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Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor protein.

Authors
  • Watanabe, Rikiya
  • Noji, Hiroyuki
Type
Published Article
Journal
Nature Communications
Publisher
Springer Nature
Publication Date
Jan 01, 2014
Volume
5
Pages
3486–3486
Identifiers
DOI: 10.1038/ncomms4486
PMID: 24686317
Source
Medline
License
Unknown

Abstract

F1-ATPase is a rotary motor protein driven by ATP hydrolysis. The rotary motion of F1-ATPase is tightly coupled to catalysis, in which the catalytic sites strictly obey the reaction sequences at the resolution of elementary reaction steps. This fine coordination of the reaction scheme is thought to be important to achieve extremely high chemomechanical coupling efficiency and reversibility, which is the prominent feature of F1-ATPase among molecular motor proteins. In this study, we intentionally change the reaction scheme by using single-molecule manipulation, and we examine the resulting effect on the rotary motion of F1-ATPase. When the sequence of the products released, that is, ADP and inorganic phosphate, is switched, we find that F1 frequently stops rotating for a long time, which corresponds to inactivation of catalysis. This inactive state presents MgADP inhibition, and thus, we find that an improper reaction sequence of F1-ATPase catalysis induces MgADP inhibition.

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