Information on EC 1.12.99.6 - hydrogenase (acceptor)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
1.12.99.6
-
RECOMMENDED NAME
GeneOntology No.
hydrogenase (acceptor)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2 + acceptor = reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hydrogen oxidation I (aerobic)
-
-
hydrogen to dimethyl sulfoxide electron transfer
-
-
hydrogen to fumarate electron transfer
-
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hydrogen to trimethylamine N-oxide electron transfer
-
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hydrogen production
-
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Nitrotoluene degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:acceptor oxidoreductase
Uses molecular hydrogen for the reduction of a variety of substances. Contains iron-sulfur clusters. The enzyme from some sources contains nickel.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-05-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SY1, JCM12091
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Manually annotated by BRENDA team
strain SY1, JCM12091
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Manually annotated by BRENDA team
strain PCC 7120, also named Nostoc sp. strain PCC 7120
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
fragment; strain M1
UniProt
Manually annotated by BRENDA team
fragment; strain M1
UniProt
Manually annotated by BRENDA team
strain WH8501
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-
Manually annotated by BRENDA team
Cyanobium sp.
-
-
-
Manually annotated by BRENDA team
Cyanothece sp.
Cyanothece sp. CCY 0110
-
-
-
Manually annotated by BRENDA team
large subunit of HupL and small subunit of HupL; strain TISTR 8012
Q84GM3 and Q4G6A7
UniProt
Manually annotated by BRENDA team
strain 195
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-
Manually annotated by BRENDA team
strain 9974
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-
Manually annotated by BRENDA team
Norway strain
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-
Manually annotated by BRENDA team
strain Groningen
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-
Manually annotated by BRENDA team
strain Hildenborough
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Manually annotated by BRENDA team
IIT-BT 08
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-
Manually annotated by BRENDA team
IIT-BT 08
-
-
Manually annotated by BRENDA team
K-12 BW25113; strain K-12 BW25113
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-
Manually annotated by BRENDA team
strains UGL011102, AVCI1 and KB5
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain TK-6
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-
Manually annotated by BRENDA team
strain TK-6
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-
Manually annotated by BRENDA team
Hydrogenophaga sp.
AH-24
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-
Manually annotated by BRENDA team
AH-24
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Lyngbya sp.
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Nostoc azollae
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-
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Manually annotated by BRENDA team
Nostoc sp. PCC 7422
large subunit
UniProt
Manually annotated by BRENDA team
strain 29W, JCM11663
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-
Manually annotated by BRENDA team
strain 29W, JCM11663
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain DSM 3638
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-
Manually annotated by BRENDA team
biovar viciae
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-
Manually annotated by BRENDA team
strain S12
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Manually annotated by BRENDA team
strain S12
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-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
synthetic construct
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Manually annotated by BRENDA team
NCIM 1605
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-
Manually annotated by BRENDA team
Tetraselmis sp. KSN-2002 NCIM 1605
NCIM 1605
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-
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
strain DSM 1276 formerly Desulfovibrio thermophilus
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-
Manually annotated by BRENDA team
strain BBS
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
heterologous expression of the two structural genes of [FeFe]-hydrogenase in Escherichia coli yields an inactive enzyme, only the two ferredoxin-like [Fe4S4] clusters are unambiguously assembled
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formate
H2 + CO2
show the reaction diagram
H2 + 2,3-dimethyl-1,4-naphthoquinone
2,3-dimethyl-naphthoquinol
show the reaction diagram
-
-
-
-
?
H2 + 2,4,6-trinitrotoluene
?
show the reaction diagram
-
-
-
-
?
H2 + acceptor
acceptor-H2
show the reaction diagram
H2 + acceptor
acceptorH2
show the reaction diagram
H2 + acceptor
H+ + reduced acceptor
show the reaction diagram
H2 + acceptor
H2-acceptor
show the reaction diagram
H2 + anthraquinone 2,6-disulfonic acid
anthraquinol 2,6-disulfonic acid
show the reaction diagram
-
-
-
-
?
