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Assembly of a chimeric respiratory chain from bovine heart submitochondrial particles and cytochrome bd terminal oxidase of Escherichia coli |
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| Authors: | Eleonora V Gavrikova Vitaliy B Borisov Andrei D Vinogradov |
| Institution: | a Department of Biochemistry, School of Biology, Moscow State University, Moscow 119991, Russian Federation b Department of Molecular Energetics of Microorganisms, Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119991, Russian Federation c Molecular Biology Division, VA Medical Center, 4150 Clement Street, San Francisco, CA 94121, USA d Department of Biochemistry & Biophysics, University of California, San Francisco, CA 94158, USA e Mitoengineering Center of Moscow State University, Moscow 119991, Russian Federation |
| Abstract: | Cytochrome bd is a terminal quinol oxidase in Escherichia coli. Mitochondrial respiration is inhibited at cytochrome bc1 (complex III) by myxothiazol. Mixing purified cytochrome bd oxidase with myxothiazol-inhibited bovine heart submitochondrial particles (SMP) restores up to 50% of the original rotenone-sensitive NADH oxidase and succinate oxidase activities in the absence of exogenous ubiquinone analogs. Complex III bypassed respiration and is saturated at amounts of added cytochrome bd similar to that of other natural respiratory components in SMP. The cytochrome bd tightly binds to the mitochondrial membrane and operates as an intrinsic component of the chimeric respiratory chain. |
| Keywords: | SMP submitochondrial particles |
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