Pause and rotation of F1-ATPase during catalysis

Yoko Hirono-Hara, Hiroyuki Noji, Masaya Nishiura, Eiro Muneyuki, Kiyotaka Y. Hara, Ryohei Yasuda, Kazuhiko Kinosita, Masasuke Yoshida

Research output: Contribution to journalArticle

149 Citations (Scopus)


F1-ATPase is a rotary motor enzyme in which a single ATP molecule drives a 120° rotation of the central γ subunit relative to the surrounding α3β3 ring. Here, we show that the rotation of F1-ATPase spontaneously lapses into long (≅30 s) pauses during steady-state catalysis. The effects of ADP-Mg and mutation on the pauses, as well as kinetic comparison with bulk-phase catalysis, strongly indicate that the paused enzyme corresponds to the inactive state of F1-ATPase previously known as the ADP-Mg inhibited form in which F1-ATPase fails to release ADP-Mg from catalytic sites. The pausing position of the γ subunit deviates from the ATP-waiting position and is most likely the recently found intermediate 90° position.

Original languageEnglish
Pages (from-to)13649-13654
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number24
Publication statusPublished - 2001 Nov 20
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • General

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    Hirono-Hara, Y., Noji, H., Nishiura, M., Muneyuki, E., Hara, K. Y., Yasuda, R., Kinosita, K., & Yoshida, M. (2001). Pause and rotation of F1-ATPase during catalysis. Proceedings of the National Academy of Sciences of the United States of America, 98(24), 13649-13654.