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Literature summary for 1.12.2.1 extracted from

  • Aubert, C.; Brugna, M.; Dolla, A.; Bruschi, M.; Giudici-Orticoni, M.T.
    A sequential electron transfer from hydrogenases to cytochromes in sulfate-reducing bacteria (2000), Biochim. Biophys. Acta, 1476, 85-92.
    View publication on PubMed
Search for more literature for 1.12.2.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0368
-
 ferricytochrome c3
-
 Desulfomicrobium norvegicum

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Desulfomicrobium norvegicum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
 Desulfovibrio vulgaris
Iron [NiFeSe] hydrogenase Desulfomicrobium norvegicum
Nickel
-
 Desulfovibrio vulgaris
Nickel [NiFeSe] hydrogenase Desulfomicrobium norvegicum
selenium [NiFeSe] hydrogenase Desulfomicrobium norvegicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Desulfomicrobium norvegicum cytochrome c3 is the natural electron acceptor ?
-
 ?

Organism

Organism UniProt Comment Textmining
Desulfomicrobium norvegicum
-
-
-
Desulfovibrio vulgaris
-
 Hildenborough
-
Desulfovibrio vulgaris Hildenborough
-
 Hildenborough
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + ferricytochrome c3
-
 Desulfovibrio vulgaris H+ + ferrocytochrome c3
-
 ?
H2 + ferricytochrome c3
-
 Desulfomicrobium norvegicum H+ + ferrocytochrome c3
-
 ?
H2 + ferricytochrome c3
-
 Desulfovibrio vulgaris Hildenborough H+ + ferrocytochrome c3
-
 ?
additional information cytochrome c3 is the natural electron acceptor Desulfomicrobium norvegicum ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
38
-
 ferricytochrome c3
-
 Desulfomicrobium norvegicum
490
-
 ferricytochrome c3
-
 Desulfovibrio vulgaris

Cofactor

Cofactor Comment Organism Structure
cytochrome c3 the electron transfer between [NiFeSe] hydrogenase and octaheme cytochrome c3 is activated by tetraheme cytochrome c3, cytochrome c3 can acts as an electron shuttle between hydrogenase and polyheme cytochromes Desulfovibrio vulgaris
cytochrome c3 the electron transfer between [NiFeSe] hydrogenase and octaheme cytochrome c3 is activated by tetraheme cytochrome c3, cytochrome c3 can acts as an electron shuttle between hydrogenase and polyheme cytochromes Desulfomicrobium norvegicum