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Literature summary extracted from

  • Mulkidjanian, A.
    Activated Q-cycle as a common mechanism for cytochrome bc1 and cytochrome b6f complexes (2010), Biochim. Biophys. Acta, 1797, 1858-1868.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.1.1.6 additional information the bf complex, however, can be dark-activated via reduction of heme cn by ferredoxin Rhodobacter capsulatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.6 (E)-beta-methoxyacrylate stilbene weak inhibition, retards concurrently the flashinduced re-reduction of cytochrome f, the oxidation of cytochrome b6 and the onset of voltage generation, thereby hardly affecting the rate of the flash-induced cytochrome b6 reduction and the steady turnover of the bf Rhodobacter capsulatus
7.1.1.6 2-n-Nonyl-4-hydroxyquinoline N-oxide weak inhibition, retards concurrently the flashinduced re-reduction of cytochrome f, the oxidation of cytochrome b6 and the onset of voltage generation, thereby hardly affecting the rate of the flash-induced cytochrome b6 reduction and the steady turnover of the bf Rhodobacter capsulatus

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.6 Zn2+ concurrent action of Zn2+ ions on the re-reduction of cytochrome c1 by the Rieske protein, voltage generation, and proton release from the bc1 Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.6 plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] Rhodobacter capsulatus
-
 plastoquinone + 2 reduced plastocyanin + 2 H+[side 2]
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.6 plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1]
-
 Rhodobacter capsulatus plastoquinone + 2 reduced plastocyanin + 2 H+[side 2]
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.6 dimer
-
 Rhodobacter capsulatus

Synonyms

EC Number Synonyms Comment Organism
7.1.1.6 cytochrome b6 f complex
-
 Rhodobacter capsulatus
7.1.1.6 quinol:plastocyanin oxidoreductase
-
 Rhodobacter capsulatus

General Information

EC Number General Information Comment Organism
7.1.1.6 evolution cytochrome bc1-complexes of animals and bacteria, as well as related cytochrome b6 f complexes of plants and cyanobacteria are dimeric quinol:cytochrome c/plastocyanin oxidoreductases capable of translocating protons across energy-converting membranes. These enzymes oxidize two quinolmolecules in their catalytic centers P to yield one quinol molecule in another catalytic center N. The simplest cytochrome bc1-complexes of Rhodobacter capsulatus, which contains only 3 subunits, matches the structure of the three catalytic subunits of mitochondrial bc1 Rhodobacter capsulatus
7.1.1.6 additional information Q-cycle in the cytochrome bc1 complex using the X-ray structure of the three catalytic subunits of a dimeric bc1 of phototrophic bacteria, i.e. the X-ray structure of the bc1 of Rhodobacter sphaeroides, PDB entry 2QJY, modificationss of Mitchell's Q-cycle, detailed overview Rhodobacter capsulatus
7.1.1.6 physiological function the subunit IV binds single molecules of chlorophyll alpha and beta-carotene, which are likely to be involved in photoprotection Rhodobacter capsulatus