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Literature summary for 7.1.1.8 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
Search for more literature for 7.1.1.8

Protein Variants

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

Localization

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-
Rhodobacter capsulatus MT-RBC1
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
 Rhodobacter capsulatus