  F1-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy
into mechanical rotation. The hydrolysis reaction in F1-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 F1-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 F1-ATPase. This complexity may be
taken into account to resolve the arguments on the bindingchange mechanism in
F1-ATPase.
