Information on EC 1.12.7.2 - ferredoxin hydrogenase

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

EC NUMBER
COMMENTARY
1.12.7.2
-
RECOMMENDED NAME
GeneOntology No.
ferredoxin hydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
glutamate degradation VII (to butanoate)
-
hydrogen production III
-
hydrogen production VIII
-
Methane metabolism
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen:ferredoxin oxidoreductase
Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bidirectional hydrogenase
-
-
-
-
EC 1.12.1.1
-
-
formerly
-
EC 1.12.7.1
-
-
formerly
-
EC 1.18.3.1
-
-
formerly
-
EC 1.18.99.1
-
-
formerly
-
EC 1.98.1.1
-
-
formerly
-
Ech hydrogenase
-
-
Ech hydrogenase
-
-
EhbM
-
small subunit of energy-conserving hydrogenase B
EhbN
-
large subunit of energy-conserving hydrogenase B
energy-conserving hydrogenase B
-
-
Fe hydrogenlyase
-
-
-
-
Fe-Fe hydrogenase
-
-
Fe-hydrogenase
-
-
ferredoxin-dependent [FeFe] hydrogenase
-
-
ferredoxin-dependent [FeFe] hydrogenase
Thermotoga maritima DSM 3109
-
-
-
H2 oxidizing hydrogenase
-
-
-
-
H2 producing hydrogenase [ambiguous]
-
-
-
-
HYD1
-
-
-
-
HYD2
-
-
-
-
hydA
'Chlorella' fusca, Chlorococcum submarinum
-
-
hydrogen-lyase [ambiguous]
-
-
-
-
hydrogenase (ferredoxin)
-
-
-
-
hydrogenase I
-
-
-
-
hydrogenase II
-
-
-
-
hydrogenase of the Fe-only type
-
-
hydrogenlyase
-
-
-
-
hydrogenlyase [ambiguous]
-
-
-
-
MbhJ
Q8U0Z8
subunit of membrane-bound hydrogenase
MbhK
Q8U0Z7
membrane-bound hydrogenase subunit beta
MbhL
Q8U0Z6
membrane-bound hydrogenase subunit alpha
membrane bound NiFe hydrogenase
-
-
NiFe hydrogenase
-
-
-
-
reversible Fe-hydrogenase
-
-
uptake hydrogenase [ambiguous]
-
-
-
-
[FeFe]-hydrogenase
-
-
[FeFe]-hydrogenase
-
-
[FeFe]-hydrogenase
-
-
[FeFe]-hydrogenase
Thermotoga maritima DSM 3109
-
-
-
[Fe]-hydrogenase
-
-
[Ni-Fe] hydrogenase
-
-
[Ni-Fe] hydrogenase
Tetraselmis sp. KSN-2002 NCIM 1605
-
-
-
[NiFeSe] Hase
-
-
[NiFeSe] hydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9080-02-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATC 19859
-
-
Manually annotated by BRENDA team
Acidithiobacillus ferrooxidans ATC 19859
strain ATC 19859
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 137 C(+)
strain 137 C(+)
-
-
Manually annotated by BRENDA team
Chlorococcum submarinum
-
-
-
Manually annotated by BRENDA team
strain ATCC 824
-
-
Manually annotated by BRENDA team
hydrogenase I, bidirectional hydrogenase; hydrogenase II, uptake hydrogenase
-
-
Manually annotated by BRENDA team
hydrogenase I, bidirectional hydrogenase; hydrogenase II, uptake hydrogenase; strain MR 505
-
-
Manually annotated by BRENDA team
hydrogenase I, bidirectional hydrogenase; hydrogenase II, uptake hydrogenase; strain W5
-
-
Manually annotated by BRENDA team
hydrogenase I, bidirectional hydrogenase; strain W5
-
-
Manually annotated by BRENDA team
hydrogenase II, uptake hydrogenase
-
-
Manually annotated by BRENDA team
hydrogenase II, uptake hydrogenase; strain W5
-
-
Manually annotated by BRENDA team
strain ATCC 6013
-
-
Manually annotated by BRENDA team
Clostridium pasteurianum MR 505
strain MR 505
-
-
Manually annotated by BRENDA team
Clostridium pasteurianum W5
strain W5
-
-
Manually annotated by BRENDA team
strain H16, ATCC 17699
-
-
Manually annotated by BRENDA team
strain Hildenborough ATCC 29579
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough ATCC 29579
strain Hildenborough ATCC 29579
-
-
Manually annotated by BRENDA team
IIT-BT08 (MTCC 5373)
-
-
Manually annotated by BRENDA team
strain LC1, formerly Peptostreptococcus elsdenii
-
-
Manually annotated by BRENDA team
Megasphaera elsdenii LC1
strain LC1, formerly Peptostreptococcus elsdenii
-
-
Manually annotated by BRENDA team
strain Fusaro DSM 804
-
-
Manually annotated by BRENDA team
strain MS, DSM 800
-
-
Manually annotated by BRENDA team
Methanosarcina barkeri Fusaro
strain Fusaro DSM 804
-
-
Manually annotated by BRENDA team
strain MS, DSM 800
-
-
Manually annotated by BRENDA team
hydrogenase II; strain DSM 3638
-
-
Manually annotated by BRENDA team
wild-type Ktzing 276-6
-
-
Manually annotated by BRENDA team
strain DSM 2875
-
-
Manually annotated by BRENDA team
strain NCIM 1605
-
-
Manually annotated by BRENDA team
Tetraselmis sp. KSN-2002 NCIM 1605
strain NCIM 1605
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
all ehb mutants have severe growth deficiencies except the DeltaehbO::pac strain: The membrane-spanning ion translocator (DELTAehbF) and the large hydrogenase subunit (DELTAehbN) deletion strains display the severest growth defects. The DELTAehbN mutant strain is sensitive to growth inhibition by aryl acids
malfunction
-
the Ech hydrogenase deletion mutant shows 50% decreased ferredoxin-dependent membrane-bound electron transport activity, a lower growth rate, and 2fold faster substrate (trimethylamine) consumption compared to the wild type enzyme
physiological function
Q8U0Z6, Q8U0Z7, Q8U0Z8
enzyme of hydrogen metabolism; enzyme of hydrogen metabolism; enzyme of hydrogen metabolism
physiological function
-
photosynthetic induction of Chlamydomonas reinhardtii in anaerobic conditions is facilitated by the presence of hydrogenase as transient electron sink. Lack of hydrogenase activity in a state 1 locked mutant is detrimental to its ability to induce photosynthesis in an anaerobic environment
