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Information on EC 1.12.1.2 - hydrogen dehydrogenase
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1.12.1.2 hydrogen dehydrogenaseIUBMB Comments
An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme contain nickel.
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Word Map
- 1.12.1.2
- alcaligenes
- hydrogenases
- eutrophus
-
ralstonia
-
hydrogen-oxidizing
-
lithoautotrophic
- roseopersicina
-
thiocapsa
-
h2-dependent
-
h2-oxidizing
-
oxygen-tolerant
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
bidirectional hydrogenase, bidirectional Ni-Fe hydrogenase, bidirectional NiFe-hydrogenase, bidirectional [NiFe] hydrogenase, dehydrogenase, hydrogen, FeHyd, H2:NAD+ oxidoreductase, H2ase, Hox, Hox hydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FeHyd
H2ase
Hox
Hox hydrogenase
Hox type hydrogenase
HoxE
HoxEFUYH
HoxF
HoxFUYHI2
HoxH
HoxS
HoxU
HoxY
Hyn
iron-hydrogenase
NAD+-reducing [NiFe]-hydrogenase
NAD-dependent hydrogenase
SH
soluble [NiFe]-hydrogenase
[FeFe] hydrogenase
[FeFe]-hydrogenase
[NiFe] hydrogenase
[NiFe]-hydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2 + NAD+ = H+ + NADH
catalytic activity may be regulated by the reduction of a regulatory center followed by a series of structural changes
-
H2 + NAD+ = H+ + NADH
catalytic activity may be regulated by the reduction of a regulatory center followed by a series of structural changes
-
H2 + NAD+ = H+ + NADH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:NAD+ oxidoreductase
An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme contain nickel.
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CAS REGISTRY NUMBER
COMMENTARY
37256-54-5
deleted
9027-05-8
-
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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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
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 + 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
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
-
key enzyme in H2 metabolism
-
-
r
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
-
enzyme delivers hydrogen-driven reducing power for methane oxidation
-
-
r
H2 + NAD+
H+ + NADH
in vivo H2 evolution under nitrogenase-repressed conditions
-
-
r
additional information
?
-
-
at high H2 partial pressure enzyme activity is reduced and fermentation is partially shifted to ethanol production
-
-
?
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
?
-
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
?
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4Fe-4S-center
presence of a 4Fe-4S-center in addition to the active site iron
Ferredoxin
-
the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically for catalysis of H2 production
-
[2Fe-2S]-center
HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters
[4Fe-4S]-center
HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters
flavin
-
only when FMN or riboflavin are added in combination with Mg2+ or Ni2+, NAD-reducing system is activated
FMN
-
2 molecules per enzyme molecule, one of 2 can be reversibly released upon reduction of the enzyme
FMN
-
required, 2 molecules per tetrameric enzyme complex, reduced enzyme reversibly releases half of the FMN bound, kinetics, FMN release induces reduction with NADH, overview
FMN
-
required, enzyme contains 1 mol FMN per mol of enzyme
FMN
module HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters
NADH
-
the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically for catalysis of H2 production
additional information
-
benzyl viologen, methyl viologen or methylene blue can replace NAD+/NADH
-
additional information
-
methyl viologen or benzyl viologen can replace NAD+/NADH
-
additional information
methyl viologen or dithionite can act as electron donor/acceptor
-
additional information
-
methyl viologen, oxidized and reduced can replace NAD+/NADH
-
additional information
-
Ni-Fe cofactor, analysis of the non-standard structure of the Ni-Fe cofactor bound at the active site, interaction mechanism with H2, structural changes during reaction, reduction, and inactivation, the cofactor structure is (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO), overview
-
additional information
-
no activity with NADPH/NADP+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CN-
CO
Co2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
cyanide
-
enzyme contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
Fe
Fe2+
Iron
Mg2+
Mn2+
Ni
Ni2+
Nickel
additional information
CN-
-
enzyme contains four cyanides in its active site, one is bound to the Ni2+, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, the CN- bound to the nickel ion can be irreversibly removed inducing enzyme inhibition by oxygen
CN-
-
enzyme contains four cyanides in its active site, the Ni2+ bound one is responsible for the insensitivity towards oxygen, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, the CN- bound to the nickel ion can be irreversibly removed inducing enzyme inhibition by oxygen
CO
-
bound to the active site, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
CO
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Fe
-
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO)
Fe
-
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover
Fe
-
the (CO)3Fe(II) site is octahedral. An octahedral iron and a distorted square pyramidal nickel are linked by three bridging ligands
