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Literature summary extracted from

  • Francia, F.; Malferrari, M.; Lanciano, P.; Steimle, S.; Daldal, F.; Venturoli, G.
    The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1 (2016), Biochim. Biophys. Acta, 1857, 1796-1806 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.8 H291L the mutant shows reduced activity compared to the wild type enzyme Rhodobacter capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.8 membrane
-
Rhodobacter capsulatus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.8 Zn2+ the enzyme contains zinc binding sites Rhodobacter capsulatus

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.8 Rhodobacter capsulatus
-
-
-
7.1.1.8 Rhodobacter capsulatus MT-RBC1
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 decylbenzohydroquinol + ferricytochrome c
-
Rhodobacter capsulatus decylbenzohydroquinone + ferrocytochrome c + H+
-
?
7.1.1.8 decylbenzohydroquinol + ferricytochrome c
-
Rhodobacter capsulatus MT-RBC1 decylbenzohydroquinone + ferrocytochrome c + H+
-
?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.8 cytochrome c
-
Rhodobacter capsulatus