1.12.99.6: hydrogenase (acceptor)
This is an abbreviated version!
For detailed information about hydrogenase (acceptor), go to the full flat file.
Word Map on EC 1.12.99.6
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1.12.99.6
-
hydrogenases
-
h-cluster
-
nitrogenase
-
reinhardtii
-
chlamydomonas
-
diiron
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ferredoxins
-
dithiolate
-
desulfovibrio
-
hydf
-
hupls
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subcluster
-
maturase
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heterocystous
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nostoc
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organometallic
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eutropha
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acetobutylicum
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pasteurianum
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n2-fixing
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o2-tolerant
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diazotrophic
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photoproduction
-
electrocatalytic
-
electrocatalysts
-
photobiological
-
fhl
-
mixed-valence
-
gallinae
-
hydrogen-producing
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biohydrogen
-
overpotential
-
nickel-containing
-
cubane
-
diphosphine
-
sacrificial
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heterolytic
-
oxygen-tolerant
-
hydrogen-oxidizing
-
h2-producing
-
desulfuricans
-
roseopersicina
-
syntrophic
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h2-oxidizing
-
photocatalytic
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f0f1-atpase
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h2ases
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thiocapsa
-
industry
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brewing
- 1.12.99.6
- hydrogenases
-
h-cluster
- nitrogenase
- reinhardtii
- chlamydomonas
-
diiron
- ferredoxins
-
dithiolate
- desulfovibrio
- hydf
-
hupls
-
subcluster
-
maturase
-
heterocystous
- nostoc
-
organometallic
- eutropha
- acetobutylicum
- pasteurianum
-
n2-fixing
-
o2-tolerant
-
diazotrophic
-
photoproduction
-
electrocatalytic
-
electrocatalysts
-
photobiological
- fhl
-
mixed-valence
- gallinae
-
hydrogen-producing
-
biohydrogen
-
overpotential
-
nickel-containing
- cubane
-
diphosphine
-
sacrificial
-
heterolytic
-
oxygen-tolerant
-
hydrogen-oxidizing
-
h2-producing
- desulfuricans
- roseopersicina
-
syntrophic
-
h2-oxidizing
-
photocatalytic
- f0f1-atpase
- h2ases
-
thiocapsa
- industry
- brewing
Reaction
Synonyms
ECH, Ech hydrogenase, EchA, EchB, EchD, EchE, EchF, endo-hydrogenase, energy-converting hydrogenase, exo-hydrogenase, F420-reducing [NiFe] hydrogenase, factor420 hydrogenase, Fe-hydrogenase, Fe-only hydrogenase, ferredoxin hydrogenase, H2 producing hydrogenase [ambiguous], H2-sensing [NiFe] hydrogenase, Hfs, Hmd, HoxEFUYH type [NiFe] hydrogenase, HoxG, HupB, HupL, HupS, hupSLW, Hya, HyaA, HyaB, Hyb, HybA, HyC, HycE, Hyd X, Hyd-1, Hyd-2, Hyd-3, Hyd-4, HYD1, hydA, HydA1, HydA2, HydB, hydrogen dehydrogenase, hydrogen uptake hydrogenase, hydrogen-forming methylenetetrahydromethanopterin dehydrogenase, hydrogen-lyase, hydrogen-lyase [ambiguous], hydrogen:ferredoxin oxidoreductase, hydrogen:methylviologen oxidoreductase, hydrogenase (ferredoxin), hydrogenase 1, hydrogenase 2, hydrogenase 3, hydrogenase I (bidirectional), hydrogenase II, hydrogenase II (uptake), hydrogenase-1, hydrogenase-2, hydrogenase-Fe-S, hydrogenases Hyd-1, hydrogenases Hyd-2, hydrogenlyase [ambiguous], hyf, HyhL, HynSL, HynSL hydrogenase, Hyq, iron-sulfur-cluster-free hydrogenase, Mbh, membrane-bound [NiFe]-hydrogenase, methyl viologen-reducing hydrogenase, methylviologen hydrogenase, Ni-Fe hydrogenase, nickel-iron hydrogenase, NiFe hydrogenase, NiFe(Se) hydrogenase, NiFe-hydrogenase, NIFeSe-hydrogenase, regulatory hydrogenase, respiratory hydrogenase, SHI, uptake hydrogenase, uptake hydrogenase [ambiguous], uptake [NiFe] hydrogenase:, uptake [NiFe]-hydrogenase, [FeFe] hydrogenase, [FeFe]-H2ase, [FeFe]-hydrogenase, [FeFe]H2ase, [Fe] hydrogenase, [Fe]-hydA, [Fe]-hydrogenase, [Ni-Fe] hydrogenase, [NiFeSe]-hydrogenase, [NiFe] hydrogenase, [NiFe]-hydrogenase, [NiFe]-hydrogenase 2, [NiFe]-hydrogenase-2, [NiFe]H2ase, [NiFe]hydrogenase
ECTree
1.12.99.6 hydrogenase (acceptor)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.12.99.6 - hydrogenase (acceptor)
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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
H2 + 2,3,5-triphenyltetrazolium chloride
reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
-
?
