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Literature summary extracted from

  • Ding, M.G.; di Rago, J.P.; Trumpower, B.L.
    Investigating the Qn site of the cytochrome bc1 complex in Saccharomyces cerevisiae with mutants resistant to ilicicolin H, a novel Qn site inhibitor (2006), J. Biol. Chem., 281, 36036-36043.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.8 cytochrome b gene, DNA sequence determination of wild-type and mutant strains Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.8 G37D site-directed mutagenesis, the mutation is located on exon 1, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows normal growth Saccharomyces cerevisiae
7.1.1.8 G37S site-directed mutagenesis, the mutation is located on exon 1, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows impaired growth Saccharomyces cerevisiae
7.1.1.8 L198F site-directed mutagenesis, the mutation is located on exon 4, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows normal growth Saccharomyces cerevisiae
7.1.1.8 additional information construction of several mutants, some of which are resistant to center N site enzyme inhibitors, such as ilicicolin H or antimycin, genomic structure of mutants, effects of the cytochrome b mutations on respiratory growth and cross-resistance to other Qn site inhibitors, overview Saccharomyces cerevisiae
7.1.1.8 Q22E site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth Saccharomyces cerevisiae
7.1.1.8 Q22T site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth Saccharomyces cerevisiae
7.1.1.8 S20L site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows impaired growth Saccharomyces cerevisiae
7.1.1.8 S20T site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.8 Antimycin a Qn site inhibitor Saccharomyces cerevisiae
7.1.1.8 funiculosin a Qn site inhibitor Saccharomyces cerevisiae
7.1.1.8 ilicicolin H a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.8 mitochondrial inner membrane
-
 Saccharomyces cerevisiae 5743
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.8 ubiquinol + ferricytochrome c Saccharomyces cerevisiae the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively ubiquinone + ferrocytochrome c
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.8 Saccharomyces cerevisiae
-
 wild-type strain W303-1B
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 decylubiquinol + ferricytochrome c
-
 Saccharomyces cerevisiae decylubiquinone + ferrocytochrome c
-
 ?
7.1.1.8 ubiquinol + ferricytochrome c
-
 Saccharomyces cerevisiae ubiquinone + ferrocytochrome c
-
 ?
7.1.1.8 ubiquinol + ferricytochrome c the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively Saccharomyces cerevisiae ubiquinone + ferrocytochrome c
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.8 More secondary structure of yeast cytochrome b and a view of center N, overview Saccharomyces cerevisiae

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 65
-
 decylubiquinol pH 7.0, wild-type enzyme Saccharomyces cerevisiae

pH Optimum

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

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
7.1.1.8 0.000012
-
 a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM Saccharomyces cerevisiae ilicicolin H