The chemistry and mechanics of ubihydroquinone oxidation at center P (Qo) of the cytochrome bc1 complex.

The emerging X-ray structures of the cytochrome bc1 complexes from bovine and chicken heart mitochondria support the protonmotive Q-cycle as the overall electron- and proton-pathway within the cytochrome bc1 complex. The energy conserving reaction within this reaction scheme is the unique bifurcation of electron flow into a high potential and a low potential pathway occurring at the ubihydroquinone-oxidation center (center P or Qo). This step is prerequisite for the 'recycling' of every second electron across the membrane onto the ubiquinone-reduction center, which results in vectorial proton translocation. It has been shown that during steady-state the step controlling this reaction is the first deprotonation of ubihydroquinone and not, as proposed earlier, the formation of a highly unstable semiquinone species. Ubiquinone has not yet been detected at the ubihydroquinone-oxidation center of the protein structures now available, but the pocket seems spacious enough to accommodate two ubiquinone molecules. This is in line with recent enzymological studies, which have shown that not only two ubiquinones, but also two inhibitor molecules can bind to center P. The most striking result from the structures is that the hydrophilic domain of the 'Rieske' protein can be found in two different positions which seem to allow electron transfer between the iron-sulfur cluster and either ubiquinone binding at center P or heme c1. This provides strong support for the 'catalytic switch' model proposed earlier based on detailed analysis of inhibitor binding to cytochrome bc1 complex in different redox states.