H2 + 2,3-dimethyl-1,4-naphthoquinone
2,3-dimethyl-naphthoquinol
-
-
-
-
?
H2 + anthraquinone 2,6-disulfonic acid
anthraquinol 2,6-disulfonic acid
-
-
-
-
?
H2 + oxidized 2,3-dimethylnaphthoquinone
2,3-dimethylnaphthoquinol
-
-
-
-
?
H2 + oxidized phenazine methosulfate
reduced phenazine methosulfate + H+
-
-
-
-
?
H2 + phenazine methosulfate
H+ + reduced phenazine methosulfate
-
best electron acceptor
-
-
?
H2 + acceptor
acceptor-H2
-
Hyb is essential for hydrogen-dependent growth with a variety of electron acceptors, including Fe3+
-
-
?
H2 + acceptor
acceptor-H2
Megalodesulfovibrio gigas
-
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
enzyme acts on artificial electron-accepting dyes, but is ineffective with pyridine nucleotides or other soluble physiological electron acceptors
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methylene blue acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
inactivation of hydrogenase genes impairs bacterial nitrogenase activity in Bradyrhizobium sp. (Vigna) and has an effect on total nitrogen content of the symbiotic plant partner, Vigna unguiculata. Hydrogenase activity might be necessary for optimal levels of nitrogenase activity in Bradyrhizobium sp. (Vigna) bacteroids
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
2 different enzymes, hydrogenase I and II
-
r
H2 + acceptor
H+ + reduced acceptor
-
2 different enzymes, hydrogenase I and II
-
-
r
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen acts as electron acceptor
-
r
H2 + acceptor
H+ + reduced acceptor
Cronbergia siamensis SAG 11.82 TISTR 8012
Q84GM3; Q4G6A7
-
-
-
r
H2 + acceptor
H+ + reduced acceptor
-
benzyl viologen acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen acts as electron acceptor
-
r
H2 + acceptor
H+ + reduced acceptor
-
methylene blue acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methylene blue acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
enzyme is more active in hydrogen evolution than in hydrogen uptake
-
?
H2 + acceptor
H+ + reduced acceptor
-
reaction mechanism
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
benzyl viologen, methylene blue and methylviologen can act as electron acceptors
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methylene blue acts as electron acceptor
-
r
H2 + acceptor
H+ + reduced acceptor
-
methylene blue, methyl viologen, methionaquinone, FMN and FAD can serve as electron acceptors, but not NAD+ or NADP+
-
-
?
H2 + acceptor
H+ + reduced acceptor
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
methylene blue, methyl viologen, methionaquinone, FMN and FAD can serve as electron acceptors, but not NAD+ or NADP+
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
2 different enzymes, hydrogenase I and II
-
-
r
H2 + acceptor
H+ + reduced acceptor
-
benzyl viologen, methylene blue, ferredoxin and methylviologen can act as electron acceptors
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
ferredoxin acts as physiological electron donor
-
-
?
H2 + acceptor
H+ + reduced acceptor
Methanosarcina barkeri Fusaro / DSM 804
-
benzyl viologen, methylene blue, ferredoxin and methylviologen can act as electron acceptors
-
-
?
