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Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation.

Authors
  • Watanabe, Rikiya
  • Noji, Hiroyuki
Type
Published Article
Journal
Scientific Reports
Publisher
Springer Nature
Publication Date
Jan 01, 2014
Volume
4
Pages
4962–4962
Identifiers
DOI: 10.1038/srep04962
PMID: 24825532
Source
Medline
License
Unknown

Abstract

F1-ATPase (F1) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F1 that was characterized by a rate constant remarkably sensitive to temperature and had a Q10 factor of 6-19. Since reactions with high Q10 values are considered to involve large conformational changes, we speculated that the TS reaction plays a key role in the rotation of F1. To clarify the role of the TS reaction, in this study, we conducted a stall and release experiment using magnetic tweezers, and assessed the torque generated during the TS reaction. The results indicate that the TS reaction generates the same amount of rotational torque as does ATP binding, but more than that generated during ATP hydrolysis. Thus, we confirmed that the TS reaction contributes significantly to the rotation of F1.

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