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Literature summary extracted from

  • Gao, X.; Wen, X.; Esser, L.; Quinn, B.; Yu, L.; Yu, C.A.; Xia, D.
    Structural basis for the quinone reduction in the bc1 complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc1 with bound substrate and inhibitors at the Qi site (2003), Biochemistry, 42, 9067-9080.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.1.1.8 purified native oxidized enzyme complex or enzyme bound to antimycin A1 or 2-nonyl-4-hydroxyquinoline N-oxide, hanging drop vapour diffusion method, 20 mg/ml protein in 50 mM MOPS, pH 7.2, 20 mM ammonium acetate, 20% w/v glycerol, and either 0.1% decanoyl-N-methylglucamide or 0.1% diheptanoyl phosphatidylcholine, or 0.16% sucrose monocaprate, mixed with precipitant solution, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution, modeling Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.8 2-nonyl-4-hydroxyquinoline N-oxide binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview Bos taurus
7.1.1.8 antimycin A1 binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview Bos taurus
7.1.1.8 additional information structure determination of the inhibitor binding site Qi, located near the matrix side of the membrane bilayer Bos taurus

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.8 additional information Bos taurus enzyme is a central component of cellular energy conservation machinery ?
-
 ?
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c Bos taurus enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.8 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.8 fully oxidized enzyme complex to homogeneity Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
7.1.1.8 quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] substrate binding site Qo structure, conformational changes upon inhibitor binding, overview Bos taurus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.1.1.8 heart
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 additional information enzyme is a central component of cellular energy conservation machinery Bos taurus ?
-
 ?
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes Bos taurus ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c binding interaction of ubiquinone with cytochrome b, overview Bos taurus ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.8 dimer enzyme complex Bos taurus

Synonyms

EC Number Synonyms Comment Organism
7.1.1.8 Cyt bc1 complex
-
 Bos taurus
7.1.1.8 cytochrome bc1 complex
-
 Bos taurus
7.1.1.8 quinol cyt. c oxidoreductase (bc1)
-
 Bos taurus