Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Trumpower, B.L.
    A concerted, alternating sites mechanism of ubiquinol oxidation by the dimeric cytochrome bc1 complex (2002), Biochim. Biophys. Acta, 1555, 166-173.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.8 Antimycin highly reduces the rate of cytochrome c1 Saccharomyces cerevisiae
7.1.1.8 menaquinol inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative Saccharomyces cerevisiae
7.1.1.8 methoxyacrylate stilbene inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative Saccharomyces cerevisiae
7.1.1.8 additional information the rate of cytochrome c1 is highly reduced in absence of ubiquinone Saccharomyces cerevisiae
7.1.1.8 Myxothiazol
-
 Saccharomyces cerevisiae
7.1.1.8 Stigmatellin inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative 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 of the enzyme complex activity dependent on pH and on the Rieske iron-sulfur protein midpoint potential, thermodynamic profile of the Q cycle Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.8 Iron enzyme complex contains a Rieske Fe-S protein which controls the rate of reduction of the cytochrome b 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 ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation 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] 2 reaction mechanism variants, a fully active enzyme mechanism and a half-of-the sites mechanism of ubiquinol oxidation, switching between the two variants may regulate the enzyme, Glu272 and His181 are involved 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
-
 Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?
7.1.1.8 ubiquinol-2 + 2 ferricytochrome c ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.8 dimer cytochrome bc1 complex, electron transfer complex structure Saccharomyces cerevisiae

Synonyms

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.8 7.5 8
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
7.1.1.8 0.0000025 0.000005 methoxyacrylate stilbene
-
 Saccharomyces cerevisiae