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Met23Lys mutation in subunit gamma of FOF1-ATP synthase from Rhodobacter capsulatus impairs the activation of ATP hydrolysis by protonmotive forceстатья
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: 18 июля 2013 г.
- Авторы: Feniouk Boris A., Rebecchi Alberto, Giovannini Donatella, Anefors Sofie, Mulkidjanian Annen Y., Junge Wolfgang, Turina Paola, Melandri Andrea
- Журнал: Biochimica et Biophysica Acta - Bioenergetics
- Том: 1767
- Номер: 11
- Год издания: 2007
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 1319
- Последняя страница: 1330
- DOI: 10.1016/j.bbabio.2007.07.009
- Аннотация: H+-F0F1-ATP synthase couples proton flow through its membrane portion, F-0, to the synthesis of ATP in its headpiece, F-1. Upon reversal of the reaction the enzyme functions as a proton pumping ATPase. Even in the simplest bacterial enzyme the ATPase activity is regulated by several mechanisms, involving inhibition by MgADP, conformational transitions of the epsilon subunit, and activation by protonmotive force. Here we report that the Met23Lys mutation in the gamma subunit of the Rhodobacter capsulatus ATP synthase significantly impaired the activation of ATP hydrolysis by protonmotive force. The impairment in the mutant was due to faster enzyme deactivation that was particularly evident at low ATP/ADP ratio. We suggest that the electrostatic interaction of the introduced gamma Lys23 with the DELSEED region of subunit stabilized the ADP-inhibited state of the enzyme by hindering the rotation of subunit gamma rotation which is necessary for the activation. (c) 2007 Elsevier B.V. All rights reserved.
- Добавил в систему: Мулкиджанян Армен Яковлевич