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Enzyme Nomenclature
Information on EC 1.12.1.4 - hydrogenase (NAD+, ferredoxin)
for references in articles please use BRENDA:EC1.12.1.4
Word Map on EC 1.12.1.4
- 1.12.1.4
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desulfovibrio
- desulfuricans
- fructosovorans
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dinuclear
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nickel-iron
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diiron
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The expected taxonomic range for this enzyme is: Bacteria
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EC NUMBER 
COMMENTARY 
1.12.1.4
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RECOMMENDED NAME
GeneOntology No.
hydrogenase (NAD+, ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 H2 + NAD+ + 2 oxidized ferredoxin = 5 H+ + NADH + 2 reduced ferredoxin
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:NAD+, ferredoxin oxidoreductase
The enzyme from Thermotoga maritima contains a [FeFe] cluster (H-cluster) and iron-sulfur clusters. It works in the direction evolving hydrogen as a means of eliminating excess reducing equivalents.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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an active HydF GTPase domain is essential to produce a functional [FeFe]-hydrogenase
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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
NAD+ + 2 oxidized methyl viologen + 2 H2
NADH + 3 H+ + 2 reduced methyl viologen
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-
-
-
?
NADH + 3 H+ + 2 reduced ferredoxin
NAD+ + 2 oxidized ferredoxin + 2 H2
-
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per mol NADH, about 2 mol H2 is formed
-
?
NADH + 3 H+ + 2 reduced methyl viologen
NAD+ + 2 oxidized methyl viologen + 2 H2
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-
-
-
?
NADH + H+ + reduced methyl viologen
H2 + NAD+ + oxidized methyl viologen
-
-
-
-
?
sodium dithionite + H+ + reduced anthraquinone-2,6-disulfonic acid
H2 + oxidized anthraquinone-2,6-disulfonic acid + ?
H2 + NAD+ + oxidized ferredoxin
H+ + NADH + reduced ferredoxin
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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-
-
-
?
NAD+ + 2 oxidized ferredoxin + 2 H2
NADH + 3 H+ + 2 reduced ferredoxin
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ferredoxin reduction with H2 is driven by the exergonic reduction of NAD+ (E0 -320 mV) with H2. In the absence of NAD+, ferredoxin is not reduced
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?
NAD+ + 2 oxidized ferredoxin + 2 H2
NADH + 3 H+ + 2 reduced ferredoxin
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-
-
-
?
NAD+ + 2 oxidized ferredoxin + 2 H2
NADH + 3 H+ + 2 reduced ferredoxin
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-
-
-
?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
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the iron hydrogenase requires the presence of both electron carriers, NADH and ferredoxin, for catalysis of H2 production
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-
?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
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the iron hydrogenase requires the presence of both electron carriers, NADH and ferredoxin, for catalysis of H2 production
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-
?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
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-
-
-
?
sodium dithionite + H+ + reduced anthraquinone-2,6-disulfonic acid
H2 + oxidized anthraquinone-2,6-disulfonic acid + ?
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-
-
-
?
sodium dithionite + H+ + reduced anthraquinone-2,6-disulfonic acid
H2 + oxidized anthraquinone-2,6-disulfonic acid + ?
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-
-
-
?
sodium dithionite + H+ + reduced methyl viologen
H2 + oxidized methyl viologen + ?
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-
-
-
?
sodium dithionite + H+ + reduced methyl viologen
H2 + oxidized methyl viologen + ?
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-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + NAD+ + oxidized ferredoxin
H+ + NADH + reduced ferredoxin
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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-
-
-
?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
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the iron hydrogenase requires the presence of both electron carriers, NADH and ferredoxin, for catalysis of H2 production
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-
?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
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the iron hydrogenase requires the presence of both electron carriers, NADH and ferredoxin, for catalysis of H2 production
-
-
?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4Fe-4S-center
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displays electron paramagnetic resonance signals characteristic of oxidized [3Fe-4S]+ cluster. Cysteine residues C302, C353, and C356 are strictly required for the binding of the [4Fe-4S] cluster, whereas the fourth ligand of the coordination sphere can vary depending on the molecular environment created by local residues and/or experimental conditions
iron-sulfur centre
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the alpha subunit contains two [2Fe-2S] clusters and three [4Fe-4S] clusters, the beta subunit contains three [4Fe-4S] clusters and one [2Fe-2S] clusters, the gamma subunit contains one [2Fe-2S] cluster
iron-sulfur centre
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subunit HydA (63 kDa) is predicted to harbor the H cluster, i.e., the [6Fe4S] hydrogenase active site, three [4Fe4S] clusters, and one [2Fe2S] cluster. Subunit HydB (67 kDa) is predicted to harbor three [4Fe4S] clusters, a flavin binding site, and an NAD binding site. HydC (17 kDa) is predicted to harbor one [2Fe2S] cluster
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
H2
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apparent Km value for H2 is about 6% in the gas phase, pH 7.5, 45°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18025
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1 * 72248 + 1 * 68676 + 1 * 18025, calculated from amino acid sequence
68000
68676
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1 * 72248 + 1 * 68676 + 1 * 18025, calculated from amino acid sequence
72248
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1 * 72248 + 1 * 68676 + 1 * 18025, calculated from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterohexamer
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2 * 67000, subunit HydB, plus 2 * 63000, subunit HydA, plus 2 * 17000, subunit HydC, SDS-PAGE
heterotrimer
multimer
heterotrimer
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1 * 72248 + 1 * 68676 + 1 * 18025, calculated from amino acid sequence; 1 * 73000 + 1 * 68000 + 1 * 19000, SDS-PAGE
heterotrimer
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; 1 * 72248 + 1 * 68676 + 1 * 18025, calculated from amino acid sequence; 1 * 73000 + 1 * 68000 + 1 * 19000, SDS-PAGE
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multimer
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x * 68000, subunit HdB, plus x * 64000, subunit HydA, plus x * 18000, subunit HydC
multimer
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x * 68000, subunit HdB, plus x * 64000, subunit HydA, plus x * 18000, subunit HydC
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, hydroxyapatite column chromatography, phenyl-Sepharose column chromatography, and Superdex 200 gel filtration
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nickel affinity column chromatography and Superdex 200 gel filtration
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nickel affinity column chromatography, and Superose 12 gel filtration
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under strictly anoxic conditions, the enzyme is inactivated in the presence of even trace amounts of O2
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A85P
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the mutant has an altered reduction potential compared to the wild type enzyme
V131N
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the mutant has an altered reduction potential compared to the wild type enzyme
A85P
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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the mutant has an altered reduction potential compared to the wild type enzyme
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V131N
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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the mutant has an altered reduction potential compared to the wild type enzyme
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C302S
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mutant displays a very weak electron paramagnetic resonance signal
C353S
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mutant displays a very weak electron paramagnetic resonance signal
C356S
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mutant displays a very weak electron paramagnetic resonance signal
H304A
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similar to wild-type, mutant exhibits electron paramagnetic resonance signals characteristic of oxidized [3Fe-4S]+ cluster
H352A
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similar to wild-type, mutant exhibits electron paramagnetic resonance signals characteristic of oxidized [3Fe-4S]+ cluster
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LINKS TO OTHER DATABASES (specific for EC-Number 1.12.1.4)
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