Fe2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Iron
-
enzyme contains multiple iron-sulfur clusters, [4Fe-4S] or [2Fe-2S]
Iron
-
11.5 iron atoms per enzyme molecule, enzyme contains 2 [4Fe-4S] and 2 [2Fe-2S] clusters
Iron
-
the diaphorase contains 3 [2Fe-2S] cluster, the hydrogenase subunit HoxY contains one [2Fe-2S] cluster coordinated by 9 Cys residues
Iron
the active site iron atom has a standard ligation, i.e., one CO and two cyanide ligands
Iron
-
the enzyme contains at least one [4Fe4S]+ and at least one [2Fe2S]+ cluster
Iron
-
[NiFe] hydrogenases carry a metal centre composed of Fe and Ni atoms at the active site
Iron
-
[NiFe]-hydrogenase, the ratio of iron to nickel is 13 gatom Fe/1 gatom Ni. The absorption spectrum is typical of iron-sulfur proteins having [4Fe-4S] clusters
Mg2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
Mg2+
-
NAD-reduction: no linear kinetics in absence of metals, 0.5 mM Ni2+ and 5 mM Mg2+ required
Mn2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+, or of high salt concentrations of 500-1500 mM
Ni
-
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO). The unusual ligation of the Ni by only two thiols plus further (C,O) ligands seems to be a prerequisite of the exceptionally rapid activation of the SH by NADH, involving the loss of an oxygen ligand from the Ni. Evidence for the binding of hydrogen to the open coordination site at Ni has been obtained. The hydrogen cleavage reaction seems not to involve a Ni-C state (Ni(III)-H-). The CN ligand at the Ni may be involved in establishing both rapid activation and oxygen-insensitive catalytic behavior in the SH. Possibly, one important function of the CN is stabilization of the Ni(II) oxidation state throughout the catalytic cycle of hydrogen cleavage
Ni
-
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover
Ni2+
-
below 0.06 mol Ni2+ per mol of enzyme
Ni2+
-
nickel is essential for the catalytic activity of the enzyme
Ni2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Ni2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, H2 activation solely takes place on Ni2+
Ni2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
Ni2+
-
NAD-reduction: no linear kinetics in absence of metals, 0.5 mM Ni2+ and 5 mM Mg2+ required
Ni2+
-
take-up/release of substrates may occur at the Ni site. Flexible coordination structures at Ni may be responsible for the interconversion between H2 and (2H+) as the unique function of the [NiFe] hydrogenase. The coordination mode of the Ni(II) center can vary from square planar, to distorted square pyramidal, and to octahedral geometries, dependent on the nature of the ligands. An octahedral iron and a distorted square pyramidal nickel are linked by three bridging ligands
Nickel
-
[NiFe] hydrogenases carry a metal centre composed of Fe and Ni atoms at the active site
Nickel
-
[NiFe]-hydrogenase, the ratio of iron to nickel is 13 gatom Fe/1 gatom Ni
additional information
-
no increase of activity by addition of Co2+, Mn2+, Ni2+ or Fe2+
additional information
-
stimulation of activity by salt is greater the less chaotrophic the anion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
-
chemical modification of active site His residues results in reduced enzymatic hydrogenase and diaphorase activities, pH-dependence and kinetics of modifications/inactivation
DTNB
-
modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation
iodoacetic acid
-
modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation
Ni2+
-
0.5-1 mM, strong inhibition of artificial electron acceptor reduction
O2
-
irreversible enzyme inhibition by oxygen occurs if the CN- bound to Ni2+ is irreversibly removed or if the enzyme is reduced by NADH
O2
incubation of subunits HoxHY with O2 at high potentials causes slow inactivation, but activity is recovered within seconds at potentials below -170 mV at 30°C, even in the presence of 2% O2; incubation of subunits HoxHY with O2 at high potentials causes slow inactivation, but activity is recovered within seconds at potentials below -170 mV at 30°C, even in the presence of 2% O2
p-chloromercuribenzoate
-
0.02 mM, complete inhibition, reversed by addition of glutathione
additional information
-
release of one FMN reduces the NAD+ reduction by 90%, but is reversible by addition of excess FMN, insensitivity towards oxygen, with all 4 CN- groups bound to the enzyme, and towards CO
-
additional information
-
when light adapted cells are transferred to darkness the expression of hoxE and hoxF is only slightly affected, while the transcript levels of hoxU, hoxY and hoxH are significantly (3-5fold) decreased. Putative regulators of hox gene expression sll0359 is suppressed in dark to a similar extent as hoxU, hoxY and hoxH. The transcriptional regulator lexA shows the opposite expression pattern than that of the hox genes, since it decreases in the light. When cells in microaerobic conditions are transferred to darkness the transcript levels of hoxU, hoxY, hoxH transcripts slightly decrease
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HypC
-
[NiFe] hydrogenase maturation protein HypC catalyzes the insertion and cyanation of the iron center of [NiFe] hydogenase
-
HypD
-
[NiFe] hydrogenase maturation protein HypD catalyzes the insertion and cyanation of the iron center of [NiFe] hydogenase
-
HypE
-
[NiFe] hydrogenase maturation protein HypE catalyzes the insertion and cyanation of the iron center of [NiFe] hydogenase
