TCB Publications - Abstract
Markus Dittrich, Shigehiko Hayashi, and Klaus Schulten. On the mechanism of ATP hydrolysis in F1-ATPase. Biophysical Journal, 85:2253-2266, 2003. (PMC: 1303451)
-ATP synthase.
The water soluble 
part of the enzyme
can also work in reverse and utilize the chemical energy released
during ATP hydrolysis to generate mechanical motion.
Despite the availability of a large amount of biochemical
data and several X-ray crystallographic structures of ,
there still remains a considerable lack of understanding as
to how this protein efficiently converts the chemical energy
released during the reaction
into mechanical motion of the stalk.
We report here an ab initio QM/MM study
of ATP hydrolysis in the 
catalytic site of .
Our simulations provide an atomic level description of
the reaction path, its energetics,
and the interaction of the nucleotide with the protein
environment during catalysis. The simulations suggest that the
reaction path with the lowest potential
energy barrier proceeds
via nucleophilic attack on the 
-phosphate involving
two water molecules.
Furthermore, the ATP hydrolysis reaction in
is found to be endothermic, demonstrating that the catalytic
site is able to support the synthesis of ATP and does not promote ATP
hydrolysis in the particular conformation studied
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