EC Number |
Natural Substrates |
---|
7.1.1.8 | naphthoquinol + 2 ferricytochrome c |
- |
7.1.1.8 | quinol + 2 ferricytochrome c |
- |
7.1.1.8 | ubiquinol + 2 ferricytochrome c |
- |
7.1.1.8 | ubiquinol + 2 ferricytochrome c |
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced |
7.1.1.8 | ubiquinol + 2 ferricytochrome c |
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site |
7.1.1.8 | ubiquinol + 2 ferricytochrome c552 |
- |
7.1.1.8 | ubiquinol + ferricytochrome c |
- |
7.1.1.8 | ubiquinol + ferricytochrome c |
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively |
7.1.1.8 | ubiquinol-2 + 2 ferricytochrome c |
- |
7.1.1.8 | ubiquinol-2 + 2 ferricytochrome c |
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis |