Inhibition of respiratory complex I by 6-ketocholestanol: Relevance to recoupling action in mitochondria

Grivennikova, V.G.; Khailova, L.S.; Zharova, T.V.; Kotova, E.A.; Antonenko, Y.N.

Авторы: Grivennikova Vera G., Khailova Ljudmila S., Zharova Tatyana V., Kotova Elena A., Antonenko Yuri N.
Журнал: Biochimica et Biophysica Acta - Bioenergetics
Том: 1863
Номер: 7
Год издания: 2022
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Номер статьи: 148594
DOI: 10.1016/j.bbabio.2022.148594
Аннотация: 6-Ketocholestanol (kCh) is known as a mitochondrial recoupler, i.e. it abolishes uncoupling of mitochondria by such potent agents as carbonyl cyanide m-chlorophenyl hydrazone (CCCP) and 3,5-di(tert-butyl)-4-hydroxybenzylidenemalononitril (SF6847) [Starkov et al., 1997]. Here, we report data on the kCh-induced inhibition of both NADH-oxidase and NADH-ubiquinone oxidoreductase activities of the respiratory complex I in bovine heart submitochondrial particles (SMP). Based on the absence of such inhibition with hexaammineruthenium (III) (HAR) as the complex I electron acceptor, the kCh effect could be associated with the ubiquinone-binding centre of this respiratory enzyme. In isolated rat liver mitochondria (RLM), kCh inhibited oxygen consumption with the glutamate/malate, substrates of NAD-linked dehydrogenases, while no inhibition of RLM respiration was observed with succinate, in agreement with the absence of the kCh effect on the succinate oxidase activity in SMP. Three kCh analogs (cholesterol, 6α-hydroxycholesterol, and 5α,6α-epoxycholesterol) exhibited no effect on the NADH oxidase activities in both SMP and RLM. Importantly, the kCh analogs were ineffective in the recoupling of RLM treated with CCCP or SF6847. Therefore, interaction of kCh with the complex I may be involved in the kCh-mediated mitochondrial recoupling.
Добавил в систему: Антоненко Юрий Николаевич

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