-
LexA protein
-
the transcription factor LexA contributes to enzyme expression
-
Na2S2O4
-
1 mM, activity of initially inactive enzyme increases within 1 h to a stable level in the presence of 101 kPa H2
Sll0359 protein
-
the AbrB-like protein Sll0359 interacts specifically with the hox promoter region and works as an activator of hox gene expression
-
[NiFe] hydrogenase maturation protein
-
maturation of the [NiFe] hydrogenase involves assembly of nonproteinaceous ligands on the large subunit by accessory proteins encoded by the hyp operon, HypE is an essential accessory protein and participates in the synthesis of two cyano groups found in the large subunit
-
FMN
H2 oxidation by subunits HoxHY is enhanced on addition of excess FMN
NADH
-
activates hexameric enzyme form, no activation of the tetrameric enzyme form
NADPH
-
specific activation of the soluble oligomeric enzyme, the binding domain is located on subunit HoxI
NADPH
-
activates hexameric enzyme form. Subunit HoxI provides a binding domain for NADPH
additional information
-
at a redox potential of approx. -100 mV the inactive form of the enzyme is transformed into an active one
-
additional information
-
putative regulators of hox gene expression sll0359 is induced in light to a similar extent as hoxU, hoxY and hoxH. The transcriptional regulator lexA shows the opposite expression pattern than that of the hox genes, since it is induced in darkness by up to 3fold. When cells in microaerobic conditions are transferred to darkness the transcript levels of hoxE and hoxF are further increased
-
additional information
-
the hydrogenase maturation protein HypE catalyzes the synthesis of the CN ligand of the active-site iron of the [NiFe] hydrogenase using carbamoyl phosphate and ATP as substrates (HypE dehydrates the S-carbamoyl moiety by an ATP-dependent reaction to produce HypE-thiocyanate)
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00025
reduced ferredoxin
-
pH and temperature not specified in the publication
0.197
NAD+
pH 8.0, temperature not specified in the publication
0.056
NADH
pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
NADPH
-
pH 8.0, wild-type enzyme complex including HoxI, with ferrocyanide
2
ferrocyanide
-
pH 8.0, wild-type enzyme complex including HoxI, with NADPH
222
ferrocyanide
-
pH 8.0, wild-type enzyme complex including HoxI, with NADH
372
ferrocyanide
-
pH 8.0, wild-type enzyme complex including HoxI, with H2
70
H2
-
pH 8.0, HoxI deletion mutant enzyme, with oxidized benzyl viologen
120
H2
-
pH 8.0, wild-type enzyme complex including HoxI, with oxidized benzyl viologen
372
H2
-
pH 8.0, wild-type enzyme complex including HoxI, with ferrocyanide
222
NADH
-
pH 8.0, wild-type enzyme complex including HoxI, with ferrocyanide
70
Oxidized benzyl viologen
-
pH 8.0, HoxI deletion mutant enzyme, with H2
120
Oxidized benzyl viologen
-
pH 8.0, wild-type enzyme complex including HoxI, with H2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
NAD+
pH 8.0, temperature not specified in the publication
0.2
NADH
pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0006
0.0017
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor oxidized methyl viologen
0.0018
cell culture in nitrogen-limited medium, anaerobic conditions, H2 production using reduced methyl viologen as electron donor
0.0029
-
soluble periplasmic fraction, hydrogen producing activity with electron donor NADH
0.006
-
soluble periplasmic fraction, hydrogen producing activity with electron donor reduced benzyl viologen
0.0095
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor oxidized benzyl viologen
0.0113
-
soluble periplasmic fraction, hydrogen producing activity with electron donor reduced methyl viologen
0.0175
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor oxidized methylene blue
0.0255
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor NAD+
0.035
-
H2 producing activity, strain R43 grown without nitrogen and nickel, from host plant Compotonia cunninghamiana, with reduced methyl viologen as electron donor
0.11
-
H2 producing activity, strain UGL011101 grown without nitrogen and nickel, from host plant Alnus incana, with reduced methyl viologen as electron donor
0.3
-
H2 producing activity, strain HFPCcI3 grown without nitrogen and nickel, from host plant Compotonia cunninghamiana, with reduced methyl viologen as electron donor
0.6
102.1
-
reaction with H2 and ferrocyanide, purified HoxI deletion mutant enzyme
108.8
-
reaction with H2 and ferrocyanide, purified wild-type enzyme complex including HoxI
1300
-
purified enzyme, with substrates oxidized benzyl viologen and NADH
15
native purified enzyme complex from strain PCC 6301, hydrogen-forming activity, cofactor reduced methyl viologen
1700
-
purified enzyme, both reaction directions with substrates oxidized/reduced methyl viologen and H2/H+
230
-
recombinant protein, pH 8.0, temperature not specified in the publication
25.2
-
reaction with H2 and benzyl viologen, purified HoxI deletion mutant enzyme
30 - 100
-
purified enzyme, forward reaction under aerobic conditions with NAD+
35.1
-
reaction with H2 and benzyl viologen, purified wild-type enzyme complex including HoxI
4.91
-
H2 producing activity, strain UGL140102 grown without nitrogen and nickel, from host plant Hippophae rhamnoides, with reduced methyl viologen as electron donor
41.9
-
reaction with H2 and NAD+, purified wild-type enzyme complex including HoxI
