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Recent progress in understanding the Q-cycle mechanism of the bc 1 complex is reviewed. The data strongly support a mechanism in which the Q o -site operates through a reaction in which the first electron transfer from ubiquinol to the oxidized iron–sulfur protein is the rate-determining step for the overall process. The reaction involves a proton-coupled electron transfer down a hydrogen...
The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc 1 functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have constructed site-specific variants at two of these residues, measured their thermodynamic and functional...
The Q-cycle mechanism of the bc 1 complex explains how the electron transfer from ubihydroquinone (quinol, QH 2 ) to cytochrome (cyt) c (or c 2 in bacteria) is coupled to the pumping of protons across the membrane. The efficiency of proton pumping depends on the effectiveness of the bifurcated reaction at the Q o -site of the complex. This directs the two electrons...
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