A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F1-ATPase.

ABSTRACT: Although the binding change mechanism of rotary catalysis by which F1-ATPase hydrolyzes ATP has been supported by equilibrium, kinetic, and structural observations, many questions concerning the function remain unanswered. Because of the importance of this enzyme, the search for a full understanding of its mechanism is a key problem in structural biology. Making use of the results of free energy simulations and experimental binding constant measurements, a model is developed for the free energy change during the hydrolysis cycle. This model makes possible the development of a kinetic scheme for ATP hydrolysis by F1-ATPase, in which the rate constants are associated with specific configurations of the beta subunits. An essential new element is that the strong binding site for ADP,Pi is show

SUBMITTER: Gao YQ 

PROVIDER: S-EPMC208758 | biostudies-literature | 2003 Sep

REPOSITORIES: biostudies-literature