Abstract
Cluster model: Large active-site models (see figure) are used to investigate the selectivity of limonene epoxide hydrolase, both the wild type and mutants optimized through directed evolution. Good agreement is found between theory and the experimental data, thus demonstrating that the quantum chemical cluster approach can be a powerful tool in the field of asymmetric biocatalysis.
Highlights
Quantum chemical models of enzyme active sites have in recent years proven to be a very powerful tool in the elucidation of enzymatic reaction mechanisms.[1]
The accuracy of modern density functional theory (DFT) methods has been proven to be sufficiently high to achieve this. These methods have in recent years been applied very successfully to a multitude of problems in the field of asymmetric homogenous catalysis.[4]
Modeling enzymatic enantioselectivity with the cluster approach has remained somewhat out of reach because larger active-site models are in general required to create the chiral environment provided by the enzyme
Summary
Quantum chemical models of enzyme active sites have in recent years proven to be a very powerful tool in the elucidation of enzymatic reaction mechanisms.[1]. To examine the capabilities of the cluster approach in terms of reproducing enantioselectivity and mutational effects we have chosen to focus on the enzyme limonene epoxide hydrolase (LEH) from rhodoccoccus erythropolis as a test case.
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