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

Research output: Contribution to journalArticle

169 Citations (Scopus)

Abstract

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
Volume97
Issue number13
DOIs
Publication statusPublished - 2000 Jun 20
Externally publishedYes

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Proton-Translocating ATPases
Adenosine Triphosphate
Videotape Recording
Hydrolysis
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging. / Adachi, Kengo; Yasuda, Ryohei; Noji, Hiroyuki; Itoh, Hiroyasu; Harada, Yoshie; Yoshida, Masasuke; Kinosita, Kazuhiko.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, No. 13, 20.06.2000, p. 7243-7247.

Research output: Contribution to journalArticle

Adachi, Kengo ; Yasuda, Ryohei ; Noji, Hiroyuki ; Itoh, Hiroyasu ; Harada, Yoshie ; Yoshida, Masasuke ; Kinosita, Kazuhiko. / Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging. In: Proceedings of the National Academy of Sciences of the United States of America. 2000 ; Vol. 97, No. 13. pp. 7243-7247.
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