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  • Title: [Reconstitution of succinate-ubiquinone reductase of the respiratory chain of mitochondria].
    Author: Gavrikov VG, Gavrikova EV, Vinogradov AD.
    Journal: Biokhimiia; 1980 Apr; 45(4):747-55. PubMed ID: 7378499.
    Abstract:
    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.
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