Features of organization and mechanism of catalysis of two families of terminal oxidases: Heme-copper and bd-type

Borisov, V.B.; Siletsky, S.A.

Авторы: Borisov V.B., Siletsky S.A.
Журнал: Biochemistry (Moscow)
Том: 84
Номер: 11
Год издания: 2019
Издательство: Pleiades Publishing, Ltd
Местоположение издательства: Road Town, United Kingdom
Первая страница: 1390
Последняя страница: 1402
Оригинальные версии: Особенности устройства и механизма катализа двух семейств терминальных оксидаз: Гем-медных и bd-типа
DOI: 10.1134/S0006297919110130
Аннотация: Terminal oxidases of aerobic respiratory chains of organisms catalyze the transfer of electrons from the respiratory substrate, cytochrome c or quinol, to O2 to form 2H2O. There are two known families of these oxidoreductases integrated into membrane: heme-copper oxidase superfamily and bd-type oxidase family (cytochromes bd) found only in prokaryotes. The redox reaction catalyzed by these enzymes is coupled to the generation of a proton motive force which is used by the cell to synthesize ATP and perform other useful work. Due to the presence of the proton pump, heme-copper oxidases create the membrane potential with greater energy efficiency than cytochromes bd. The latter enzymes, however, play an important physiological role that enables bacteria, including pathogens, to survive and reproduce under adverse environmental conditions. This review considers the features of the organization and the molecular mechanisms of functioning of terminal oxidases from these two families in the light of the experimental data obtained recently.
Добавил в систему: Борисов Виталий Борисович

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Features of organization and mechanism of catalysis of two families of terminal oxidases: Heme-copper and bd-typeстатья

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