Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/4291

Title

Operating mechanism and chemomechanics of the F1-ATPase molecular motor

Author(s)

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

Abstract

Enzyme F1-ATPase catalyzes the hydrolysis of ATP and converts chemical energy into mechanical rotation with exceptionally high efficiency. It performs cellular functions like a rotary energy-transducing molecular motor and thus promises unique applications in nanobiotechnology. To better understand the operating mechanism and chemomechanics of F1-ATPase, we propose a simulation model based on the binding-change schemes, 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 ATP molecules are hydrolyzed. An effective 'ratchet' drag is also derived to account the motor's unidirectional spin. Complex schemes of binding-changes may exist in the F1-ATPase motor at different operating conditions. The chemomechanics described in this work is of fundamental importance to all ATP-fueled motor proteins.

Publication type

Conference poster

Research centre

Swinburne University of Technology. Centre for Molecular Simulation

Source

Proceedings of the 11th International Conference on Intelligent Systems for Molecular Biology (ISMB 2003), Brisbane, Queensland, Australia, 29 June-03 July 2003, Bioinformatics (v. 19, Supplement 1)

Publication year

2003

Publisher

Oxford University Press

ISSN

1367-4803

Publisher URL

http://www.iscb.org/ismb2003/posters/mingATit.swin.edu.au_486.html