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Literature summary for 1.12.2.1 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

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron nonheme iron protein Megalodesulfovibrio gigas
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
Iron presence of a three-iron center Desulfovibrio desulfuricans
Iron 11-12 gatom of nonheme iron per molecule Megalodesulfovibrio gigas
Nickel
-
Desulfovibrio desulfuricans
Nickel 1 gatom of nickel per molecule Megalodesulfovibrio gigas
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]

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

Organism

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

Oxidation Stability

Oxidation Stability Organism
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)

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

Subunits

Subunits Comment Organism
? x * 26000 + x * 62000 Megalodesulfovibrio gigas

Cofactor

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