EC Number   |
Reaction |
Reference |
|---|
    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 |
658160 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
alternating half-of-sites mechanism of ubiquinol oxidation |
659318 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
alternating half-of-the-sites mechanism of ubiquinol oxidation, enzyme links electron transfer from ubiquinol to cytochrome c by a protonmotive Q cycle mechanism in which ubiquinol is oxidized at one center in the enzyme, referred to as center P, und ubiquinone is re-reduced at a second center, referred to as center N |
659170 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
binding structure and mode of cytochrome c1 within the enzyme complex and cytochrome c during the catalytic reaction, direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c, half-of-the sites mechanism |
658161 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. depending on the organism and the physiological conditions, either two or four protons are extruded from the cytoplasmic to the non-cytoplasmic compartment (cf.EC1.6.99.3 NADH2 dehydrogenase) |
- |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
current competing models for the two-electron oxidation of quinol QH2 at the cytochrome bc1 complex and related complexes impose distinct requirements for the reaction intermediate, the initial and rate-limiting step in quinol oxidation, both in the biological and biomimetic systems, involves electron and proton transfer, probably via a proton-coupled electron-transfer mechanism, a neutral semiquinone intermediate is formed in the biomimetic system, and oxidation of the QH*/QH2 couple for UQH2-0, but not TMQH2-0, exhibits an unusual and unexpected primary deuterium kinetic isotope effect on its Arrhenius activation energy, DELTA GTS, where DELTA GTS for the protiated form is larger than that for the deuterated form, detailed reaction mechanism, molecular modeling, electrochemical and computational study, overview |
674163 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
reaction and substrate binding mechanism, overview, conformational changes at the binding site of inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole confirm the proton transfer pathway and reveal plasticity at the active site |
659238 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex |
725396 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
reaction mechanism, kinetic modeling |
674665 |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] |
reaction mechanism, similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex |
674721 |
