A combined quantum mechanical/molecular mechanical model of the potential energy surface of ester hydrolysis by the enzyme phospholipase A2
Abstract
A combined molecular orbital/molecular mechanical computational model has been developed to study the potential energy surface of catalysis by the enzyme phospholipase A2. By the integration of molecular mechanical and quantum mechanical forces, the model allows the geometry optimisation of a molecule within a large and complex environment, such as the enzyme active site. The method has been applied to an examination of the role of histidine in the hydrolysis of an ester by phospholipase A2. Proton transfer to and from the imidazole ring of histidine is shown to be a valid mechanism, in that it occurs with minimal structural change and against a favourable potential energy surface.
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