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Literature summary extracted from

  • Palsdottir, H.; Lojero, C.G.; Trumpower, B.L.; Hunte, C.
    Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound (2003), J. Biol. Chem., 278, 31303-31311.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.1.1.8 purified enzyme with inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole bound, microseeding and vapour diffusion method, protein solution contains 50 mg/ml protein, mixing with precipitant solution containing 5% PEG 4000, Tris-HCl, pH 7.5, 0.05% n-undecyl-beta-D-maltopyranoside, 0.01 mM 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole, room temperature, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.8 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole competitive, structure of the enzyme with the hydroxyquinone anion Qo site inhibitor bound, binding mechanism Saccharomyces cerevisiae
7.1.1.8 5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
-
 Saccharomyces cerevisiae
7.1.1.8 methoxyacrylate stilbene
-
 Saccharomyces cerevisiae
7.1.1.8 myxothiazole
-
 Saccharomyces cerevisiae
7.1.1.8 n-alkyl-6-hydroxy-4,7-dioxobenzothiazole length of side chain 7-15 carbon atoms Saccharomyces cerevisiae
7.1.1.8 Stigmatellin
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.8 membrane
-
 Saccharomyces cerevisiae 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.8 Iron enzyme contains a Rieske [2Fe-2S] cluster required for activity Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.8 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.8 active enzyme to homogeneity Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
7.1.1.8 quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] reaction and substrate binding mechanism, overview, conformational changes at the binding site of inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole confirm the proton transfer pathway and reveal plasticity at the active site Saccharomyces cerevisiae
a

Synonyms

EC Number Synonyms Comment Organism
7.1.1.8 cytochrome bc1 complex
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.8 82
-
 cytochrome c purified enzyme Saccharomyces cerevisiae