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Title

Kinetics and chemomechanical properties of the F[sub 1]-ATPase molecular motor

Author(s)

Liu, Ming S.;  Todd, B. D.;  Sadus, Richard J.

Abstract

F1-ATPase hydrolyzes ATP into ADP and Pi and converts chemical energy into mechanical rotation with exceptionally high efficiency. This energy-transducing molecular motor increasingly attracts interest for its unique cellular functions and promising application in nanobiotechnology. To better understand the chemomechanics of rotation and loading dynamics of F1-ATPase, we propose a computational model based on enzyme kinetics and Langevin dynamics. We show that the torsional energy and stepwise rotation can be regulated by a series of near-equilibrium reactions when nucleotides bind or unbind, as well as characterized by an effective 'ratchet' drag coefficient and a fitting chemomechanic coefficient. For the case of driving an actin filament, the theoretical load-rotation profile is analyzed and comparison with experimental data indicates reasonable agreement. The chemomechanics described in this work is of fundamental importance to all ATP-fueled motor proteins.

Publication type

Journal article

Research centre

Swinburne University of Technology. Centre for Molecular Simulation

Source

Journal of Chemical Physics, Vol. 118, no. 21 (2003), pp. 9890-9898

Publication year

2003

Keyword(s)

Biomechanics;  Direct energy conversion;  Molecular biophysics;  Nanotechnology;  Proteins;  Transducers

Publisher

American Institute of Physics

ISSN

0021-9606

Publisher URL

http://dx.doi.org/10.1063/1.1568083

Copyright

Copyright © 2003 American Institute of Physics. Published version of this paper reproduced here in accordance with the copyright policy of the publisher.

Full text

Peer reviewed