Reference: Graham LA, et al. (1993) Mutational analysis of assembly and function of the iron-sulfur protein of the cytochrome bc1 complex in Saccharomyces cerevisiae. J Bioenerg Biomembr 25(3):245-57

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Abstract


The iron-sulfur protein of the cytochrome bc1 complex oxidizes ubiquinol at center P in the protonmotive Q cycle mechanism, transferring one electron to cytochrome c1 and generating a low-potential ubisemiquinone anion which reduces the low-potential cytochrome b-566 heme group. In order to catalyze this divergent transfer of two reducing equivalents from ubiquinol, the iron-sulfur protein must be structurally integrated into the cytochrome bc1 complex in a manner which facilitates electron transfer from the iron-sulfur cluster to cytochrome c1 and generates a strongly reducing ubisemiquinone anion radical which is proximal to the b-566 heme group. This radical must also be sequestered from spurious reactivities with oxygen and other high-potential oxidants. Experimental approaches are described which are aimed at understanding how the iron-sulfur protein is inserted into center P, and how the iron-sulfur cluster is inserted into the apoprotein.

Reference Type
Comparative Study | Journal Article | Review
Authors
Graham LA, Brandt U, Sargent JS, Trumpower BL
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