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The effect of molecular oxygen on the electron transfer activity of the cytochrome bc 1 complex was investigated by determining the activity of the complex under the aerobic and anaerobic conditions. Molecular oxygen increases the activity of Rhodobacter sphaeroides bc 1 complex up to 82%, depending on the intactness of the complex. Since oxygen enhances the reduction rate of heme...
Intensive biochemical, biophysical and structural studies of the cytochrome (cyt) bc 1 complex in the past have led to the formulation of the “protonmotive Q-cycle” mechanism for electron and proton transfer in this vitally important complex. The key step of this mechanism is the separation of electrons during the oxidation of a substrate quinol at the Q P site with both electrons...
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