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(SeO3)2- + H2 + ?
Se + H2O + ?
show the reaction diagram
Clostridium pasteurianum, Clostridium pasteurianum W5
-
methyl viologen and benzyl viologen as electron acceptors
-
-
?
(TeO3)2- + H2 + ?
Te + H2O + ?
show the reaction diagram
Clostridium pasteurianum, Clostridium pasteurianum W5
-
methyl viologen as electron acceptor
-
-
?
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
-, the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
show the reaction diagram
-
-
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
show the reaction diagram
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced benzyl viologen
H2 + oxidized benzyl viologen
show the reaction diagram
-
58.8% relative activity, purified enzyme
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
-
-
-
r
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
Mbh function as a redox-driven ion pump coupling the reduction of protons with electrons derived from the oxidation of a low-potential ferredoxin to the generation of a H+ motive force
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
reaction is proposed to be coupled to energy conservation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
94.3% relative activity, purified enzyme
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
-
-
-
-
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
-
-
-
-
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
-
-
-
2
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
100% relative activity, purified enzyme
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
-
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
-
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
-
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
ferricyanide as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methylene blue as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
cytochrome b as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
cytochrome b as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
FAD and FMN as electron acceptors
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
phenosafranine as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
FAD, FMN or riboflavin as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
FAD, FMN or riboflavin as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
coenzyme F420 or factor F0 as electron acceptor, menadione as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
sulfonatopropyl viologen, sodium metatungstate and sodium silicotungstate as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
benzyl viologen as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
NADP+ as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
dichlorophenol indophenol as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Clostridium pasteurianum W5
-
methylene blue as electron acceptor, methyl viologen as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Clostridium pasteurianum W5
-
methylene blue as electron acceptor, methyl viologen as electron acceptor, FAD, FMN or riboflavin as electron acceptor, benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Clostridium pasteurianum W5
-
methylene blue as electron acceptor, methyl viologen as electron acceptor, benzyl viologen as electron acceptor, dichlorophenol indophenol as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Clostridium pasteurianum W5
-
methylene blue as electron acceptor, methyl viologen as electron acceptor, FAD and FMN as electron acceptors, dichlorophenol indophenol as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Clostridium pasteurianum W5
-
methylene blue as electron acceptor, methyl viologen as electron acceptor, benzyl viologen as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Clostridium pasteurianum W5
-
methylene blue as electron acceptor, methyl viologen as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Acidithiobacillus ferrooxidans ATC 19859
-
ferricyanide as electron acceptor, methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Methanosarcina barkeri Fusaro
-
methylene blue as electron acceptor, methyl viologen as electron acceptor, FAD, FMN or riboflavin as electron acceptor, coenzyme F420 or factor F0 as electron acceptor, menadione as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Methanosarcina barkeri Fusaro
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
-
methylene blue as electron acceptor, cytochrome b as electron acceptor, methyl viologen as electron acceptor, phenosafranine as electron acceptor, benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
methyl viologen as electron acceptor, sulfonatopropyl viologen, sodium metatungstate and sodium silicotungstate as electron acceptor
-
-
-
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
Megasphaera elsdenii LC1
-
methyl viologen as electron acceptor, benzyl viologen as electron acceptor
-
-
r
H2 + ferredoxin + oxidized metronidazole
H+ + ferredoxin + reduced metronidazole
show the reaction diagram
-
-
-
-
?
