
thiocapsa
- roseopersicina
-
h2-oxidizing
-
oxygen-tolerant
- synthesis
Reaction
Synonyms
bidirectional hydrogenase, bidirectional Ni-Fe hydrogenase, bidirectional NiFe-hydrogenase, bidirectional [NiFe] hydrogenase, dehydrogenase, hydrogen, FeHyd, H2:NAD+ oxidoreductase, H2ase, Hox, Hox hydrogenase, Hox type hydrogenase, HoxE, HoxEFUYH, HoxF, HoxFUYHI2, HoxH, HoxS, HoxU, HoxY, hydrogen-evolving enzyme, hydrogenase, Hyn, iron-hydrogenase, NAD+-reducing hydrogenase, NAD+-reducing NiFe hydrogenase, NAD+-reducing [NiFe]-hydrogenase, NAD-dependent hydrogenase, NAD-reducing hydrogenase, NADH-dependent Fe-only hydrogenase, NiFe hydrogenase, NiFe-type reversible hydrogenase, SH, soluble hydrogenase, soluble [NiFe]-hydrogenase, [FeFe] hydrogenase, [FeFe]-hydrogenase, [NiFe] H2ase, [NiFe] hydrogenase, [NiFe]-hydrogenase
ECTree
1.12.1.2 hydrogen dehydrogenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.12.1.2 - hydrogen dehydrogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ferrocyanide + NAD(P)H
ferricyanide + NAD(P)+
-
enzyme complex including HoxI
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
NADH + oxidized 2,6-dichlorophenol indophenol
NAD+ + reduced 2,6-dichlorophenol indophenol
NADH + oxidized benzyl viologen
NAD+ + reduced benzyl viologen
-
-
-
-
r
NADH + reduced 3-acetylpyridine adenine dinucleotide
NAD+ + oxidized 3-acetylpyridine adenine dinucleotide
NADPH + K3Fe(CN)6
?
-
low reaction with hexameric enzyme form, no reaction with tetrameric enzyme form
-
-
?
oxidized 2,6-dichlorophenol indophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
oxidized cytochrome c + NAD(P)H
reduced cytchrome c + NAD(P)+
-
-
-
?
oxidized methylene blue + H2
reduced methylene blue + H+
-
1058% activity compared to NAD+
-
-
r
oxidized methylene blue + NAD(P)H
reduced methylene blue + NAD(P)+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
ferrocyanide + NAD+
ferricyanide + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
r
H+ + NADH
H2 + NAD+
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H+ + NADH
H2 + NAD+
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the enzyme simultaneously uses electrons from NADH and reduced ferredoxin to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the enzyme simultaneously uses electrons from NADH and reduced ferredoxin to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
bifurcating [FeFe]-hydrogenase in Syntrophobacter fumaroxidans simultaneously uses electrons from NADH and reduced ferredoxin in a 1:2 ratio to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
bifurcating [FeFe]-hydrogenase in Syntrophobacter fumaroxidans simultaneously uses electrons from NADH and reduced ferredoxin in a 1:2 ratio to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically in a 1:1 ratio for catalysis of H2 production
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically in a 1:1 ratio for catalysis of H2 production
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H2
H+ + e-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
hydrogenase reaction part
-
-
r
H2 + acceptor
H+ + reduced acceptor
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
1257% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
585% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
1257% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
389% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
708% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
708% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
708% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
r
H2 + ferricyanide
H+ + ferrocyanide
-
350% activity compared to electron acceptor NAD+
-
?
H2 + NAD+
H+ + NADH
-
electron transfer between the catalytic site for NADH-oxidation and the hydrogenase catalytic site is rate-limiting
-
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptors: Janus green, 2,6-dichlorophenolindophenol, phenazine methosulfate, menaquinone, ubiquinone, cytochrome c
-
r
H2 + NAD+
H+ + NADH
-
hydrogenase produces superoxide free radical anions, which are responsible for enzyme inactivation
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
r
H2 + NAD+
H+ + NADH
-
enzyme also has diaphorase and NAD(P)H oxidase activity
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor ferricyanide
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
r
H2 + NAD+
H+ + NADH
-
utilization of H2 as energy source during autotrophic growth on hydrogen and CO2
-
r
H2 + NAD+
H+ + NADH
-
utilization of H2 as energy source during autotrophic growth on hydrogen and CO2
-
r
H2 + NAD+
H+ + NADH
-
enzyme provides reducing equivalents for CO2 fixation
-
-
r
H2 + NAD+
H+ + NADH
-
the enzyme catalyzes electron transfer from molecular hydrogen to NAD+, thereby producing reducing equivalents for CO2 fixation in the form of NADH
-
-
?
