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

研究成果: Article

172 引用 (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.

ジャーナルProceedings of the National Academy of Sciences of the United States of America
出版物ステータスPublished - 2000 6 20

ASJC Scopus subject areas

  • General
  • Genetics

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