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Literature summary extracted from

  • Kessl, J.J.; Ha, K.H.; Merritt, A.K.; Lange, B.B.; Hill, P.; Meunier, B.; Meshnick, S.R.; Trumpower, B.L.
    Cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae (2005), J. Biol. Chem., 280, 17142-17148.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.8 F278I site-directed mutagenesis, the mutation does not affect the residues of the EF helix of cytochrome b, the mutant shows similar ubiquinol-binding as the wild-type complex Saccharomyces cerevisiae
7.1.1.8 I269M site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex Saccharomyces cerevisiae
7.1.1.8 L282V site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone Saccharomyces cerevisiae
7.1.1.8 additional information cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes, overview Saccharomyces cerevisiae
7.1.1.8 Y279C site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone Saccharomyces cerevisiae
7.1.1.8 Y279S site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.8 atovaquone an anti-malarial agent that specifically targets the cytochrome bc1 complex and inhibits parasite respiration in vivo, mutants Y279S, Y279C, and L282V are resistant to the inhibition, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.8 0.008
-
QH2 pH 7.0, 23°C, mutant I269M Saccharomyces cerevisiae
7.1.1.8 0.013
-
QH2 pH 7.0, 23°C, wild-type enzyme and mutant F278I Saccharomyces cerevisiae

Localization

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

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c ubiquinol binds to the specific binding pocket of the cytochrome bc1 complex Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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Subunits

EC Number Subunits Comment Organism
7.1.1.8 More modeling the variations in cytochrome b structure with the mutated bc1 complexes Saccharomyces cerevisiae

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.1.1.8 23
-
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 10
-
QH2 pH 7.0, 23°C, mutant Y279C Saccharomyces cerevisiae
7.1.1.8 15
-
QH2 pH 7.0, 23°C, mutant L282V Saccharomyces cerevisiae
7.1.1.8 20
-
QH2 pH 7.0, 23°C, mutant Y279S Saccharomyces cerevisiae
7.1.1.8 30
-
QH2 pH 7.0, 23°C, mutant I269M Saccharomyces cerevisiae
7.1.1.8 220
-
QH2 pH 7.0, 23°C, wild-type enzyme and mutant F278I Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.8 7
-
assay at Saccharomyces cerevisiae