H2 + benzyl viologen
H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
H2 + Cr6+
Cr3+ + H+
show the reaction diagram
H2 + methenyltetrahydromethanopterin
H+ + methylenetetrahydromethanopterin
show the reaction diagram
H2 + methyl viologen
H+ + reduced methyl viologen
show the reaction diagram
H2 + O2
?
show the reaction diagram
H2 + oxidized 2,3-dimethylnaphthoquinone
2,3-dimethylnaphthoquinol
show the reaction diagram
-
-
-
-
?
H2 + oxidized acceptor
H+ + reduced acceptor
show the reaction diagram
H2 + oxidized amaranth
H+ + reduced amaranth
show the reaction diagram
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
show the reaction diagram
H2 + oxidized benzyl viologen
H+ + reduceded benzyl viologen
show the reaction diagram
H2 + oxidized benzyl viologen
reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
show the reaction diagram
H2 + oxidized dichloroindophenol
H+ + reduced dichloroindophenol
show the reaction diagram
H2 + oxidized diquat
reduced diquat + H+
show the reaction diagram
-
-
-
-
?
H2 + oxidized electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
H2 + oxidized ethyl viologen
reduced ethyl viologen + H+
show the reaction diagram
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
show the reaction diagram
H2 + oxidized methyl viologen
reduced methyl viologen + H+
show the reaction diagram
H2 + oxidized methylene blue
H+ + reduced methylene blue
show the reaction diagram
H2 + oxidized methylene blue
reduced methylene blue + H+
show the reaction diagram
-
-
-
-
?
H2 + oxidized metranidazole
H+ + reduced metranidazol
show the reaction diagram
-
-
-
-
?
H2 + oxidized phenazine methosulfate
reduced phenazine methosulfate + H+
show the reaction diagram
-
-
-
-
?
H2 + oxidized sodium hydrosulfite
H+ + reduced sodium hydrosulfite
show the reaction diagram
H2 + phenazine methosulfate
H+ + reduced phenazine methosulfate
show the reaction diagram
-
best electron acceptor
-
-
?
H2 + S
H2S
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H2 + acceptor
acceptor-H2
show the reaction diagram
H2 + acceptor
acceptorH2
show the reaction diagram
H2 + acceptor
H+ + reduced acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
FAD
-
0.83 mol FAD per enzyme
heme b
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involved in electron transport
iron-sulfur centre
additional information
-
iron-guanylylpyridinol
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mo
-
0.0025 mmol Mo per g protein
selenium
-
[NiFeSe]-hydrogenase
Sulfide
additional information
-
no increase in the hydrogenase activity is observed in response to ferric sulfate, ferric citrate, ferric ammonium citrate, and ferric nitrate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
Cd2+
-
reversible inhibition
diethyldicarbonate
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65% loss of activity 6 mM
H2
-
inhibits hydrogen production
Hg2+
-
complete inhibition at 1 mM
Mg2+
-
reversible inhibition
N-bromosuccinimide
-
complete inactivation at 10 mM, 20% inactivation at 0.1 mM
Ni2+
-
competitive vs. Oxidized methyl viologen
nitrite
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70% loss of activity after 2 min at 0.04 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dihydroxy-L-phenylalanine
-
substitutes for tyrosine to stimulate in vitro HydA1 activation, improves HydA1 maturation 4fold
HoxL
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the auxiliary protein HoxL participates specifically in the maturation of the large subunit of the enzyme. It is essential for H2-oxidizing activity and enzyme-driven growth on H2. HoxL acts as a specific chaperone assisting the transfer of the Fe(CN-)2CO cofactor intermediate from the Hyp machinery to the enzyme
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HoxV
-
the auxiliary protein HoxL participates specifically in the maturation of the large subunit of the enzyme. It is essential for H2-oxidizing activity and enzyme-driven growth on H2. HoxV functions as a scaffold delivering the Fe(CN-)2CO moiety to the precursor of the large subunit pre-HoxG of the enzyme
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HydE
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HydEF
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maturase, role in biosynthesis of the active site. HydEF and hydG, coexpressed with the structural genes hydA1 and hydA2 in Escherichia coli lead to active [FeFe]-hydrogenase
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HydF
-
HydG
-
HypB
-
accessory protein HypB is necessary for the production of active hydrogenase
-
HypC
-
is essential for cofactor assembly
-
S-adenosyl methionine
-
exogenous S-adenosyl methionine stimulates in vitro hydrogenase activation, but does not individually enhance hydrogenase activation. 2 mM increases hydrogenase activity 4fold
Sulfide
-
1 mM increases hydrogenase activity 4fold, is not sufficient to increase hydrogenase activities without S-adenosyl methionine and the standard 20 L-amino acids
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045 - 1.78
benzyl viologen
0.016 - 0.021
Cr6+
0.000047 - 25
H2
300
methionaquinone
-
-
-
0.055 - 12.5
methyl viologen
0.017 - 0.025
methylene blue
0.01
methylenetetrahydromethanopterin
-
at pH 6.0 and 25C
0.128
NAD+
-
-
0.001
oxidized ferredoxin
-
-
0.0075
reduced ferredoxin
-
-
additional information
additional information
-
Km for various electron donors
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1500 - 9000
Abz-VAA
Allochromatium vinosum
-
NiFe hydrogenase attached to a pyrolytic graphite electrode
-
240
benzyl viologen
Hydrogenophaga sp.
