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Literature summary extracted from

  • McEwan, A.G.; Richardson, D.J.; Jackson, J.B.; Ferguson, S.J.
    The periplasmic nitrate reductase and trimethylamine N-oxide reductase of the photosynthetic bacterium Rhodobacter capsulatus (1988), Biochem. Soc. Trans., 16, 182-183.
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.2.3 periplasm
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 Rhodobacter capsulatus
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-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.3 80000
-
 SDS-PAGE Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.3 trimethylamine-N-oxide + electron donor Rhodobacter capsulatus cytochrome c-556 may be the physiological electron donor trimethylamine + oxidized electron donor + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 Rhodobacter capsulatus
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 a single enzyme responsible for both trimethylamine-N-oxide and dimethylsulfoxide reductase
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 chlorate + electron donor
-
 Rhodobacter capsulatus ?
-
 ?
1.7.2.3 additional information a single enzyme responsible for both trimethylamine N-oxide and dimethylsulfoxide reductase Rhodobacter capsulatus ?
-
 ?
1.7.2.3 trimethylamine-N-oxide + electron donor cytochrome c-556 may be the physiological electron donor Rhodobacter capsulatus trimethylamine + oxidized electron donor + H2O
-
 ?