430
-
pH 6.0, 40°C, measured by hydrogen uptake with methyl viologen as electron acceptor
61.6
-
reaction with NADH and ferrocyanide, purified HoxI deletion mutant enzyme
64.9
-
reaction with NADH and ferrocyanide, purified wild-type enzyme complex including HoxI
67
native purified enzyme complex from strain PCC 6803, hydrogen-forming activity, cofactor reduced methyl viologen
87.78
-
after 1155old purification, pH and temperature not specified in the publication
additional information
0.0006
cell culture in nitrogen-enriched medium, anaerobic conditions, H2 production using reduced methyl viologen as electron donor
0.0006
-
soluble periplasmic fraction, hydrogen producing activity with electron donor reduced methylene blue
0.6
-
H2-evolution in vivo, fermenter-grown cells
0.6
-
reaction with NADPH and ferrocyanide, purified wild-type enzyme complex including HoxI, no reaction with the HoxI deletion mutant
additional information
-
no H2 producing activity in several strains grown without nitrogen and nickel, overview
additional information
-
hydrogen-driven methane monooxygenase activity in the soluble periplasmic fraction, overview
additional information
determination of H2 production rates in vivo
additional information
-
determination of H2 production rates in vivo
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 8
-
electron acceptor NAD+, in triethanolamine/HCl buffer containing NiCl2
7.9
8.5
9
-
evolution of H2 in the presence of methyl viologen or benzyl viologen
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 9.1
Hydrogenomonas sp.
-
Tris-HCl buffer and potassium phosphate buffer pH 6.9: 20% activity, Tris-HCl buffer pH 9.1: 40% activity, potassium phosphate buffer pH 9.1: 65% activity
7 - 9.5
-
triethanolamine buffer, Tris buffer pH 7.0: 40-45% activity, triethanolamine buffer, Tris buffer pH 9.5: 60-75% activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27
70
70
-
evolution of H2 in the presence of methyl viologen or benzyl viologen
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
isolates of nine different actinorhizal host plants, 18 strains, overview
-
-
brenda
-
439692, 439695, 439697, 439698, 439699, 439700, 439704, 439705, 439706, 439708, 439711, 439712, 654562, 655890, 656298, 672067, 672279, 673177, 674165, 674924, 675493, 724156, 725748, 726344
-
-
brenda
facultative lithoautotrophic proteobacterium, formerly Alcaligenes eutrophus
-
-
brenda
formerly Alcaligenes eutrophus
439692, 439694, 439695, 439696, 439697, 439698, 439699, 439700, 439704, 439705, 439706, 439707, 439708, 439709, 439710
-
-
brenda
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities
-
-
brenda
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
facultative lithoautotrophic proteobacterium, formerly Alcaligenes eutrophus
-
-
brenda
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities
-
-
brenda
hoxF, alpha-subunit; LLR02022, nitrogen-fixing actinomycete, no activity in strain KB5
SwissProt
brenda
hoxH, beta-subunit; LLR02022, nitrogen-fixing actinomycete, no activity in strain KB5
SwissProt
brenda
hoxU, gamma-subunit; LLR02022, nitrogen-fixing actinomycete, no activity in strain KB5
SwissProt
brenda
hoxY, delta-subunit; LLR02022, nitrogen-fixing actinomycete, no activity in strain KB5
SwissProt
brenda
HoxE subunit from strain PCC 6301; strain PCC 6803, and strain PCC 6301 which is identical with Anacystis nidulans SAUG 1402-1
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
activity is high in cells grown at low H2 partial pressure
brenda
additional information
-
cells are grown heterotrophically in a fructose-glycerol minimal medium
brenda
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
cells are grown heterotrophically in a fructose-glycerol minimal medium
brenda
additional information
-
propionate-grown cell, fumarate-grown cell
brenda
additional information
-
propionate-grown cell, fumarate-grown cell
brenda
additional information
-
propionate-grown cell, fumarate-grown cell
brenda
additional information
-
propionate-grown cell, fumarate-grown cell
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
located as inclusion bodies in the DNA region of the cell
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme contributes to electron transport regulation when both photosynthetic and respiratory pathways are down-regulated
Show AA Sequence and Transmembrane Helices (1038 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
-
1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
18000
x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE
20000
-
1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
21000
x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE
26000
27000
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
30000
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
31000
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
375000
native dimeric assembly of the pentameric enzyme complex, gel filtration
56000
63000
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
64000
65000
-
1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
26000
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
56000
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
56000
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
64000
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
64000
-
1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
oligomer
tetramer
additional information
?
