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Literature summary extracted from

  • Odom, J.M.; Peck, H.D.
    Hydrogenase, electron-transfer proteins, and energy coupling in the sulfate-reducing bacteria Desulfovibrio (1984), Annu. Rev. Microbiol., 38, 551-592.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.2.1 CO reversible Desulfovibrio desulfuricans
1.12.2.1 CO reversible Desulfovibrio vulgaris
1.12.2.1 CO
-
Megalodesulfovibrio gigas
1.12.2.1 O2 reversible inactivation Desulfovibrio desulfuricans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.12.2.1 membrane bound to Desulfovibrio desulfuricans 16020
-
1.12.2.1 periplasm
-
Desulfovibrio desulfuricans
-
-
1.12.2.1 periplasm
-
Megalodesulfovibrio gigas
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.2.1 Iron nonheme iron protein Megalodesulfovibrio gigas
1.12.2.1 Iron 12.5 gatom nonheme iron and 11.5 gatom of acid-labile sulfide per mol, arranged in at least two Fe4S4 clusters of the ferredoxin type Desulfovibrio vulgaris
1.12.2.1 Iron presence of a three-iron center Desulfovibrio desulfuricans
1.12.2.1 Iron 11-12 gatom of nonheme iron per molecule Megalodesulfovibrio gigas
1.12.2.1 Nickel
-
Desulfovibrio desulfuricans
1.12.2.1 Nickel 1 gatom of nickel per molecule Megalodesulfovibrio gigas
1.12.2.1 Nickel purified enzyme contains variable amounts of nickel, ranging from 0.1 to 0.6 gatom per mol of enzyme Desulfovibrio vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.12.2.1 26000
-
x * 26000 + x * 62000 Megalodesulfovibrio gigas
1.12.2.1 58000
-
-
Desulfovibrio desulfuricans
1.12.2.1 62000
-
x * 26000 + x * 62000 Megalodesulfovibrio gigas
1.12.2.1 89500
-
-
Megalodesulfovibrio gigas

Organism

EC Number Organism UniProt Comment Textmining
1.12.2.1 Desulfovibrio desulfuricans
-
Norway 4
-
1.12.2.1 Desulfovibrio desulfuricans Norway 4
-
Norway 4
-
1.12.2.1 Desulfovibrio vulgaris
-
Hildenborough
-
1.12.2.1 Desulfovibrio vulgaris Hildenborough
-
Hildenborough
-
1.12.2.1 Megalodesulfovibrio gigas
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.12.2.1 long exposure of the oxidized enzyme to oxygen does not irreversibly inactivate the hydrogenase. In the reduced form the hydrogenase is irreveribly inactivated Desulfovibrio vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.2.1 H2 + ferredoxin requires the presence of cytochrome c3 for the reduction of ferredoxin Megalodesulfovibrio gigas H+ + reduced ferredoxin
-
?
1.12.2.1 H2 + ferricytochrome c3
-
Desulfovibrio desulfuricans H+ + ferrocytochrome c3
-
?
1.12.2.1 H2 + ferricytochrome c3
-
Desulfovibrio vulgaris H+ + ferrocytochrome c3
-
?
1.12.2.1 H2 + ferricytochrome c3
-
Megalodesulfovibrio gigas H+ + ferrocytochrome c3
-
?
1.12.2.1 H2 + ferricytochrome c3
-
Desulfovibrio desulfuricans Norway 4 H+ + ferrocytochrome c3
-
?
1.12.2.1 H2 + ferricytochrome c3
-
Desulfovibrio vulgaris Hildenborough H+ + ferrocytochrome c3
-
?
1.12.2.1 H2 + rubredoxin requires the presence of cytochrome c3 for the reduction of rubredoxin Megalodesulfovibrio gigas H+ + reduced rubredoxin
-
?

Subunits

EC Number Subunits Comment Organism
1.12.2.1 ? x * 26000 + x * 62000 Megalodesulfovibrio gigas

Cofactor

EC Number Cofactor Comment Organism Structure
1.12.2.1 cytochrome c3
-
Desulfovibrio desulfuricans
1.12.2.1 cytochrome c3
-
Desulfovibrio vulgaris
1.12.2.1 cytochrome c3 requires the presence of cytochrome c3 for the reduction of ferredoxin, rubredoxin and cytochrome c3 Megalodesulfovibrio gigas