H2 + ferredoxin + oxidized metronidazole
H+ + ferredoxin + reduced metronidazole
show the reaction diagram
-
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
show the reaction diagram
-
-
-
-
-
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
show the reaction diagram
-
wild-type enzyme catalysed the reduction of benzylviologen at fourfold higher rates than the reduction of ferredoxin
-
-
?
H2 + oxidized CAC3527 ferredoxin
H+ + reduced CAC3527 ferredoxin
show the reaction diagram
-
mutant CAC3527 ferredoxin displays an almost 8fold lower reduction potential than wild type ferredoxin
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
ferredoxin links the enzyme to photosynthesis
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
2[4Fe4S] ferredoxin
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
under anoxic conditions
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Methanosarcina barkeri Fusaro
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Thermotoga maritima DSM 3109
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Megasphaera elsdenii LC1
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Tetraselmis sp. KSN-2002 NCIM 1605
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
enzyme is absolutely required for the reduction of CO2 to formylmethanofuran by H2, Ech hydrogenase provides the cell with reduced ferredoxin required as electron donor
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
enzyme activity is induced in the dark under anaerobic growth conditions
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin CAC0587
H+ + reduced ferredoxin CAC0587
show the reaction diagram
-
ferredoxin CAC0587 is the standard major ferredoxin
-
-
r
H2 + oxidized flavodoxin CAC0587
H+ + reduced flavodoxin CAC0587
show the reaction diagram
-
flavodoxin CAC0587 is the standard major flavodoxin
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
show the reaction diagram
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
S + NADPH
H2S + NADP+
show the reaction diagram
-
-
-
?
S + NADPH
H2S + NADP+
show the reaction diagram
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
show the reaction diagram
Tetraselmis sp. KSN-2002, Tetraselmis sp. KSN-2002 NCIM 1605
-
-
-
-
?
additional information
?
-
-
ferredoxin is not an efficient electron carrier for both hydrogenases
-
-
-
additional information
?
-
-
major membrane protein in acetate-grown, methanol-grown or H2/CO2-grown cells
-
-
-
additional information
?
-
-
no activity of the purified enzyme with methylene blue, NADH, NADPH and Na-dithionite as electron-donor
-
-
-
additional information
?
-
Methanosarcina barkeri Fusaro
-
major membrane protein in acetate-grown, methanol-grown or H2/CO2-grown cells
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
show the reaction diagram
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
-
-
-
r
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
Mbh function as a redox-driven ion pump coupling the reduction of protons with electrons derived from the oxidation of a low-potential ferredoxin to the generation of a H+ motive force
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
reaction is proposed to be coupled to energy conservation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
ferredoxin links the enzyme to photosynthesis
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
enzyme is absolutely required for the reduction of CO2 to formylmethanofuran by H2, Ech hydrogenase provides the cell with reduced ferredoxin required as electron donor
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Clostridium pasteurianum W5
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Methanosarcina barkeri Fusaro
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Chlamydomonas reinhardtii 137 C(+)
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
Megasphaera elsdenii LC1
-
-
-
r
additional information
?
