Chemo-Mechanical Coupling in F1-ATPase Revealed by Catalytic Site Occupancy during Catalysis

被引：38

作者：

Shimo-Kon, Rieko ^{[1
]}

Muneyuki, Eiro ^{[2
]}

Sakai, Hiroshi ^{[3
]}

Adachi, Kengo ^{[1
]}

Yoshida, Masasuke ^{[4
]}

Kinosita, Kazuhiko, Jr. ^{[1
]}

机构：

[1] Waseda Univ, Dept Phys, Fac Sci & Engn, Shinjuku Ku, Tokyo 169, Japan

[2] Chuo Univ, Dept Phys, Fac Sci & Engn, Bunkyo Ku, Tokyo 112, Japan

[3] Univ Shizuoka, Dept Food & Nutr Sci, Grad Sch Nutr & Environm Sci, Shizuoka 4228526, Japan

[4] Tokyo Inst Technol, Bioresources Div, Chem Resources Lab, Midori Ku, Yokohama, Kanagawa 227, Japan

来源：

BIOPHYSICAL JOURNAL | 2010年 / 98卷 / 07期

关键词：

BOVINE HEART-MITOCHONDRIA; THERMOPHILIC BACILLUS PS3; YEAST F-1 ATPASE; NUCLEOTIDE-BINDING; MOLECULAR MACHINE; ROTATION; HYDROLYSIS; MECHANISM; SYNTHASE; SUBCOMPLEX;

D O I：

10.1016/j.bpj.2009.11.050

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

F-1-ATPase is a rotary molecular motor in which the central gamma subunit rotates inside a cylinder made of alpha(3)beta(3) subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting gamma angle defined as 0 degrees, phosphate is released at similar to 200 degrees, and ADP is released during quick rotation between 240 degrees and 320 degrees that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly.

引用

页码：1227 / 1236

页数：10

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