Catalytic robustness and torque generation of the F1-ATPase

Hiroyuki Noji, Hiroshi Ueno, Duncan G.G. McMillan

Research output: Contribution to journalReview articlepeer-review

26 Citations (Scopus)

Abstract

The F1-ATPase is the catalytic portion of the FoF1 ATP synthase and acts as a rotary molecular motor when it hydrolyzes ATP. Two decades have passed since the single-molecule rotation assay of F1-ATPase was established. Although several fundamental issues remain elusive, basic properties of F-type ATPases as motor proteins have been well characterized, and a large part of the reaction scheme has been revealed by the combination of extensive structural, biochemical, biophysical, and theoretical studies. This review is intended to provide a concise summary of the fundamental features of F1-ATPases, by use of the well-described model F1 from the thermophilic Bacillus PS3 (TF1). In the last part of this review, we focus on the robustness of the rotary catalysis of F1-ATPase to provide a perspective on the re-designing of novel molecular machines.

Original languageEnglish
Pages (from-to)103-118
Number of pages16
JournalBiophysical Reviews
Volume9
Issue number2
DOIs
Publication statusPublished - 1 Apr 2017
Externally publishedYes

Keywords

  • ATP synthase
  • F-ATPase
  • Molecular motor
  • Single-molecule techniques

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