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
?
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
?
x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE
hexamer
-
subunit stoichiometry of HoxFUYI2. Subunit HoxIhas a MW of 19000 Da as determined by SDS-PAGE
hexamer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
subunit stoichiometry of HoxFUYI2. Subunit HoxIhas a MW of 19000 Da as determined by SDS-PAGE
oligomer
-
enzyme is composed as a dimer of pentamers, the latter consisting of subunit pairs HoxU with HoxF, and HoxY with HoxH, and a fifth 19 kDa subunit HoxI, i.e. B protein, the HoxFU dimer is the NADH-dehydrogenase moiety, the HoxHY dimer is the hydrogenase moiety, overview
oligomer
-
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity
oligomer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
enzyme is composed as a dimer of pentamers, the latter consisting of subunit pairs HoxU with HoxF, and HoxY with HoxH, and a fifth 19 kDa subunit HoxI, i.e. B protein, the HoxFU dimer is the NADH-dehydrogenase moiety, the HoxHY dimer is the hydrogenase moiety, overview
oligomer
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity
tetramer
-
1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
tetramer
-
enzyme is composed of 4 Hox subunits, HoxF, HoxH, HoxU, and HoxY, with MWs of 67 kDa, 55 kDa, 26 kDa, and 23 kDa
tetramer
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
tetramer
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
additional information
-
structure analysis and subunit composition, HoxI is associated with the NADH-dehydrogenase moiety of the enzyme
additional information
-
subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase or diaphorase activity
additional information
-
use of a reverse micelle system for study of oligomeric structure
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
structure analysis and subunit composition, HoxI is associated with the NADH-dehydrogenase moiety of the enzyme
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
use of a reverse micelle system for study of oligomeric structure
additional information
-
large dimer composed of 64000 Da and 31000 Da subunit contains 1 FMN, 1 [2Fe-2S] and 2 [4Fe-4S] cluster, diaphorase activity is located on large dimer, small dimer composed of 56000 Da and 27000 Da subunits contains 2 Ni and 1 [4Fe-4S]/[3Fe-xS] cluster, hydrogenase activity is localized on small dimer
additional information
-
in low-salt buffer the tetrameric enzyme dissociates into 2 dimeric forms accompanied by the failure to reduce NAD+
additional information
-
large dimer composed of 64000 Da and 31000 Da subunit contains 1 FMN, 1 [2Fe-2S] and 2 [4Fe-4S] cluster, diaphorase activity is located on large dimer, small dimer composed of 56000 Da and 27000 Da subunits contains 2 Ni and 1 [4Fe-4S]/[3Fe-xS] cluster, hydrogenase activity is localized on small dimer
additional information
-
in low-salt buffer the tetrameric enzyme dissociates into 2 dimeric forms accompanied by the failure to reduce NAD+
additional information
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH in cyanobacteria, the complex forms dimer (HoxEFUYH)2, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY, complex composition analysis, overview
additional information
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH of the cyanobacterial-type, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY
additional information
-
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH of the cyanobacterial-type, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
six accessory proteins HypA-F (hydrogenase pleiotropic proteins) and one protease (HoxW) are necessary for post-translational processing of the bidirectional [NiFe] hydrogenase
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, using sodium citrate and imidazole
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C461A
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
D456N
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
D456S
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
E14Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
E14V
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
G15A
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
H16L
H396L
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
H396Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 3.5fold reduced activity compared to the wild-type strain
H69Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
H69Q/P390A
-
site-directed mutagenesis, catalytic subunit HoxH alleles, reduced activity compared to the wild-type strain
I64A
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
L118A
-
site-directed mutagenesis, catalytic subunit HoxH allele, reduced activity compared to the wild-type strain
L118F
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow at O2 concentrations above 5%, about 4fold reduced activity compared to the wild-type strain
L118I
-
