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Residue 249 in subunit beta regulates ADP inhibition and its phosphate modulation in Escherichia coli ATP synthaseстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 10 апреля 2019 г.
- Авторы: Lapashina AS, Prikhodko AS, Shugaeva TE, Feniouk BA
- Журнал: Biochimica et Biophysica Acta - Bioenergetics
- Том: 1860
- Номер: 3
- Год издания: 2019
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 181
- Последняя страница: 188
- DOI: 10.1016/j.bbabio.2018.12.003
- Аннотация: ATPase activity of proton-translocating FOF1-ATP synthase (F-type ATPase or F-ATPase) is suppressed in the absence of protonmotive force by several regulatory mechanisms. The most conservative of these mechanisms found in all enzymes studied so far is allosteric inhibition of ATP hydrolysis by MgADP (ADP-inhibition). When MgADP is bound without phosphate in the catalytic site, the enzyme lapses into an inactive state with MgADP trapped. In chloroplasts and mitochondria, as well as in most bacteria, phosphate prevents MgADP inhibition. However, in Escherichia coli ATP synthase ADP-inhibition is relatively weak and phosphate does not prevent it but seems to enhance it. We found that a single amino acid residue in subunit β is responsible for these features of E. coli enzyme. Mutation βL249Q significantly enhanced ADP-inhibition in E. coli ATP synthase, increased the extent of ATP hydrolysis stimulation by sulfite, and rendered the ADP-inhibition sensitive to phosphate in the same manner as observed in FOF1 from mitochondria, chloroplasts, and most aerobic\photosynthetic bacteria.
- Добавил в систему: Фенюк Борис Александрович