Proton-translocating NADH:ubiquinone oxidoreductase of Paracoccus denitrificans plasma membranes catalyzes FMN-independent reverse electron transfer to hexaammineruthenium (III)

Авторы: Gladyshev Grigory V., Zharova Tatyana V., Kareyeva Alexandra V., Grivennikova Vera G.
Журнал: Biochimica et Biophysica Acta - Bioenergetics
Год издания: 2023
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Первая страница: 148963
DOI: 10.1016/j.bbabio.2023.148963
Аннотация: NADH-OH, the specific inhibitor of NADH-binding site of the mammalian complex I, is shown to completely block FMN-dependent reactions of P. denitrificans enzyme in plasma membrane vesicles: NADH oxidation (in a competitive manner with Ki of 1 nM) as well as reduction of pyridine nucleotides, ferricyanide and oxygen in the reverse electron transfer. In contrast to these activities, the reverse electron transfer to hexaammineruthenium (III) catalyzed by plasma membrane vesicles is insensitive to NADH-OH. To explain these results, we hypothesize the existence of a non-FMN redox group of P. denitrificans complex I that is capable of reducing hexaammineruthenium (III), which is corroborated by the complex kinetics of NADH: hexaammineruthenium (III)-reductase activity, catalyzed by this enzyme. A new assay procedure for measuring succinate-driven reverse electron transfer catalyzed by P. denitrificans complex I to hexaammineruthenium (III) is proposed.
Добавил в систему: Гладышев Григорий Викторович

№	Имя	Описание	Имя файла	Размер	Добавлен
1.	Gladyshev_BBA_2023.pdf		Gladyshev_BBA_2023.pdf	1,8 МБ	29 ноября 2023 [VeraGrivennikova]
2.	Gladyshev_BBA_2023.pdf		Gladyshev_BBA_2023.pdf	1,8 МБ	29 ноября 2023 [VeraGrivennikova]

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