論文

査読有り
2006年4月

Probing conformations of the beta subunit of F0F1-ATP synthase in catalysis

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • T Masaike
  • ,
  • T Suzuki
  • ,
  • SP Tsunoda
  • ,
  • H Konno
  • ,
  • M Yoshida

342
3
開始ページ
800
終了ページ
807
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bbrc.2006.02.017
出版者・発行元
ACADEMIC PRESS INC ELSEVIER SCIENCE

A subcomplex of F0F1-ATP synthase (F0F1), alpha(3)beta(3)gamma, was shown to undergo the conformation(s) during ATP hydrolysis in which two of the three beta subunits have the "Closed" conformation simultaneously (CC conformation) [S.P. Tsunoda, E. Muneyuki, T. Amano, M. Yoshida, H. Noji, Cross-linking of two beta subunits in the closed conformation in F-1-ATPase, J. Biol. Chem. 274 (1999) 5701-5706]. This was examined by the inter-subunit disulfide cross-linking between two mutant beta(1386C)s that was formed readily only when the enzyme was in the CC conformation. Here, we adopted the same method for the holoenzyme F0F1 from Bacillus PS3 and found that the CC conformation was generated during ATP hydrolysis but barely during ATP synthesis. The experiments using F0F1 with the epsilon subunit lacking C-terminal helices further suggest that this difference is related to dynamic nature of the e subunit and that ATP synthesis is accelerated when it takes the pathway involving the CC conformation. (c) 2006 Elsevier Inc. All rights reserved.

リンク情報
DOI
https://doi.org/10.1016/j.bbrc.2006.02.017
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000236168600017&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/j.bbrc.2006.02.017
  • ISSN : 0006-291X
  • eISSN : 1090-2104
  • Web of Science ID : WOS:000236168600017

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