Pause and rotation of F-1-ATPase during catalysis

Hirono-Hara Y; Noji H; Nishiura MMuneyuki EHara KYYasuda R

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Pause and rotation of F-1-ATPase during catalysis

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摘要

FI-ATPase is a rotary motor enzyme in which a single ATP molecule drives a 120 degrees rotation of the central gamma subunit relative to the surrounding alpha (3)beta (3) ring. Here, we show that the rotation of F-1-ATPase spontaneously lapses into long (approximate to 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 gamma subunit deviates from the ATP-waiting position and is most likely the recently found intermediate 90 degrees position.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2001年第24期|13649-13654|共6页
作者
Hirono-Hara Y; Noji H; Nishiura MMuneyuki EHara KYYasuda R;
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作者单位

Yoshida M, Tokyo Inst Technol, Chem Resources Lab, 4259 Nagatsuta, Yokohama, Kanagawa 2268503, Japan;

sych.purdue.edu;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Thermophilic bacillus ps3; Binding change mechanism; Atp synthase; Alpha(3)beta(3)gamma complex; Nucleotide-binding; F0f1-atp synthase; Inhibitory mgadp; Escherichia-coli; F1-atpase; Site;

Pause and rotation of F-1-ATPase during catalysis

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