Mutational analysis of assembly and function of the iron-sulfur protein of the cytochromebc 1 complex inSaccharomyces cerevisiae
- 1 June 1993
- journal article
- Published by Springer Nature in Journal of Bioenergetics and Biomembranes
- Vol. 25 (3) , 245-257
- https://doi.org/10.1007/bf00762586
Abstract
The iron-sulfur protein of the cytochromebc 1 complex oxidizes ubiquinol at center P in the protonmotive Q cycle mechanism, transferring one electron to cytochromec 1 and generating a low-potential ubisemiquinone anion which reduces the low-potential cytochromeb-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 cytochromebc 1 complex in a manner which facilitates electron transfer from the iron-sulfur cluster to cytochromec 1 and generates a strongly reducing ubisemiquinone anion radical which is proximal to theb-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.Keywords
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