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

doi:10.1073/pnas.241365698

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^*

^*この研究の対応する著者

研究成果: Article › 査読

164 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	13649-13654
ページ数	6
ジャーナル	Proceedings of the National Academy of Sciences of the United States of America
巻	98
号	24
DOI	https://doi.org/10.1073/pnas.241365698
出版ステータス	Published - 2001 11月 20
外部発表	はい

ASJC Scopus subject areas

遺伝学
一般

文献へのアクセス

10.1073/pnas.241365698

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引用スタイル

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AU - Hirono-Hara, Yoko

AU - Noji, Hiroyuki

AU - Nishiura, Masaya

AU - Muneyuki, Eiro

AU - Hara, Kiyotaka Y.

AU - Yasuda, Ryohei

AU - Kinosita, Kazuhiko

AU - Yoshida, Masasuke

PY - 2001/11/20

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AB - 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.

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