[Reconstitution of succinate-ubiquinone reductase of the respiratory chain of mitochondria].
A soluble protein fraction, which confers the reactivity of soluble succinate dehydrogenase towards ubiquinone, was isolated from beef heart mitochondria. This fraction contains three polypeptides as revealed by SDS-electrophoresis; the major peptide (about 80% of protein) has a molecular weight less than 13 000. Several properties of the reconstituted succinate-ubiquinone reductase, i. e. the turnover number of succinate dehydrogenase inhibitor sensitivity, stability and reactivity towards artificial electron acceptors were found to be identical to those of the native succinate-ubiquinone region of the respiratory chain. A model of the minimal functionally active structure capable of reduction of ubiquinone by succinate is proposed.
D000818:Animals; D002417:Cattle; D004579:Electron Transport; D042963:Electron Transport Complex II; D007700:Kinetics; D046911:Macromolecular Substances; D008929:Mitochondria, Heart / Q000201:enzymology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010101:Oxygen Consumption; D013385:Succinate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D010088:Oxidoreductases; D042963:Electron Transport Complex II; D013385:Succinate Dehydrogenase
Rekonstruktsiia suktsinat-ubikhinon-reduktaznogo uchastka dykhatel'noĭ tsepi mitokhondriĭ.