Information on EC 1.12.1.4 - hydrogenase (NAD+, ferredoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.12.1.4
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RECOMMENDED NAME
GeneOntology No.
hydrogenase (NAD+, ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 H2 + NAD+ + 2 oxidized ferredoxin = 5 H+ + NADH + 2 reduced ferredoxin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hydrogen production I
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + 2 oxidized ferredoxin + 2 H2
NADH + 3 H+ + 2 reduced ferredoxin
show the reaction diagram
NAD+ + 2 oxidized methyl viologen 2 H2
NADH + 3 H+ + 2 reduced methyl viologen
show the reaction diagram
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?
NADH + 3 H+ + 2 reduced ferredoxin
NAD+ + 2 oxidized ferredoxin + 2 H2
show the reaction diagram
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per mol NADH, about 2 mol H2 is formed
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?
NADH + 3 H+ + 2 reduced methyl viologen
NAD+ + 2 oxidized methyl viologen + 2 H2
show the reaction diagram
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?
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
show the reaction diagram
NADH + H+ + reduced methyl viologen
H2 + NAD+ + oxidized methyl viologen
show the reaction diagram
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?
sodium dithionite + H+ + reduced anthraquinone-2,6-disulfonic acid
H2 + oxidized anthraquinone-2,6-disulfonic acid + ?
show the reaction diagram
sodium dithionite + H+ + reduced methyl viologen
H2 + oxidized methyl viologen + ?
show the reaction diagram
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
NADH + H+ + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
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no cofactor: NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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the holoprotein contains 31.1 mol iron per mol enzyme
Iron
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purified enzyme contains 31 irons and 0.8 FMN per heterotrimer
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
NAD+
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pH 7.5, 45°C
additional information
H2
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apparent Km value for H2 is about 6% in the gas phase, pH 7.5, 45°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
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oxidation of ferredoxin, pH 7.5, 45°C
57.5
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reduction of ferredoxin, pH 7.5, 45°C
60
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pH 7.0, 37°C
195
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reduction of methyl viologen, pH 7.5, 45°C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18025
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1 * 72248 + 1 * 68676 + 1 * 18025, calculated from amino acid sequence
19000
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1 * 73000 + 1 * 68000 + 1 * 19000, SDS-PAGE
68000
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1 * 73000 + 1 * 68000 + 1 * 19000, SDS-PAGE
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
73000
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1 * 73000 + 1 * 68000 + 1 * 19000, SDS-PAGE
158900
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gel filtration
160000
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calculated from amino acid sequence
300000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
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2 * 67000, subunit HydB, plus 2 * 63000, subunit HydA, plus 2 * 17000, subunit HydC, SDS-PAGE
heterotrimer
multimer
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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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
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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