-
Methanosarcina barkeri, Methanosarcina barkeri Fusaro
-
major membrane protein in acetate-grown, methanol-grown or H2/CO2-grown cells
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
2.1 mol per mol enzyme
FAD
-
hydrogenase II, 0.83 mol per mol heterotetramer; putative nucleotide-binding site in the gamma subunit
Ferredoxin
-
dependent
-
Ferredoxin
-
-
-
Ferredoxin
'Chlorella' fusca, Chlorococcum submarinum
-
-
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
iron-sulfur centre
-
the three [4Fe-4S] clusters simultaneously mediate electron and proton transfer and thus could be an essential part of the proton-translocating machinery
iron-sulfur centre
-
-
iron-sulfur centre
-
-
iron-sulfur centre
-
electron paramagnetic study of the light-induced species of the active site. The dissociation of the bridging CO ligand causes a major rearrangement of the sturcture of the H-cluster and large change in the distribution of the unpaired spin
NADH
-
putative nucleotide-binding site in the gamma subunit
NADPH
-
putative nucleotide-binding site in the gamma subunit
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe
-
28 mol per mol enzyme
Fe
-
31 atoms per mol
Fe
-
12 iron atoms per molecule
Fe
-
21 atoms per mol heterotetramer; five [4Fe4S] clusters, 2 in the beta subunit and 3 in the delta subunit, additionally one [2Fe2S] cluster in the gamma subunit
Fe
-
11.3 mol non-heme iron per mol enzyme
Fe
-
the catalytic site is an H-cluster, containing a [4Fe4S] subcluster and a [2Fe] center
Fe
-
the catalytic site is an H-cluster, containing a [4Fe4S] subcluster and a [2Fe] center; two ferredoxin type [4Fe4S] clusters, termed F-clusters and a catalytic H-cluster
Fe
-
4 Fe-atoms per mol hydrogenase
Fe
-
3 [4Fe4S] clusters in the small unit
Fe
-
12 iron atoms per heterodimer, one [3Fe4S] and two [4Fe4S] cluster
Fe
-
15.6 mol iron per mol enzyme
Fe
-
6.02 mol per mol enzyme
Fe
-
8 mol per mol enzyme
Fe
-
4 atoms per mol enzyme
Fe
-
three different iron-sulfur-clusters, 2 [4Fe4S]-clusters and a H-cluster
Fe
-
hydrogenase I contains 12 atoms per mol enzyme and hydrogenase II 8 atoms per mol enzyme
Fe
-
25.1 atoms per mol
Fe
-
reduced ferredoxin-type two [4Fe4S] clusters
Fe
-
12 iron atoms per molecule
Fe
-
contains [4Fe-4S] clusters
Fe
-
NiFe hydrogenase
Fe
-
Fe hydrogenase
Fe
-
the hydrogenase catalytic center H-cluster consists of a [4Fe4S]H cubane metallocluster and a [2Fe]H metallocluster
Fe
-
contains ca. 11.47 gm-atom Fe/mol, iron molecules exist as [4Fe-4S] clusters
Fe2+
-
contains 10 g atoms of Fe per mole of protein
Fe2+
-
the protein contains iron but no nickel, the active site cofactor is a unique [Fe-S] compound commonly referred to as H-cluster
Iron
-
one mol of HydA contains 7 mol iron
Ni
-
19 mol per mol enzyme
Ni
-
0.98 atoms per mol enzyme
Ni
-
1 Ni atom per mol, redox active Ni-site
Ni
-
0.9 atoms per mol heterotetramer, NiFe-catalytic site in the alpha-subunit
Ni
-
0.9 mol Ni per mol enzyme
Ni
-
1 Ni atom per mol, redox active Ni-site
Ni
-
1 atom per mol enzyme
Ni
-
0.6 mol per mol enzyme
Ni
-
0.72 mol per mol enzyme
Ni
-
0.5 mol per mol enzyme
Ni
-
NiFe hydrogenase, contains 0.9 mol Ni per mol enzyme
Ni
-
contains NiFe centers
Ni
-
NiFe hydrogenase
Ni2+
-
contains 1 g atoms of Ni per mole of protein
Se
-
0.2 mol per mol enzyme
Se
-
the large subunit contains a selenocysteine
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2'-Bipyridyl
-
66% activity at 1 mM
2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
inhibition of H2 production, photosystem 1 is involved in the supply of electrons to the hydrogenase
CO
-
strong inhibition
CO
-
both activities are inhibited
CO
-
hydrogenase I is readily inhibited, hydrogenase II is irreversibly inactivated
CO
-
at 0.5 atm 98% inhibition
CO
-
