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Fo·F1 ATP-synthase/ATPase of Paracoccus denitrificans: Mystery of Unidirectional Catalysisстатья Исследовательская статья
- Авторы: Zharova Tatiana V., Grivennikova Vera G.
- Журнал: Biochemistry (Moscow)
- Том: 90
- Номер: Suppl. 1
- Год издания: 2025
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: S86
- Последняя страница: S104
- DOI: 10.1134/s000629792460399x
- Аннотация: Fo∙F1 ATP synthases/ATPases (Fo∙F1) catalyze ATP synthesis by consuming energy of electrochemical potential of hydrogen ions (pmf), or ATP hydrolysis resulting in the pmf formation. It is generally accepted to consider Fo∙F1 as a reversible chemomechanical-electrical molecular machine, however: 1) the mechanism of energy-dependent ATP synthesis is based only on the data on hydrolytic activity of the enzyme, 2) Fo∙F1 from a number of organisms effectively synthesize, but is unable to hydrolyze ATP, which indicates non-observance of the principle of microreversibility and requires development of a new hypotheses concerning the enzyme mechanism. Since 1980, the group of A. D. Vinogradov has been developing a concept according to which the elementary catalysis stages of ATP hydrolysis and ATP synthesis do not coincide, and there are two independently operating forms of Fo∙F1 in the coupled membranes – pmf-generating ATPase and pmf-consuming ATP synthase. Fo∙F1 of P. denitrificans as a natural model of an irreversibly functioning enzyme is a convenient object for experimental verification of the hypothesis of unidirectional energy conversion. The review considers modern concepts of the molecular mechanisms of regulation of Fo∙F1 ATP synthase/ATPase of P. denitrificans and development of the hypothesis of two forms of Fo∙F1.
- Добавил в систему: Жарова Татьяна Вадимовна
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | BiochemistryM_2025_ZharovaGrivennikova.pdf | 565,9 КБ | 31 марта 2025 [TVZharova] |