H2 + acceptor
H+ + reduced acceptor
Methanosarcina barkeri Fusaro / DSM 804
-
ferredoxin acts as physiological electron donor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
benzyl viologen, methyl viologen, NADPH and NADH can serve as electron donors
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen acts as electron acceptor
-
r
H2 + acceptor
H+ + reduced acceptor
-
methylene blue acts as electron acceptor
-
r
H2 + acceptor
H+ + reduced acceptor
-
reduced ferredoxin can act as acceptor
-
r
H2 + acceptor
H+ + reduced acceptor
-
ferredoxin acts as physiological electron donor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
Hya can oxidize both exogenously added H2 and formate hydrogen lyase-evolved H2 anaerobically
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
Hya can oxidize both exogenously added H2 and formate hydrogen lyase-evolved H2 anaerobically
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
benzyl viologen acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen acts as electron acceptor
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
methyl viologen and benzyl viologen can serve as electron acceptors
-
-
?
H2 + acceptor
reduced acceptor
the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient
-
-
?
H2 + acceptor
reduced acceptor
the periplasmic-facing membrane-bound complex functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient
-
-
?
H2 + methenyltetrahydromethanopterin
H+ + methylenetetrahydromethanopterin
-
the heterolytic cleavage of H2 by the enzyme is dependent on the presence of methenyltetrahydromethanopterin
-
-
r
H2 + methenyltetrahydromethanopterin
H+ + methylenetetrahydromethanopterin
-
the presence of methenyltetrahydromethanopterin is essentially required for H2 activation by [Fe] hydrogenase
-
-
r
H2 + methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized acceptor
H+ + reduced acceptor
-
almost 100% of the membrane-attached MBH is reversibly redox-active
-
-
?
H2 + oxidized acceptor
H+ + reduced acceptor
-
[NiFeSe]-hydrogenase is a highly efficient H2 cycling catalyst
-
-
?
H2 + oxidized acceptor
H+ + reduced acceptor
Solidesulfovibrio fructosivorans
-
heterolytic H2 cleavage, with one hydrogen ending up as a bridging hydride and one as a proton on a cysteine ligand, which has a barrier slightly too high to be compatible with measured catalytic turnover rates. Alternative mechanisms suggest heterolytic cleavage as an initial step to generate a complex with nickel in oxidation state Ni(I). In the following cycles, H2 is instead cleaved on nickel using an oxidative addition mechanism with a lower barrier
-
-
?
H2 + oxidized acceptor
H+ + reduced acceptor
Q2PWI0, Q2PWI3, Q2PWI4, Q2PWI5, Q2PWI6, Q2PWI7, Q2PWI9, Q2PWJ0, Q2PWJ8, Q38IH5, Q38IH6, Q38IH8, Q38IH9, Q38II3, Q38II4, Q38IJ1
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduceded benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduceded benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduceded benzyl viologen
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduceded benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduceded benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
-
-
-
r
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
there is at least one autocatalytic reaction step in the hydrogenase-catalyzed reaction
-
-
?
H2 + oxidized dichloroindophenol
H+ + reduced dichloroindophenol
-
-
-
-
?
H2 + oxidized dichloroindophenol
H+ + reduced dichloroindophenol
-
-
-
-
?
H2 + oxidized electron acceptor
H+ + reduced electron acceptor
-
-
-
-
?
H2 + oxidized electron acceptor
H+ + reduced electron acceptor
-
both platinum and pyrolytic graphite edge/HydA electrodes are effective catalysts operating near the reversible potential of the H+/H2 redox couple
-
-
?
H2 + oxidized electron acceptor
H+ + reduced electron acceptor
-
-
-
-
?
H2 + oxidized electron acceptor
H+ + reduced electron acceptor
-
-
-
-
?
H2 + oxidized electron acceptor
H+ + reduced electron acceptor
-
-
-
-
?
H2 + oxidized methionaquinone
reduced methionaquinone
Hydrogenobacter thermophilus TK-6 / IAM 12695
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
Aeropyrum camini SY1 / ATCC BAA-758 / DSM 16960 / JCM 2091
-
-
-
-
?
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
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
Tetraselmis sp. KSN-2002 NCIM 1605
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen + H+
-
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen + H+
-
-
-
-
?