site-directed mutagenesis, catalytic subunit HoxH allele, reduced activity compared to the wild-type strain
L394A
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
L394N
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
P390A
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
R12L
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
R12Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
R391L
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
R391Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
R60Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
S68V
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
T415S
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
T415V
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
T415V/N415H
-
site-directed mutagenesis, catalytic subunit HoxH alleles, O2-sensitive growth, highly reduced activity compared to the wild-type strain
I64M
-
the mutation alters gas diffusion kinetics and improves O2 tolerance
I64M/L107M
-
the mutant shows strongly reduced activity compared to the wild type enzyme
I64M/L107M/L112M
-
the mutant shows strongly reduced activity compared to the wild type enzyme
I64M/L112M
-
the mutant shows strongly reduced activity compared to the wild type enzyme
L107M/L112M
-
the mutant shows reduced activity compared to the wild type enzyme
L112F
-
the mutant shows strongly reduced activity compared to the wild type enzyme
L112M
-
the mutant shows slightly reduced activity compared to the wild type enzyme
additional information
H16L
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
H16L
-
in the HoxH-mutant protein H16L, H2 oxidation is impaired, but H2 production occurrs via a stable Ni-C state (N(III)-(H-)-Fe(II))
additional information
-
construction of a HoxI deletion mutant enzyme, which shows different activation behaviour than the wild-type, it is not activated by and does not react with NADPH
additional information
-
construction of an inactive null mutant strain, mutant strain growth characteristics, overview
additional information
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
construction of a HoxI deletion mutant enzyme, which shows different activation behaviour than the wild-type, it is not activated by and does not react with NADPH
additional information
in-frame deletion of HoxE, deletion of HoxH
additional information
-
in-frame deletion of HoxE, deletion of HoxH
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
1 day: 9% loss of activity in the presence of 0.5 mM NiCl2 + 5 mM MgCl2, 56% loss of activity in the absence of NiCl2 and MgCl2, 3 days: 44% loss of activity in the presence of 0.5 mM NiCl2 + 5 mM MgCl2, 80% loss of activity in the absence of NiCl2 and MgCl2
439702
6.2 - 7
-
stability of the enzyme complex including HoxI in potassium phosphate buffer at pH 6.2 and pH 7.0, not at pH 8.0 or in Tris-HCl buffer at pH 7.2 and pH 8.0, or in Tris-nitrate buffer at pH 7.4
655890
7
-
1 day: no loss of activity in the presence of 0.5 mM NiCl2 + 5 mM MgCl2, 62% loss of activity in the absence of NiCl2 and MgCl2, 3 days: 21% loss of activity in the presence of 0.5 mM NiCl2 + 5 mM MgCl2, 87% loss of activity in the absence of NiCl2 and MgCl2
439702
8
-
1 day: no loss of activity in the presence of 0.5 mM NiCl2 + 5 mM MgCl2, 86% loss of activity in the absence of NiCl2 and MgCl2, 3 days: 27% loss of activity in the presence of 0.5 mM NiCl2 + 5 mM MgCl2, complete loss of activity in the absence of NiCl2 and MgCl2
439702
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
enzyme prepared in Tris or triethanolamine buffer: 90% loss of activity after 10 min, enzyme prepared in K-phosphate buffer: 30% loss of activity after 10 min
50
-
thermoinactivation by dissociation of the native enzyme tetramer into constituent heterodimers
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly diluted enzyme preparations are significantly inactivated even at 20°C
-
oxidized inactive form of the enzyme is the most stable against thermodenaturation, proteolysis, and inactivation in urea
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
air the presence of NADH leads to rapid destruction of the hexameric enzyme
-
674924
insensitivity towards oxygen, irreversible enzyme inhibition by oxygen occurs if the CN- bound to Ni2+ is irreversibly removed or if the enzyme is reduced by NADH
-
656298
oxidation with O2 and ferricyanide in absence of reducing components stabilizes, simultaneous presence of H2, NADH and O2 causes irreversible inactivation, half-lives in H2/O2 mixtures: 5% O2, 60 min, 20% O2, 30 min, 50% O2, 12 min
-
439708
oxidized hydrogenase purified under aerobic conditions is highly stable but not reactive, reductive activation of the enzyme by H2 in the presence of catalytic amounts of NADH or by reducing agents destabilizes
-
439699
rapid and irreversible inactivation under aerobic conditiones in the presence of reductants e.g. 1-10 mM NADH
-
439704
redox-dependent inactivation and activation, proposed inactivation mechanism