H2 + NAD+
H+ + NADH
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H2 + NAD+
H+ + NADH
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
utilization of H2 as energy source during autotrophic growth on hydrogen and CO2
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
electron acceptor FMN
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
electron acceptor FAD
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
artificial electron acceptors: Janus green, 2,6-dichlorophenolindophenol, phenazine methosulfate, menaquinone, ubiquinone, cytochrome c
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
hydrogenase produces superoxide free radical anions, which are responsible for enzyme inactivation
-
?
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
no activity with NADP+
-
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
key enzyme in H2 metabolism
-
-
r
H2 + NAD+
H+ + NADH
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
overall reaction
-
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor resazurin
-
?
H2 + NAD+
H+ + NADH
-
physiological function of the enzyme in Frankia strains, overview
-
-
r
H2 + NAD+
H+ + NADH
H2 producing activity is not dependent on NAD+ reduction
-
-
r
H2 + NAD+
H+ + NADH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + NAD+
H+ + NADH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + NAD+
H+ + NADH
Hydrogenomonas sp.
-
electron acceptor FAD, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
Hydrogenomonas sp.
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
Hydrogenomonas sp.
-
electron acceptor FMN, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
electron acceptor FAD, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
electron acceptor FMN, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
enzyme delivers hydrogen-driven reducing power for methane oxidation
-
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor ferricyanide
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
r
H2 + NAD+
H+ + NADH
in vivo H2 evolution under nitrogenase-repressed conditions
-
-
r
H2 + NADP+
H+ + NADPH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + NADP+
H+ + NADPH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
hydrogenase activity
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
50fold higher specific activity compared to NAD+ reduction
-
r
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
the artificial electron donor is accepted by the cells for H2 production when added to the culture medium
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
best cofactor
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
r
H2 + oxidized methyl viologen
reduced methyl viologen + H+
-
-
-
-
r
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
NADH + oxidized 2,6-dichlorophenol indophenol
NAD+ + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenol indophenol
NAD+ + reduced 2,6-dichlorophenol indophenol
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
NADH + reduced 3-acetylpyridine adenine dinucleotide
NAD+ + oxidized 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADH + reduced 3-acetylpyridine adenine dinucleotide
NAD+ + oxidized 3-acetylpyridine adenine dinucleotide
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
oxidized 2,6-dichlorophenol indophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized 2,6-dichlorophenol indophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
-
-
?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
-
-
?
oxidized methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
-
r
oxidized methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
-
r
additional information
?
-
-
at high H2 partial pressure enzyme activity is reduced and fermentation is partially shifted to ethanol production
-
-
?
additional information
?
-
-
enzyme autoxidation
-
-
?
additional information
?
-
-
activity is equally high in atmosperes of 20% O2, 20% N2, or 100% H2, the latter being slightly preferred
-
-
?
additional information
?
-
-
enzyme regulation involves a regulatory hydrogenase RH which acts as a sensor for H2 content, interaction via signal cascade
-
-
?
additional information
?
-
-
the organism can grow on H2 as sole energy source in an oxic environment
-
-
?
additional information
?
-
-
addition of NADH prolonged the lag phase before H2 consumption
-
-
?
additional information
?
-
-
deuterium-hydrogen proton exchange activity of wild-type and mutantenzymes, overview
-
-
?
additional information
?
-
-
enzyme shows both hydrogenase and diaphorase activities, proton channeling
-
-
?
additional information
?
-
-
FMN release induces reduction with NADH, enzyme shows both hydrogenase and diaphorase activities, proton channeling
-
-
?
additional information
?
-
-
tetrameric or hexameric enzyme form: no H2 production from NADPH
-
-
?
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
?
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
?
additional information
?
-
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
?
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
?
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the organism can grow on H2 as sole energy source in an oxic environment
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
tetrameric or hexameric enzyme form: no H2 production from NADPH
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
enzyme shows both hydrogenase and diaphorase activities, proton channeling
-
-
?
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
?
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
?
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
?
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
?
additional information
?
-
-
physiological role of the hydrogenase seems to be equally associated with both formation and uptake of H2, depending on the redox state of the intracellular medium
-
-
?
additional information
?
-
-
physiological role of the hydrogenase seems to be equally associated with both formation and uptake of H2, depending on the redox state of the intracellular medium
-
-
?
additional information
?
-
-
flavodoxin and ferredoxin directly reduce the enzyme in vitro
-
-
?
