Activation of pausing F1 motor by external force

Yoko Hirono-Hara, Koji Ishizuka, Kasuhiko Kinosita, Masasuke Yoshida, Hiroyuki Noji*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

91 Citations (Scopus)


A rotary motor F1, a catalytic part of ATP synthase, makes a 120° step rotation driven by hydrolysis of one ATP, which consists of 80° and 40° substeps initiated by ATP binding and probably by ADP and/or Pi dissociation, respectively. During active rotations, F 1 spontaneously fails in ADP release and pauses after a 80° substep, which is called the ADP-inhibited form. In the present work, we found that, when pushed >+40° with magnetic tweezers, the pausing F1 resumes its active rotation after releasing inhibitory ADP. The rate constant of the mechanical activation exponentially increased with the pushed angle, implying that F1 weakens the affinity of its catalytic site for ADP as the angle goes forward. This finding explains not only its unidirectional nature of rotation, but also its physiological function in ATP synthesis; it would readily bind ADP from solution when rotated backward by an Fo motor in the ATP synthase. Furthermore, the mechanical work for the forced rotation was efficiently converted into work for expelling ADP from the catalytic site, supporting the tight coupling between the rotation and catalytic event.

Original languageEnglish
Pages (from-to)4288-4293
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number12
Publication statusPublished - 2005 Mar 22
Externally publishedYes


  • ADP inhibition
  • ATP synthase
  • F1-ATPase
  • Magnetic tweezers
  • Single-molecule observation

ASJC Scopus subject areas

  • Genetics
  • General


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