-
439704, 439705
the hexameric SH preparation is both active and stable in the presence of NADPH and air
-
674924
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 4 mg/ml protein concentration, pH 7.0
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein. The as-isolated module HoxHY is initially catalytically inactive, but after reductive activation at low potentials, exhibits both H2 oxidation and H+ reduction
recombinant Strep-tagged HoxI-deletion mutant tetramer from Escherichia coli by 2 different procedures
-
sp. H16, cetavlon, ammonium sulfate, DEAE-cellulose, Sephadex G-200, hydroxyapatite
-
under anaerobic conditions, pentameric bidirectional hydrogenase complex HoxEFUYH to near homogeneity 647fold from strain PCC 6803 and 1290fold from strain PCC 6301, recombinant His-tagged HoxE from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, HoxE is encoded in a cluster of 5 genes encoding the enzyme complex subunits, sigma54-type promotor with probably inducible expression of the operon
gene cluster HoxFUYHI, cloning and expression of the Strep-tagged HoxI-deletion mutant, a tetramer composed of HoxFU and HoxHY dimers forming a tetramer in Escherichia coli strains JM109 and XL-1 Blue
-
over-expression of a plasmid carrying the hoxFUYWI-hypA2B2F2CDEXA genes in Cupriavidus necator
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
coupling of enzyme reaction to carbonyl reductase from Candida parapsilosis leads to total turnover numbers up to 143666 with maximum activity for NAD+ reduction at 35°C and pH 8.0. Half-life of enzyme is 5.3 h under these conditions. Presence of ammonium and potassium ions increases the enzyme stability
synthesis
-
immobilization of enzyme onto the anionic resin AmberliteTMFPA54 with immobilisation yield of 93.4% for adsorptive and 100% forcovalent attachment, corresponding activities of 48.9 and 39.3%, respectively, leading to stabilisation of enzyme. At elevated temperature and under agitation, stabilisation is further increased by modification of the covalently bound SH with methoxy-poly(ethylene) glycol(mPEG). In stationary aqueous solution, half-lives of up to 161 h at 25°C and 32 h at 35°C are obtained.In presence of the DMSO, DMF, 2-propanol and [EMIM][EtSO4] half-lives of 14-29 h can be achieved
synthesis
-
system for cloning and expression of multiple genes in Escherichia coli BL21 demonstrate tby production and maturation of the NAD+reducing soluble [NiFe]-hydrogenase from Cupriavidus necator H16. The enzyme encoded in hoxFUYHI is successfully matured by co-expression of a dedicated set of auxiliary genes, comprising seven hyp genes (hypC1D1E1A2B2F2X) along with hoxW, which encodes a specific endopeptidase. Deletion of genes involved in enzyme maturation reduces maturation efficiency substantially. Further addition of hoxN1, encoding a high-affinity nickel permease, considerably increases maturation efficiency in Escherichia coli
synthesis
-
coupling of enzyme reaction to carbonyl reductase from Candida parapsilosis leads to total turnover numbers up to 143666 with maximum activity for NAD+ reduction at 35°C and pH 8.0. Half-life of enzyme is 5.3 h under these conditions. Presence of ammonium and potassium ions increases the enzyme stability
synthesis
-
immobilization of enzyme onto the anionic resin AmberliteTMFPA54 with immobilisation yield of 93.4% for adsorptive and 100% forcovalent attachment, corresponding activities of 48.9 and 39.3%, respectively, leading to stabilisation of enzyme. At elevated temperature and under agitation, stabilisation is further increased by modification of the covalently bound SH with methoxy-poly(ethylene) glycol(mPEG). In stationary aqueous solution, half-lives of up to 161 h at 25°C and 32 h at 35°C are obtained.In presence of the DMSO, DMF, 2-propanol and [EMIM][EtSO4] half-lives of 14-29 h can be achieved
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Burgdorf, T.; De Lacey, A.L.; Friedrich, B.
Functional analysis by site-directed mutagenesis of the NAD+-reducing hydrogenase from Ralstonia eutropha
J. Bacteriol.
184
6280-6288
2002
Cupriavidus necator
brenda
Tran-Betcke, A.; Warnecke, U.; Böcker, C.; Zaborosch, C.; Friedrich, B.
Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16
J. Bacteriol.
172
2920-2929
1990
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Pfitzner, J.; Linke, H.A.B.; Schlegel, H.G.
Properties of the NAD-specific hydrogenase from Hydrogenomonas H 16
Arch. Mikrobiol.
71
67-78
1970
Hydrogenomonas sp., Hydrogenomonas sp. H16
brenda
Rohde, M.; Johannssen, W.; Mayer, F.
Immunocytochemical localization of the soluble NAD-dependent hydrogenase in cells of alcaligenes eutrophus
FEMS Microbiol. Lett.
36
83-86
1986
Cupriavidus necator
-
brenda
Hyman, M.R.; Arp, D.J.
Reversible and irreversible effects of nitric oxide on the soluble hydrogenase from Alcaligenes eutrophus H16
Biochem. J.
254
469-475
1988
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Hyman, M.R.; Fox, C.A.; Arp, D.J.
