Abstract
F 1 -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 α 3 β 3 ring. Here, we show that the rotation of F 1 -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 F 1 -ATPase previously known as the ADP-Mg inhibited form in which F 1 -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.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:35 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 9:08 a.m.) |
Indexed | 2 weeks, 5 days ago (Aug. 6, 2025, 9:21 a.m.) |
Issued | 23 years, 9 months ago (Nov. 13, 2001) |
Published | 23 years, 9 months ago (Nov. 13, 2001) |
Published Online | 23 years, 9 months ago (Nov. 13, 2001) |
Published Print | 23 years, 9 months ago (Nov. 20, 2001) |
@article{Hirono_Hara_2001, title={Pause and rotation of F 1 -ATPase during catalysis}, volume={98}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.241365698}, DOI={10.1073/pnas.241365698}, number={24}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Hirono-Hara, Yoko and Noji, Hiroyuki and Nishiura, Masaya and Muneyuki, Eiro and Hara, Kiyotaka Y. and Yasuda, Ryohei and Kinosita, Kazuhiko and Yoshida, Masasuke}, year={2001}, month=nov, pages={13649–13654} }