Rotation of F1-ATPase:: How an ATP-driven molecular machine may work

被引:140
作者
Kinosita, K
Adachi, K
Itoh, H
机构
[1] Okazaki Natl Res Inst, Ctr Integrat Biosci, Okazaki, Aichi 4448585, Japan
[2] Tsukuba Res Lab, Hamamatsu Photon KK, Tsukuba, Ibaraki 3002635, Japan
[3] CREST Creat & Applicat Soft Nanomachine, Hyperfunct Mol Machine Team 13, Tsukuba, Ibaraki 3002635, Japan
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2004年 / 33卷
关键词
molecular motor; single-molecule physiology; torque generation; efficiency of energy conversion; free energy;
D O I
10.1146/annurev.biophys.33.110502.132716
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
F-1-ATPase is a rotary motor made of a single protein molecule. Its rotation is driven by free energy obtained by ATP hydrolysis. In vivo, another motor, F-0, presumably rotates the F-1 motor in the reverse direction, reversing also the chemical reaction in F-1 to let it synthesize ATP. Here we attempt to answer two related questions, How is free energy obtained by ATP hydrolysis converted to the mechanical work of rotation, and how is mechanical work done on F-1 converted to free energy to produce ATP? After summarizing single-molecule observations of F-1 rotation, we introduce a toy model and discuss its free-energy diagrams to possibly answer the above questions. We also discuss the efficiency of molecular motors in general.
引用
收藏
页码:245 / 268
页数:30
相关论文
共 73 条
[31]  
Kinosita K Jr, 2000, Essays Biochem, V35, P3
[32]   A single myosin head moves along an actin filament with regular steps of 5.3 nanometres [J].
Kitamura, K ;
Tokunaga, M ;
Iwane, AH ;
Yanagida, T .
NATURE, 1999, 397 (6715) :129-134
[33]   THERMODYNAMIC ANALYSIS OF MUSCLE ATPASE MECHANISMS [J].
KODAMA, T .
PHYSIOLOGICAL REVIEWS, 1985, 65 (02) :467-551
[34]   A dynamic analysis of the rotation mechanism for conformational change in F1-ATPase [J].
Ma, JP ;
Flynn, TC ;
Cui, Q ;
Leslie, AGW ;
Walker, JE ;
Karplus, M .
STRUCTURE, 2002, 10 (07) :921-931
[35]   SYNTHESIS OF ATP FROM ADP AND INORGANIC-PHOSPHATE AT MYOSIN-SUBFRAGMENT-1 ACTIVE-SITE [J].
MANNHERZ, HG ;
SCHENCK, H ;
GOODY, RS .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1974, 48 (01) :287-295
[36]   F1-ATPase changes its conformations upon phosphate release [J].
Masaike, T ;
Muneyuki, E ;
Noji, H ;
Kinosita, K ;
Yoshida, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (24) :21643-21649
[37]   Catalytic activity of the alpha(3)beta(3)gamma complex of F-1-ATPase without noncatalytic nucleotide binding site [J].
Matsui, T ;
Muneyuki, E ;
Honda, M ;
Allison, WS ;
Dou, C ;
Yoshida, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (13) :8215-8221
[38]   Myosin-V is a processive actin-based motor [J].
Mehta, AD ;
Rock, RS ;
Rief, M ;
Spudich, JA ;
Mooseker, MS ;
Cheney, RE .
NATURE, 1999, 400 (6744) :590-593
[39]   Structure of bovine mitochondrial Fl-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis [J].
Menz, RI ;
Walker, JE ;
Leslie, AGW .
CELL, 2001, 106 (03) :331-341
[40]  
Milgrom YM, 1998, BIOCHEM J, V330, P1037