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Literature summary for 7.1.1.8 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
Search for more literature for 7.1.1.8

Inhibitors

Inhibitors Comment Organism Structure
Antimycin highly reduces the rate of cytochrome c1 Saccharomyces cerevisiae
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
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
additional information the rate of cytochrome c1 is highly reduced in absence of ubiquinone Saccharomyces cerevisiae
Myxothiazol
-
 Saccharomyces cerevisiae
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinol-2 + 2 ferricytochrome c
-
 Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
 ?
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

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

Synonyms

Synonyms Comment Organism
cytochrome bc1 complex
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
 Saccharomyces cerevisiae

Ki Value [mM]

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