Abstract
The unique bifurcation of electron flow at the ubihydroquinone-oxidation center of the cytochrome bc 1 complex is the energy-conserving reaction of the protonmotive Q-cycle and is prerequisite to vectorial proton translocation. The widely accepted Q-cycle reaction scheme describes the overall electron and proton pathways, but does not address the detailed chemistry of this central step. Based on a model of the ubihydroquinone-oxidation pocket containing two ubiquinone molecules in a stacked configuration, a detailed model for the reactions during steady-state catalysis is proposed. In this proton-gated charge-transfer mechanism the reaction is controlled by the deprotonation of the substrate ubihydroquinone.

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