Rotational catalysis by F1-ATPase

K. Adachi, T. Nishizaka, K. Kinosita

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

F1-ATPase, a water-soluble portion of ATP synthase, is a fully reversible rotary molecular machine in which a central γ subunit rotates inside a cylinder made of three α and three β subunits alternately arranged. This motor rotates counterclockwise by hydrolyzing ATP in three catalytic sites but synthesizes ATP when forced to rotate clockwise by an external force. Single-molecule studies have revealed how the chemical reactions that occur in the three catalytic sites are coupled to mechanical rotation.

Original languageEnglish
Title of host publicationComprehensive Biophysics
PublisherElsevier Inc.
Pages35-49
Number of pages15
Volume8
ISBN (Print)9780080957180
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • ATP synthase
  • Chemo-mechanical coupling
  • Conformational change
  • F-ATPase
  • Fluorescent ATP analog
  • Free energy
  • High efficiency
  • High-speed imaging
  • Induced fit
  • Molecular motor
  • Power stroke
  • Single fluorophore imaging
  • Single-molecule study
  • Torque generation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'Rotational catalysis by F<sub>1</sub>-ATPase'. Together they form a unique fingerprint.

  • Cite this

    Adachi, K., Nishizaka, T., & Kinosita, K. (2012). Rotational catalysis by F1-ATPase. In Comprehensive Biophysics (Vol. 8, pp. 35-49). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-374920-8.00804-3