Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme

Ryohei Yasuda, Hiroyuki Noji, Kazuhiko Kinosita, Fumihiro Motojima, Masasuke Yoshida

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

ATP-dependent, azide-sensitive rotation of the γ subunit relative to the α3β3 hexagonal ring of ATP synthase was observed with a single molecule imaging system. Thus, ATP synthase is a rotary motor enzyme, the first ever found.

Original languageEnglish
Pages (from-to)207-209
Number of pages3
JournalJournal of Bioenergetics and Biomembranes
Volume29
Issue number3
DOIs
Publication statusPublished - 1997
Externally publishedYes

Fingerprint

Proton-Translocating ATPases
Adenosine Triphosphate
Enzymes
Azides

Keywords

  • ATP synthase
  • F-ATPase
  • Loose coupling
  • Rotary motor
  • Single molecule imaging

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme. / Yasuda, Ryohei; Noji, Hiroyuki; Kinosita, Kazuhiko; Motojima, Fumihiro; Yoshida, Masasuke.

In: Journal of Bioenergetics and Biomembranes, Vol. 29, No. 3, 1997, p. 207-209.

Research output: Contribution to journalArticle

Yasuda, Ryohei ; Noji, Hiroyuki ; Kinosita, Kazuhiko ; Motojima, Fumihiro ; Yoshida, Masasuke. / Rotation of the γ subunit in F1-ATPase; Evidence that ATP synthase is a rotary motor enzyme. In: Journal of Bioenergetics and Biomembranes. 1997 ; Vol. 29, No. 3. pp. 207-209.
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