reversible competitive inhibitor versus hydrogen
CO
-
inhibition can be reversed by light
CO
Q9FYU1
exhibits reversible sensitivity to CO inhibition
CuSO4
-
inhibition of hydrogenase and selenite reduction activity
CuSO4
-
0% activity at 1 mM
EDTA
-
at 0.2 M 35% inhibition of hydrogen production and 27% inhibition of hydrogen oxidation
ethylene glycol
-
inhibitory to hydrogen production
guanidine hydrochloride
-
at 10 mM inhibitory, hydrogen production
o-phenanthroline
-
36% activity at 1 mM
O2
-
reversible inhibition
O2
-
90% inactivation after 30 min
O2
-
strong inhibition
O2
-
irreversible inactivation
O2
-
50% loss of H2 evolution activity after 3 h
O2
-
95% activity loss, few min at 4C
O2
-
50% activity loss after 2 min
O2
-
50% inactivation after 46 min, in the presence of 0.057 mM ferredoxin, after 11 h 50% inactivation
O2
-
inactivation after 1 h in aqueous solution exposed to air, 0.5 M EDTA protects, after 3 d 41% activity
O2
-
after 4 min in air 50% inactivation
O2
-
irreversible inactivation
O2
Q9FYU1
exhibits irreversible sensitivity to O2
phenylmethanesulfonyl fluoride
-
61% activity at 1 mM
Procion red
-
competitive inhibition, bidirectional hydrogenase
Sodium mersalyl
-
at 12.2 mol per mol protein, 70% inhibition
sulfo-disalicylidinepropandiamine
-
hydrogenase activity is reduced up to 30-fold
Tiron
-
inhibits methyl viologen hydrogen oxidation
Tris-HCl
-
at 30 mM inhibitory, hydrogen production
Urea
-
at 10 mM inhibitory, hydrogen production
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
HydEF protein
Q9FYU1
required for [FeFe]-hydrogenase activity
-
HydG protein
Q9FYU1
required for [FeFe]-hydrogenase activity
-
NaCl
-
up to 0.5 M, activation of methyl or benzyl viologen mediated hydrogen oxidation
rubredoxin
-
3fold increase of sulfur reductase activity at pH 7.6
Tris-HCl
-
at pH 8, activation of methyl or benzyl viologen mediated hydrogen oxidation
MgCl2
-
up to 0.5 M, activation of methyl or benzyl viologen mediated hydrogen oxidation
additional information
Q8U0Z6, Q8U0Z7, Q8U0Z8
the enzyme is activated by an incubation of 20 min at 80C under a hydrogen atmosphere
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5
-
benzyl viologen
-
-
5.7
-
benzyl viologen
-
hydrogen oxidation
36
-
benzyl viologen
-
-
2.9
-
coenzyme F420
-
-
4.8
-
factor F0
-
-
-
0.00068
-
Ferredoxin
-
-
-
0.001
-
Ferredoxin
-
-
-
0.01
-
Ferredoxin
-
hydrogen evolution
-
0.035
-
Ferredoxin
-
-
-
0.05
-
Ferredoxin
-
hydrogen evolution, hydrogenase I
-
0.13
-
Ferredoxin
-
hydrogen evolution, hydrogenase II
-
0.000033
-
H2
-
using ferredoxin CAC0587 as electron carrier, at 35C
0.000088
-
H2
-
using flavodoxin CAC0587 as electron carrier, at 35C
0.016
-
H2
-
using methyl viologen as electron carrier, at 35C
0.31
-
methyl viologen
-
hydrogen evolution, hydrogenase II
0.5
-
methyl viologen
-
-
0.8
-
methyl viologen
-
-
0.83
-
methyl viologen
-
-
1
-
methyl viologen
-
at 120 kPa H2
5
-
methyl viologen
-
hydrogen oxidation, hydrogenase I
5.7
-
methyl viologen
-
hydrogen oxidation, hydrogenase II
6.25
-
methyl viologen
-
hydrogen evolution, hydrogenase I
171
-
methyl viologen
-
hydrogen oxidation
340
-
methyl viologen
-
-
0.18
-
methylene blue
-
hydrogen oxidation, hydrogenase I
0.4
-
methylene blue
-
hydrogen oxidation, hydrogenase II
41
-
methylene blue
-
-
0.017
-
NADP+
-
-
0.0075
-
reduced ferredoxin
-
-
0.051
-
reduced ferredoxin
-
hydrogen evolution
0.72
-
reduced ferredoxin
-
-
0.57
-
reduced methyl viologen
-
-
1.25
-
reduced methyl viologen
-
-
6.25
-
reduced methyl viologen
-
hydrogen evolution
8.3
-
riboflavin
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
133
-
H2
-
using ferredoxin CAC0587 as electron carrier, at 35C
454
-
H2
-
using methyl viologen as electron carrier, at 35C
483
-
H2
-