-
pH 7.0, 30C
0.09 - 1.3
Cr6+
48.3
methionaquinone
Hydrogenobacter thermophilus
-
-
-
20
methyl viologen
Hydrogenophaga sp.
-
pH 7.0, 30C
560
methylene blue
Hydrogenophaga sp.
-
pH 7.0, 30C
additional information
additional information
Pyrococcus furiosus
-
turnover number for various electron donors
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
135
benzyl viologen
Hydrogenophaga sp.
-
pH 7.0, 30C
648
1.6
methyl viologen
Hydrogenophaga sp.
-
pH 7.0, 30C
355
22400
methylene blue
Hydrogenophaga sp.
-
pH 7.0, 30C
512
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00016 - 0.0355
CO
0.16 - 1.35
Ni2+
0.0025 - 0.0055
O2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
-
hydrogen uptake specific activity of the hydrogenase 3 lacking mutant enzyme HD705/pBS(Kan), using methyl viologen as a substrate
0.035
-
hydrogen uptake specific activity of the wild type enzyme, using methyl viologen as a substrate
0.107
-
crude extract
0.4 - 0.7
-
H2 evolution
1.92
-
methyl viologen reduction by H2
2
-
crude extract, at 55C, pH 7.0, using methylene blue as electron acceptor
14.6
-
purified enzyme, proton reduction activity
14.8
-
2.4fold purified enzyme, hydrogen oxidation activity
30
-
after 152fold purification, at 55C, pH 7.0, using dichloroindophenol as electron acceptor
55
-
after 152fold purification, at 55C, pH 7.0, using methyl viologen as electron acceptor
80
-
Cr6+ reduction; H2 uptake
90
-
H2 formation with reduced ferredoxin
110
Hydrogenophaga sp.
-
purified enzyme
114
-
acceptor methyl viologen
150
-
at pH 6.0 and 25C
161
-
Cr6+ reduction
230
-
H2 evolution
300
-
; acceptor benzyl viologen
332
-
H2 uptake
344
-
after 152fold purification, at 55C, pH 7.0, using methylene blue as electron acceptor
484
-
after 152fold purification, at 80C, pH 7.0, using methylene blue as electron acceptor
624
-
acceptor 2,3-dimethylnaphthoquinol
1078
-
after 152fold purification, at 55C, pH 7.0, using phenazine methosulfate as electron acceptor
7680
-
Cr6+ reduction
50000
-
H2 uptake
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
the steady-state current caused by catalytic uptake of hydrogen is maximal at pH 5.5-6.5 under overvoltage of 30-60 mV
5.9
-
the maximum H2 oxidation current increases as the pH is raised from 4.3 to 5.9
6 - 6.5
-
the steady-state current caused by catalytic uptake of hydrogen is maximal at pH 6.0-6.5 under overvoltage of 30-60 mV
6.5
-
optimal pH for the proton reduction activity
8.5 - 9.5
-
H2 oxidation
9.5
-
in solution
additional information
-
solubilization of the imer is associated with a downshift of the optimum pH for H2-oxidizing activity