Rotational catalysis by F1-ATPase

K. Adachi*, T. Nishizaka, K. Kinosita

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter


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.
Number of pages15
ISBN (Print)9780080957180
Publication statusPublished - 2012
Externally publishedYes


  • 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)


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