Single molecule thermodynamics of ATP synthesis by F1-ATPase

Shoichi Toyabe, Eiro Muneyuki

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)


FoF1-ATP synthase is a factory for synthesizing ATP in virtually all cells. Its core machinery is the subcomplex F1-motor (F1-ATPase) and performs the reversible mechanochemical coupling. The isolated F1-motor hydrolyzes ATP, which is accompanied by unidirectional rotation of its central γ-shaft. When a strong opposing torque is imposed, the γ-shaft rotates in the opposite direction and drives the F1-motor to synthesize ATP. This mechanical-to-chemical free-energy transduction is the final and central step of the multistep cellular ATP-synthetic pathway. Here, we determined the amount of mechanical work exploited by the F1-motor to synthesize an ATP molecule during forced rotations using a methodology combining a nonequilibrium theory and single molecule measurements of responses to external torque. We found that the internal dissipation of the motor is negligible even during rotations far from a quasistatic process.

Original languageEnglish
Article number015008
JournalNew Journal of Physics
Publication statusPublished - 2015 Jan 15


  • F-ATPase
  • motor proteins
  • nonequilibrium and irreversible thermodynamics


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