using flavodoxin CAC0587 as electron carrier, at 35C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.004
-
-
hydrogen oxidation, benzyl viologen as electron acceptor
0.02
-
-
hydrogen production, oxidized ferredoxin as electron donor, hydrogenase II
0.107
-
-
crude extract
0.2
-
-
sulfur reduction, hydrogenase II
0.26
-
-
crude extract
0.69
-
-
hydrogen oxidation, methylene blue as electron acceptor
0.98
-
-
hydrogen production, sodium dithionite as electron donor, hydrogenase II
3.5
-
-
hydrogen production, methyl viologen as electron donor, hydrogenase II
5
-
-
hydrogen evolution
6.02
-
-
hydrogen oxidation, methylene blue as electron acceptor
7.8
-
-
hydrogen oxidation, phenosafranine as electron acceptor
9.4
-
-
hydrogen evolution, reduced methyl viologen as electron donor
11
-
-
hydrogen oxidation, methyl viologen as electron acceptor, hydrogenase II
11
-
-
hydrogen production, methylene blue as electron donor, hydrogenase I
19.8
-
-
hydrogen oxidation, benzyl viologen as electron acceptor
28
-
-
recombinant, purified enzyme
38.5
-
-
reduction of metronidiazole
40
-
-
hydrogen production, methyl viologen as electron donor, hydrogenase II
45
-
-
hydrogen production, methyl viologen as electron donor
50
-
-
hydrogen oxidation, ferredoxin as electron acceptor
50
-
-
after 467.2fold purification
53
-
-
hydrogen oxidation, methyl viologen as electron acceptor
61
-
-
hydrogen oxidation, methylene blue as electron acceptor, hydrogenase I
75.7
-
-
hydrogen evolution, reduced methyl viologen as electron donor
82.8
-
-
hydrogen mediated coenzyme F420 reduction
89
-
-
hydrogen production, methyl viologen as electron donor
90
-
-
hydrogen evolution, ferredoxin as electron donor
94
-
-
hydrogen mediated selenite reduction
96
-
-
hydrogen oxidation, benzyl viologen as electron acceptor
98.6
-
-
hydrogen oxidation, methyl viologen as electron acceptor
120
-
-
hydrogen oxidation, methyl viologen as electron acceptor
121
-
-
hydrogen oxidation
123
-
-
hydrogen oxidation, methylene blue as electron acceptor
131
-
-
hydrogen oxidation, benzyl viologen as electron acceptor, hydrogenase II
174
-
-
hydrogen oxidation, benzyl viologen as electron acceptor
210
-
-
hydrogen oxidation, benzyl viologen as electron acceptor
335
-
-
1284fold purified enzyme
391
-
-
reduction of methyl viologen
400
-
-
hydrogen oxidation, methyl viologen as electron acceptor
510
-
-
reaction with methyl viologen
700
-
-
hydrogen evolution
935
-
-
hydrogen production, reduced methyl viologen as electron donor
1260
-
-
oxidation of methyl viologen
1470
-
-
after addition of 1 M NaCl, reaction with methyl viologen
1800
-
-
hydrogen production, ferredoxin as electron donor
2998
-
-
hydrogen oxidation, methylene blue as electron acceptor, hydrogenase II
4000
-
-
hydrogen evolution, ferredoxin and 1 mM methyl viologen as electron donors
17600
-
-
hydrogen oxidation, methylene blue as electron acceptor, hydrogenase II
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
-
-
hydrogen evolution, hydrogenase II
6.3
-
-
hydrogen evolution, hydrogenase I
6.9
-
-
hydrogen evolution
7
-
-
hydrogenase II, hydrogen oxidation, methylene blue as electron acceptor
8
-
-
hydrogen oxidation
8.4
-
-
sulfur reductase activity
9.1
-
-
hydrogen evolution, hydrogenase II
9.7
-
-
hydrogen oxidation with methyl and benzyl viologen
9.8
-
-
hydrogenase I, hydrogen oxidation
10.5
-
-
hydrogenase II, hydrogen oxidation, methylene blue as electron acceptor
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
pH 6.0: about 60% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
coenzyme F420-reduction and methyl viologen reduction
60
-
-
hydrogen evolution
80
-
-
sulfur reductase activity
90
-
-
above 90C, hydrogenase II
95
-
-
above 95C, hydrogen oxidation; hydrogen evolution
95
-
-
above 95C, hydrogen oxidation
