Energy conservation by bifurcated electron-transfer in the cytochrome-bc1 complex.

The overall electron- and proton-pathways within the cytochrome-bc1 complex are described by a widely accepted mechanism known as the protonmotive Q-cycle. Within this reaction scheme, the unique bifurcation of electron flow into a high potential and a low potential pathway occurring at the ubihydroquinone-oxidation center is the energy conserving reaction. It is this reaction, which results in vectorial proton translocation, as it allows the 'recycling' of every second electron across the membrane onto the ubiquinone-reduction center. However, the Q-cycle reaction scheme does not address the detailed chemistry of this central step. Based on a structural model of the ubihydroquinone-oxidation pocket and the assumption that the reaction involves two ubiquinone molecules in a stacked configuration, here I propose a detailed chemical model for the reactions occurring during steady-state catalysis. In this proton-gated charge-transfer mechanism the reaction is controlled by the deprotonation of the substrate ubihydroquinone and not, as proposed earlier, by the formation of a highly unstable semiquinone species.