Complex cooperativity of ATP hydrolysis in the F(1)-ATPase molecular motor.
F(1)-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F(1)-ATPase does not follow the widely believed Michaelis-Menten mechanism. Instead, the hydrolysis mechanism behaves in an ATP-dependent manner. We develop a model for enzyme kinetics and hydrolysis cooperativity of F(1)-ATPase which involves the binding-state changes to the coupling catalytic reactions. The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F(1)-ATPase. This complexity may be taken into account to resolve the arguments on the binding change mechanism in F(1)-ATPase.
Liu
Ming S
MS
Centre for Molecular Simulation, Swinburne University of Technology, PO Box 218, Hawthorn, Melbourne, Victoria 3122, Australia. ming@it.swin.edu.au
Todd
B D
BD
Sadus
Richard J
RJ
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D003627:Data Interpretation, Statistical; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D020409:Molecular Motor Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases