Rotation of F1-ATPase: How an ATP-driven molecular machine may work

Kazuhiko Kinosita, Kengo Adachi, Hiroyasu Itoh

Research output: Contribution to journalArticle

154 Citations (Scopus)

Abstract

F1-ATPase is a rotary motor made of a single protein molecule. Its rotation is driven by free energy obtained by ATP hydrolysis. In vivo, another motor, F0, presumably rotates the F1 motor in the reverse direction, reversing also the chemical reaction in F1 to let it synthesize ATP. Here we attempt to answer two related questions, How is free energy obtained by ATP hydrolysis converted to the mechanical work of rotation, and how is mechanical work done on F1 converted to free energy to produce ATP? After summarizing single-molecule observations of F1 rotation, we introduce a toy model and discuss its free-energy diagrams to possibly answer the above questions. We also discuss the efficiency of molecular motors in general.

Original languageEnglish
Pages (from-to)245-268
Number of pages24
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume33
DOIs
Publication statusPublished - 2004
Externally publishedYes

Fingerprint

Proton-Translocating ATPases
Adenosinetriphosphate
Free energy
Adenosine Triphosphate
Hydrolysis
Play and Playthings
Molecules
Chemical reactions
Proteins
Adenosine Triphosphatases

Keywords

  • Efficiency of energy conversion
  • Free energy
  • Molecular motor
  • Single-molecule physiology
  • Torque generation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

Rotation of F1-ATPase : How an ATP-driven molecular machine may work. / Kinosita, Kazuhiko; Adachi, Kengo; Itoh, Hiroyasu.

In: Annual Review of Biophysics and Biomolecular Structure, Vol. 33, 2004, p. 245-268.

Research output: Contribution to journalArticle

Kinosita, Kazuhiko ; Adachi, Kengo ; Itoh, Hiroyasu. / Rotation of F1-ATPase : How an ATP-driven molecular machine may work. In: Annual Review of Biophysics and Biomolecular Structure. 2004 ; Vol. 33. pp. 245-268.
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