Role of hydrogen in the activation and regulation of hydrogen oxidation by the soluble hydrogenase from Alcaligenes eutrophus H16
Biochem. J.
254
463-468
1988
Cupriavidus necator
brenda
Popov, V.O.; Ovchinnikov, A.N.; Utkin, I.B.; Gazaryan, I.G.; Egorov, A.M.; Berezin, I.V.
Inactivation of the NAD-dependent hydrogenase from the hydrogen-oxidizing bacterium Alcaligenes eutrophus Z1: Thermoinactivation mechanism
Biochim. Biophys. Acta
831
297-301
1985
Cupriavidus necator, Cupriavidus necator Z1
-
brenda
Popov, V.O.; Gazaryan, I.G.; Egorov, A.M.; Berezin, I.V.
NAD-dependent hydrogenase from the hydrogen-oxidizing bacterium Alcaligenes eutrophum Z1. Kinetic studies of the NADH-dehydrogenase activity
Biochim. Biophys. Acta
827
466-471
1985
Cupriavidus necator, Cupriavidus necator Z1
-
brenda
Schneider, K.; Schlegel, H.G.
Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16
Biochim. Biophys. Acta
452
66-80
1976
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Schneider, K.; Schlegel, H.G.
Localization and stability of hydrogenases from aerobic hydrogen bacteria
Arch. Microbiol.
112
229-238
1977
Cupriavidus necator, no activity in Alcaligenes paradoxus, no activity in Aquaspirillum autotrophicum, no activity in Corynebacterium autotrophicum, no activity in Paracoccus denitrificans, no activity in Pseudomonas facilis, no activity in Hydrogenophaga palleronii, Cupriavidus necator G27, Cupriavidus necator N9A, Cupriavidus necator b19, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Aggag, M.; Schlegel, H.G.
Studies on a gram-positive hydrogen bacterium, Nocardia opaca 1 b. III. Purification, stability and some properties of the soluble hydrogen dehydrogenase
Arch. Microbiol.
100
25-39
1974
Rhodococcus opacus, Rhodococcus opacus 1B
brenda
Schneider, K.; Schlegel, H.G.; Jochim, K.
Effect of nickel on activity and subunit composition of purified hydrogenase from Nocardia opaca 1 b
Eur. J. Biochem.
138
553-541
1984
Rhodococcus opacus, Rhodococcus opacus 1B
-
brenda
Schneider, K.; Cammack, R.; Schlegel, H.G.
Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b
Eur. J. Biochem.
142
75-84
1984
Rhodococcus opacus, Rhodococcus opacus 1B
brenda
Petrov, R.R.; Utkin, I.B.; Popov, V.O.
Redox-dependent inactivation of the NAD-dependent hydrogenase from Alcaligenes eutrophus Z1
Arch. Biochem. Biophys.
268
298-305
1989
Cupriavidus necator, Cupriavidus necator Z1
brenda
Petrov, R.R.; Utkin, I.B.; Popov, V.O.
Effect of redox potential on the activation of the NAD-dependent hydrogenase from Alcaligenes eutrophus Z1
Arch. Biochem. Biophys.
268
287-297
1989
Cupriavidus necator, Cupriavidus necator Z1
brenda
Friedrich, C.G.; Suetin, S.; Lohmeyer, M.
Nickel and iron incoorporation into soluble hydrogenase of alcaligenes eutrophus
Arch. Microbiol.
140
206-211
1984
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
brenda
Friedrich, C.G.; Schneider, K.; Friedrich, B.
Nickel in the catalytically active hydrogenase of Alcaligenes eutrophus
J. Bacteriol.
152
42-48
1982
Cupriavidus necator
brenda
Schneider, K.; Schlegel, H.G.
Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16
Biochem. J.
193
99-107
1981
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Schneider, K.; Cammack, R.; Schlegel, H.G.; Hall, D.O.
The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus
Biochim. Biophys. Acta
578
445-461
1979
Cupriavidus necator
brenda
Schneider, K.; Schlegel, H.G.
Identification and quantitative determination of the flavin component of soluble hydrogenase from Alcaligenes eutrophus
Biochem. Biophys. Res. Commun.
84
564-571
1978
Cupriavidus necator
brenda
Grzeszik, C.; Ross, K.; Schneider, K.; Reh, M.; Schlegel, H.G.
Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22
Arch. Microbiol.
167
172-176
1997
Achromobacter denitrificans, Cupriavidus necator, Achromobacter ruhlandii, Rhodococcus opacus, Cupriavidus necator Cd2/01, Achromobacter denitrificans 4a-2, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Happe, R.P.; Roseboom, W.; Egert, G.; Friedrich, C.G.; Massanz, C.; Friedrich, B.; Albracht, S.P.
Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha
FEBS Lett.
466
259-263
2000
Cupriavidus necator
brenda