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
25C: about 65% of maximal activity, 50: about 80% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
Q8U0Z6, Q8U0Z7, Q8U0Z8
calculated from sequence
5.6
-
-
isoelectric focusing
6
-
Q8U0Z6, Q8U0Z7, Q8U0Z8
calculated from sequence
6.6
-
Q8U0Z6, Q8U0Z7, Q8U0Z8
calculated from sequence
9.6
-
-
isoelectric focusing
PDB
SCOP
CATH
ORGANISM
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44500
-
-
gel filtration and SDS-PAGE
44600
-
-
calculated from amino acid sequence
45000
-
-
gel filtration
45100
-
-
calculated from amino acid sequence
45300
-
Chlorococcum submarinum
-
calculated from amino acid sequence
45400
-
-
calculated from amino acid sequence
47300
-
-
isozyme HydA2, calculated from amino acid sequence
47500
-
-
SDS-PAGE
47500
-
-
isozyme HydA1, calculated from amino acid sequence
48000
-
-
SDS- and native PAGE
48000
-
-
isozyme HydA1, SDS-PAGE
49000
-
-
gel filtration
50000
-
-
gel filtration
52000
-
-
SDS-PAGE
53000
-
-
hydrogenase II, SDS-PAGE
53600
-
-
calculated from amino acid sequence
55000
-
-
SDS-PAGE
55000
-
-
gel filtration
57000
-
-
gel filtration
60000
-
-
gel filtration, hydrogenase I
60500
-
-
SDS-PAGE
63800
-
-
calculated from amino acid sequence
64300
-
-
calculated from amino acid sequence
89000
-
-
SDS-PAGE
98000
-
-
gel filtration
100000
-
-
native PAGE
110000
-
-
native Ehb complex, gel filtration
122000
-
-
native PAGE
130000
-
-
gel filtration
185000
-
-
gel filtration
198000
-
-
native PAGE
320000
-
-
gel filtration
360000
-
-
Ehb complex, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 69000 + x * 40000, + x * 32000, + x * 17000 + x + 14100 + x * 14700, SDS-PAGE
?
Q8U0Z6, Q8U0Z7, Q8U0Z8
x * 18284, calculated from sequence; x * 20184, calculated from sequence; x * 47934, calculated from sequence
dimer
-
alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
dimer
-
1 * 49000 + 1 * 26000, SDS-PAGE
dimer
-
1 * 66400 + 1 * 32300, SDS-PAGE
dimer
-
1 * 65000 + 1 * 37000, SDS-PAGE
dimer
-
1 * 64000 + 1 * 34000, SDS-PAGE
dimer
-
alpha, beta, 1 * 57000 + 1 * 35000, SDS-PAGE
dimer
-
2 * 30000, hydrogenase I, SDS-PAGE
dimer
Acidithiobacillus ferrooxidans ATC 19859
-
1 * 64000 + 1 * 34000, SDS-PAGE
-
dimer
Clostridium pasteurianum W5
-
2 * 30000, hydrogenase I, SDS-PAGE
-
dimer
Desulfovibrio vulgaris Hildenborough ATCC 29579
-
1 * 66400 + 1 * 32300, SDS-PAGE
-
dimer
-
alpha, beta, 1 * 57000 + 1 * 35000, SDS-PAGE
-
heterodimer
-
1 * 19000 + 1 * 70000, SDS-PAGE
heterodimer
-
1 * 46100 + 1 * 14000, calculated from amino acid sequence
heterodimer
Tetraselmis sp. KSN-2002 NCIM 1605
-
1 * 19000 + 1 * 70000, SDS-PAGE
-
hexamer
-
alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 53000, hydrogenase II, SDS-PAGE
monomer
-
1 * 50000, gel filtration and SDS-PAGE, 1 * 50800, mass spectrometry
monomer
Thermotoga maritima DSM 3109
-
-
-
octamer
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
pentamer
-
alpha, beta, gamma, 2 * 48000 + 2 * 33000 + 1 * 30000, SDS-PAGE
pentamer
Methanosarcina barkeri Fusaro
-
alpha, beta, gamma, 2 * 48000 + 2 * 33000 + 1 * 30000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2.15 A resolution, reduced, active form
-
crystals of the soluble form obtained using 20% polyethylene glycol 1500 as a precipitant, which belong to the monoclinic space group P21, with unit-cell parameters a = 60.57, b = 91.05, c = 66.85 A, beta = 101.46, to 2.4 A resolution. No crystals appear for the membrane form
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
50% inactivation after 14 d
55
-
-
50% inactivation after 1 h
95
-
-
50% inactivation after 6 h, hydrogenase II
100
-
-
most of activity is retained after 1 h incubation
100
-
-
