ISSN:
1573-6881
Keywords:
Rieske iron-sulfur protein, RIP1
;
Saccharomyces cerevisiae
;
mitochondria
;
bc 1 complex
;
QCR9
;
iron-sulfur cluster, mitochondrial targeting
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00762586
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