The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer

Ryohei Yasuda*, Tomoko Masaike, Kengo Adachi, Hiroyuki Moji, Hiroyasu Itoh, Kazuhiko Kinosita

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

82 Citations (Scopus)


F1-ATPase is an ATP-driven rotary motor in which a rod-shaped γ subunit rotates inside a cylinder made of α3β 3 subunits. To elucidate the conformations of rotating F 1, we measured fluorescence resonance energy transfer (FRET) between a donor on one of the three βs and an acceptor on γ in single F 1 molecules. The yield of FRET changed stepwise at low ATP concentrations, reflecting the stepwise rotation of γ. In the ATP-waiting state, the FRET yields indicated a γ position ≈40° counterclockwise (= direction of rotation) from that in the crystal structures of mitochondrial F1, suggesting that the crystal structures mimic a metastable state before product release.

Original languageEnglish
Pages (from-to)9314-9318
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number16
Publication statusPublished - 2003 Aug 5
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • General


Dive into the research topics of 'The ATP-waiting conformation of rotating F<sub>1</sub>-ATPase revealed by single-pair fluorescence resonance energy transfer'. Together they form a unique fingerprint.

Cite this