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
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hydrogenases
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h-cluster
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nitrogenase
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reinhardtii
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chlamydomonas
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diiron
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ferredoxins
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dithiolate
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desulfovibrio
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hydf
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hupls
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subcluster
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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
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electrocatalytic
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electrocatalysts
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photobiological
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fhl
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mixed-valence
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gallinae
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hydrogen-producing
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biohydrogen
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overpotential
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nickel-containing
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cubane
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diphosphine
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sacrificial
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heterolytic
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oxygen-tolerant
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hydrogen-oxidizing
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h2-producing
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desulfuricans
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roseopersicina
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syntrophic
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h2-oxidizing
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photocatalytic
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f0f1-atpase
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h2ases
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thiocapsa
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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
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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 (Inhibitors
Inhibitors on EC 1.12.99.6 - hydrogenase (acceptor)
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
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8 residues modified by 0.5 mM in the presence of 30 mM nitrotyrosine ethylester
5-5'dithiobis-(2-nitrobenzoate)
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chemical modification of cysteine residues, 8 residues modified by 0.5 mM. 16 residues modified in the presence of 2% sodium dodecyl sulfate. 20 residues modified by 1 mM and in the presence of urea, EDTA, NaBH4
MoO42-
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inhibition of sulfate reduction by molybdate inhibited the overall oxidation of hydrogen but still facilitates an equilibrium isotope exchange reaction with water. Resulting delta2H-values of H2 correspond to theoretical thermodynamic isotope equilibria
N-bromosuccinimide
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complete inactivation at 10 mM, 20% inactivation at 0.1 mM
CO
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bond length alterations after incubation of HydA1 with CO and H2, related to structural and oxidation state changes at the catalytic Fe atoms, e.g., to the binding of an exogenous CO at 2FeH in CO-inhibited enzyme
CO
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binds irreversibly, hydrogenase I has a lower affinity for CO than hydrogenase II
CO
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noncompetitive vs. oxidized methyl viologen, competitive vs. H2
CO
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the bis(PMe3) nitrosyl complexes readily undergo CO substitution to give the (PMe3)3 derivatives
Cu2+
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65% loss of activity after 2 min at 0.005 mM, complete inhibition at 0.1 mM in the presence of ascorbate, no inhibition observed without ascorbate
O2
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maintains 100% of its initial activity after a 48 h exposure to air, after 120 and 168 h exposures, the residual activities are 90% and 75%, respectively. It is very tolerant to oxygen
O2
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non competitive versus methylene blue, uncompetitive versus H2, reversibility is time-dependent, inhibition is protected by H2
O2
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the direct interaction of the [2Fe]H subsite with dioxygen is an exothermic and specific reaction in which O2 most favorably binds in an end-on manner to the distal iron. Irreversibility of dioxygen-induced enzyme inactivation by water release and degradation of the ligand environment of the H-cluster
O2
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reacts with the enzyme, reversibly, causing inactivation. Although traces of O2 (less than 1%) rapidly and completely remove H2 oxidation activity, the enzyme sustains partial activity for H2 production even in the presence of 1% O2 in the atmosphere. O2 tolerance of the [NiFeSe]-hydrogenase is greater at higher temperature
O2
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enzyme is quite stable under air atmosphere, half-life of activity is ca. 48 h at 4°C, inactivation is irreversible
O2
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the enzyme is irreversibly inhibited under aerobic conditions
O2
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exhibits 80% residual activity after exposure to air for 24 h, decreases to 75% and 37% after 48 and 72 h exposures, respectively. After a 96 h exposure, activity is undetectable. The enzyme is oxygen sensitive
additional information
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loss of Fe-Fe distances in protein purified under mildly oxidizing conditions, partial degradation of the H-cluster
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additional information
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immobilization of synthetic analogues of the [FeFe]H2ase active site on polyethyleneglycol-rich polystyrene beads
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additional information
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isomerization of the terminal hydride is inhibited both by the basicity of the Fe2 complex as well as by the steric size of the dithiolate in the models. In the enzyme, terminal-bridge isomerization may also be inhibited by hydrogen bonding between CNdistal and a epsilon-ammonium center of a nearby, highly conserved lysine residue
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additional information
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front velocity decreases on increase of the electron acceptor benzyl viologen concentration at all measured hydrogenase concentrations
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