H2 + oxidized methyl viologen
reduced methyl viologen + H+
-
-
-
-
r
H2 + oxidized methyl viologen
reduced methyl viologen + H+
-
-
-
-
r
H2 + oxidized methyl viologen
reduced methyl viologen + H+
Solidesulfovibrio fructosivorans
-
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
-
?
H2 + oxidized methylene blue
reduced methylene blue + H+
-
-
-
-
?
H2 + oxidized sodium hydrosulfite
H+ + reduced sodium hydrosulfite
-
-
-
-
?
H2 + oxidized sodium hydrosulfite
H+ + reduced sodium hydrosulfite
-
-
-
-
?
additional information
?
-
-
although the HoxF subunit contains binding sites for flavin mononucleotide and NAD(H), cell-free extracts of Allochromatium vinosum does not catalyse a H2-dependent reduction of NAD+
-
-
?
additional information
?
-
-
the large subunit preHoxG is able to activate H2 as it performs catalytic hydrogen/deuterium exchange. However, it did not execute the entire catalytic cycle described for [NiFe] hydrogenases. H2 activation is performed by preHoxG even in the presence of O2, although the unique [4Fe-3S] cluster located in the small subunit and described to be crucial for tolerance toward O2 is absent
-
-
-
additional information
?
-
Cupriavidus necator HF795
-
the large subunit preHoxG is able to activate H2 as it performs catalytic hydrogen/deuterium exchange. However, it did not execute the entire catalytic cycle described for [NiFe] hydrogenases. H2 activation is performed by preHoxG even in the presence of O2, although the unique [4Fe-3S] cluster located in the small subunit and described to be crucial for tolerance toward O2 is absent
-
-
-
additional information
?
-
-
the enzyme exhibits both proton-reducing and H2-oxidizing activities
-
-
?
additional information
?
-
-
no activity is observed using NAD+, 2,3-dimethoxy methyl-1,4-benzoquinone, and potassium ferricyanide as electron acceptors
-
-
?
additional information
?
-
-
no activity is observed using NAD+, 2,3-dimethoxy methyl-1,4-benzoquinone, and potassium ferricyanide as electron acceptors
-
-
?
additional information
?
-
Solidesulfovibrio fructosivorans
-
the catalytic bias, i.e. the ratio of maximal rates in the two directions is not mainly determined by redox properties of the active site, but rather by steps which occur on sites of the proteins that are remote from the active site
-
-
?
additional information
?
-
-
a diiron dithiolate complex holding a micro-hydride on the iron atoms and a proton on the basic site of a chelating diphosphine ligand as a structural model of the [FeFe]-hydrogenase active site. The pendant base in the phosphine ligand may play a similar role to the proton-transfer relay as the bridging N in a diiron azadithiolate complex does
-
-
?
additional information
?
-
-
oxidation of hexacarbonyl(1,3-dithiolato-S,S')diiron complexes with varying amounts of dimethyldioxirane as mimics of the active site of [FeFe]-hydrogenase. Chemoselectivity of the oxidation products depends upon the substituent R (R=H, Me, 1/2 (CH2)5)
-
-
?
additional information
?
-
-
protonation of a model of the subsite of [FeFe]-hydrogenase, [Fe2(micro-pdt)(CO)4(PMe3)2]. The deceptively simple stoichiometric reaction is limited by the rate of protonation of the basal-apical isomer followed by its rearrangement to the transoid basal form
-
-
?
additional information
?
-
-
study on the catalytic mechanism of an active-site model of [Fe] hydrogenase by small modifications of the first ligand shell. Dispersion interactions between the active site and the hydride acceptor methenyltetrahydromethanopterin render the hydride transfer step less endergonic and lower its barrier. Substitution of CO by CN-, which resembles [FeFe] hydrogenase-like coordination, inverts the elementary steps H- transfer and H2 cleavage. The catalytic efficiency of [Fe] hydrogenase can be attributed to a flat energy profile throughout the catalytic cycle. Intermediates that are too stable, as they occur, e.g., when one CO ligand is substituted by CN-, significantly slow down the turnover rate of the enzyme. The catalytic activity of the wild-type form of the active-site model could, however, be enhanced by a PH3 ligand substitution of the CO ligand
-
-
?
additional information
?
-
-
hydrogenase during its reaction cycle has an autocatalytic step
-
-
?
