Literature summary extracted from
Covian, R.; Gutierrez-Cirlos, E.B.; Trumpower, B.L.
Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex (2004), J. Biol. Chem., 279, 15040-15049.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
7.1.1.8 |
Antimycin |
stimulation at low inhibitor/enzyme ratio |
Saccharomyces cerevisiae |
|
7.1.1.8 |
ilicicolin |
stimulation at low inhibitor/enzyme ratio |
Saccharomyces cerevisiae |
|
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
7.1.1.8 |
Y185F |
iron-sulfur protein mutant, pre-steady-state and steady-state kinetic analysis in comparison to the wild-type enzyme |
Saccharomyces cerevisiae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
7.1.1.8 |
Antimycin |
due to half-of-sites mechanism of the enzyme, 1 inhibitor molecule per enzyme complex dimer is sufficient for inhibition, center N inhibitor |
Saccharomyces cerevisiae |
|
7.1.1.8 |
ilicicolin H |
center N inhibitor |
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 |
pre-steady-state and steady-state kinetics, kinetic modeling, kinetics of interactions between monomers of the dimeric enzyme complex, pH 7.0 and pH 8.8 |
Saccharomyces cerevisiae |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
7.1.1.8 |
Iron |
enzyme complex contains an iron-sulfur protein, and heme groups in the cytochrome molecules |
Saccharomyces cerevisiae |
|
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] |
alternating half-of-sites mechanism of ubiquinol oxidation |
Saccharomyces cerevisiae |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
7.1.1.8 |
decyl-ubiquinol + ferricytochrome c |
anti-cooperative oxidation of ubiquinol, reversible partial reaction |
Saccharomyces cerevisiae |
decyl-ubiquinone + ferrocytochrome c |
- |
? |
|
7.1.1.8 |
additional information |
electron transfer takes place between the 2 cytochrome b subunits |
Saccharomyces cerevisiae |
? |
- |
? |
|
7.1.1.8 |
ubiquinol-2 + 2 ferricytochrome c |
anti-cooperative oxidation of ubiquinol, reversible partial reaction |
Saccharomyces cerevisiae |
ubiquinone-2 + 2 ferrocytochrome c + 2 H+ |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
7.1.1.8 |
More |
interaction analysis between monomers of the dimeric enzyme complex |
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 |
- |
assay at |
Saccharomyces cerevisiae |