Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/3814

Title

Modeling the chemomechanical properties of rotary F1-ATPase molecular motor

Author(s)

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

Abstract

F1-ATPase is a unique enzyme. The hydrolysis (or synthesis) of ATP into ADP and Pi produces an energy transformation from chemical energy to mechanical energy with exceptionally high efficiency. This energy transducing molecular motor is increasingly regarded as a key to the fundamental cellar motions and the nanobiotechnology. To fully understand the chemomechanical mechanism of the rotation of F1-ATPase, we propose a functional computation model based on some experimental results. We show that the torsional energy and stepwise rotation are regulated by a series of near-equilibrium reactions, with fitting parameters such as the rate constants, ATP concentration and the statistical steps, etc. The rotational characteristic, as demonstrated in experimental work done by others, may behave by the Michaelis-Menten kinetics.

Publication type

Conference paper

Research centre

Swinburne University of Technology. Centre for Molecular Simulation

Research centre

Swinburne University of Technology. School of Information Technology

Source

Proceedings of the 7th Australian Molecular Modelling Conference (MM2001), Canberra, Australian Capital Territory, Australia, 04-07 October 2001 / Ivan V. Rostov and Jill E. Gready (eds.), p. 54

Publication year

2001

Keyword(s)

ATP concentration;  F1-ATPase;  Molecular structure

Publisher

Australian National University