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
[1]   STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].
ABRAHAMS, JP ;
LESLIE, AGW ;
LUTTER, R ;
WALKER, JE .
NATURE, 1994, 370 (6491) :621-628
[2]   Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging [J].
Adachi, K ;
Yasuda, R ;
Noji, H ;
Itoh, H ;
Harada, Y ;
Yoshida, M ;
Kinosita, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (13) :7243-7247
[3]  
Adachi K, 2003, METHOD ENZYMOL, V361, P211
[4]   The unbinding of ATP from F1-ATPase [J].
Antes, I ;
Chandler, D ;
Wang, HY ;
Oster, G .
BIOPHYSICAL JOURNAL, 2003, 85 (02) :695-706
[5]   Stepping rotation of F1-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly [J].
Ariga, T ;
Masaike, T ;
Noji, H ;
Yoshida, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (28) :24870-24874
[6]   The rotary motor of bacterial flagella [J].
Berg, HC .
ANNUAL REVIEW OF BIOCHEMISTRY, 2003, 72 :19-54
[7]  
Berg J. M., 2001, Biochemistry, V5th
[8]   Conformational dynamics of the F1-ATPase β-subunit:: A molecular dynamics study [J].
Böckmann, RA ;
Grubmüller, H .
BIOPHYSICAL JOURNAL, 2003, 85 (03) :1482-1491
[9]   Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthase [J].
Böckmann, RA ;
Grubmüller, H .
NATURE STRUCTURAL BIOLOGY, 2002, 9 (03) :198-202
[10]   Stepwise rotation of the γ-subunit of EFoF1-ATP synthase during ATP synthesis:: a single-molecule FRET approach [J].
Börsch, M ;
Diez, M ;
Zimmermann, B ;
Trost, M ;
Steigmiller, S ;
Gräber, P .
MANIPULATION AND ANALYSIS OF BIOMOLECULES, CELLS AND TISSUES, 2003, 4962 :11-21