Restoration of pool function type behavior to succinate dehydrogenase having latent reconstitutive activity in ubiquinol-cytochrome reductase complex |
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Authors: | Bernard L Trumpower |
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Institution: | Department of Biochemistry Dartmouth Medical School Hanover, N.H. 03755 USA |
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Abstract: | Mitochondrial ubiquinol-cytochrome reductase complex contains small amounts of succinate dehydrogenase. Estimates from electrophoresis indicate there is one dehydrogenase per eight complexes. This dehydrogenase transfers electrons to the - complex poorly, as judged by low succinate-ubiquinone and succinate-cytochrome reductase activities. Electron transfer to the - complex is restored by reconstitution of the complex with phospholipid. This phospholipid dependent restoration of electron transfer indicates that either reconstitutive activity of the dehydrogenase is preserved under conditions where electron transfer is absent, or that addition of phospholipid allows one dehydrogenase to transfer electrons to multiple - complexes. |
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