Catalytic robustness and torque generation of the F1-ATPase

Hiroyuki Noji; Hiroshi Ueno; Duncan G G McMillan

doi:10.1007/s12551-017-0262-x

Catalytic robustness and torque generation of the F₁-ATPase

Biophys Rev. 2017 Mar 25;9(2):103-118. doi: 10.1007/s12551-017-0262-x. eCollection 2017 Apr.

Authors

Hiroyuki Noji¹, Hiroshi Ueno¹, Duncan G G McMillan¹

Affiliation

¹ Department of Applied Chemistry, Graduate School of Engineering, The University of Tokyo, Tokyo, 113-8656 Japan.

Abstract

The F₁-ATPase is the catalytic portion of the F_oF₁ 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.

Keywords: ATP synthase; F1-ATPase; Molecular motor; Single-molecule techniques.

Publication types

Review