50% inactivation after 30 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after treatment with 4 mM urea, 100% activity after several hours
-
chelating agents protect against oxygen inactivation, 0.5 M EDTA allows 41% activity after 3 d in aqueous solution exposed to air
-
in aqueous solutions at pH 8.0, under argon, nitrogen or hydrogen atmosphere, stable for many hours
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
rapid inactivation under aerobic conditions
-
439665, 439672
air inactivation is reduced up to 25fold by adsoption on common anion exchange supports like DEAE cellulose, 3 mM Tris-HCl buffer pH 8
-
439680
rapid inactivation under aerobic conditions
-
439675
rapid inactivation under aerobic conditions
-
439643
rapid inactivation under aerobic conditions
-
439652
rapid inactivation under aerobic conditions
-
439650
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, several months, strictly anaerobical storage, little loss of activity
-
-80C, several weeks, strictly anaerobical storage
-
5C, 5 d, strictly anaerobical storage
-
-180C, 4 months, 100% activity
-
crystals are stabilized with glycerol and stored under strict anaerobic conditions or in liquid nitrogen after flash-cooling
-
4C, under argon, 50% activity loss, 2 weeks
-
-20C, 3 d, 50% coenzyme F420 reducing activity
-
0C, aerobical storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Q-sepharose HiLoad, hydroxyapatite, Superdex 200
-
affinity column chromatography with immobilised ferredoxin
-
partially, 40% pure
-
Ni-Sepharose 6 Fast Flow chromatography
-
Procion Red-agarose purification
-
aerobically purified hydrogenase is inactive and requires reductive activation
-
aerobically using different ion-exchange chromatography columns
-
1284fold with a yield of 16.17%, by ultracentrifugation, ion exchange chromatography, gel filtration and hydrophobic-interaction chromatography
-
aerobic purification
-
under anaerobic conditions, solubilized with n-dodecyl-beta-D-maltoside
-
strictly under anaerobic conditions
-
purified under aerobic conditions, requires reductive activation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
activation and de novo synthesis of the protein is inhibited by cycloheximide but not chloramphenicol
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D102K
-
leads to lower binding free energies and higher association rate with [2Fe2S]-ferredoxin FDX1 and is thus a promising target for improving hydrogen production rates in engineered organisms
D102K/E221K
-
double mutant enhances association rate constant
D102K/T99K
-
double mutant enhances association rate constant
E221K
-
higher association rate with [2Fe2S]-ferredoxin FDX1
M214K
-
least enhancement of association rate with [2Fe2S]-ferredoxin FDX1, destabilizes binding complexes
T99K
-
leads to lower binding free energies and higher association rate with [2Fe2S]-ferredoxin FDX1 and is thus a promising target for improving hydrogen production rates in engineered organisms
C42S
-
mutant enzyme with almost no activity in the reaction with H2 and oxidized benzyl viologen
C45S
-
mutants with about 5% of the wild-type activity in the reaction with H2 and oxidized benzyl viologen
C48S
-
mutant enzyme with almost no activity in the reaction with H2 and oxidized benzyl viologen
C73S
-
mutants with about 5% of the wild-type activity in the reaction with H2 and oxidized benzyl viologen
C76S
-
mutant enzyme with almost no activity in the reaction with H2 and oxidized benzyl viologen
C79S
-
mutants with about 5% of the wild-type activity in the reaction with H2 and oxidized benzyl viologen
C83S
-
mutant enzyme with approximately 10% of the activity of the wild-type enzyme in the reaction with H2 and oxidized benzyl viologen
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
practical application in solar energy bioconversion