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Literature summary extracted from

  • Hunte, C.; Solmaz, S.; Lange, C.
    Electron transfer between yeast cytochrome bc1 complex and cytochrome c: a structural analysis (2002), Biochim. Biophys. Acta, 1555, 21-28.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.1.1.8 crystallization of the enzyme cytochrome bc1 complex with mitochondrial cytochrome c and the antibody fragment FV18E11, protein solution with 120 mM ionic strength is rapidly mixed with precipitation solution containing 12% PEG 4000, 20 mM Tris-HCl, pH 7.5, hanging drop vapour diffusion method, 3 weeks at 4°C, X-ray diffraction structure determination and analysis, modeling Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.8 additional information
-
 additional information kinetics Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.8 membrane integral Saccharomyces cerevisiae 16020
-
7.1.1.8 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Metals/Ions

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

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 + 2 ferricytochrome c Saccharomyces cerevisiae electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.8 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] binding structure and mode of cytochrome c1 within the enzyme complex and cytochrome c during the catalytic reaction, direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c, half-of-the sites mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c activity is highest near physiological ionic strength and decreases at higher concentrations Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.8 dimer complex composition, binding structure of cytochromes, crystal structure, overview Saccharomyces cerevisiae

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.1.1.8 25
-
 assay at 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 additional information
-
 additional information rate of direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.8 7.4
-
 assay at Saccharomyces cerevisiae