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Literature summary extracted from

  • Mulkidjanian, A.Y.
    Proton translocation by the cytochrome bc1 complexes of phototrophic bacteria: introducing the activated Q-cycle (2007), Photochem. Photobiol. Sci., 6, 19-34.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.8 Iron contains [2Fe–2S] cluster Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.8 ubiquinol + 2 ferricytochrome c Rhodobacter capsulatus
-
 ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.8 Rhodobacter capsulatus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 ubiquinol + 2 ferricytochrome c
-
 Rhodobacter capsulatus ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?
7.1.1.8 ubiquinol + 2 ferricytochrome c under physiological conditions, the dimeric cytochrome bc1 complex is suggested to be continually primed by prompt oxidation of membrane ubiquinol via center N yielding a bound semiquinone in this center and a reduced, high-potential heme b in the other monomer of the enzyme. Then the oxidation of each ubiquinol molecule in center P is followed by ubiquinol formation in center N, proton translocation and generation of membrane voltage Rhodobacter capsulatus ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.1.1.8 cytochrome bc1 complex
-
 Rhodobacter capsulatus
7.1.1.8 ubiquinol:cytochrome c oxidoreductase
-
 Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.8 cytochrome b
-
 Rhodobacter capsulatus
7.1.1.8 cytochrome c1
-
 Rhodobacter capsulatus