Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging

Kengo Adachi, Ryohei Yasuda, Hiroyuki Noji, Hiroyasu Itoh, Yoshie Harada, Masasuke Yoshida, Kazuhiko Kinosita*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

188 Citations (Scopus)


Orientation dependence of single-fluorophore intensity was exploited in order to videotape conformational changes in a protein machine in real time. The fluorophore Cy3 attached to the central subunit of F1-ATPase revealed that the subunit rotates in the molecule in discrete 120°steps and that each step is driven by the hydrolysis of one ATP molecule. These results, unlike those from the previous study under a frictional load, show that the 120° stepping is a genuine property of this molecular motor. The data also show that the rate of ATP binding is insensitive to the load exerted on the rotor subunit.

Original languageEnglish
Pages (from-to)7243-7247
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
Publication statusPublished - 2000 Jun 20
Externally publishedYes

ASJC Scopus subject areas

  • General
  • Genetics


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