Title

Docking and simulation study of the enantiospecificity of chiral epoxidation reactions catalyzed by chloroperoxidase

Document Type

Thesis

Degree

Master of Science (MS)

Department

Chemistry

First Advisor's Name

David Chatfield

First Advisor's Committee Title

Committee Chair

Second Advisor's Name

David Becker

Third Advisor's Name

Alexander Mebel

Date of Defense

11-15-2006

Abstract

Chloroperoxidase (CPO), a 298-residue glycosylated protein from the fungus Caldariomyces fumago, is probably the most versatile heme enzyme yet discovered. Interest in CPO as a catalyst is based on its power to produce enantiomerically enriched products. Recent research has focused its attention on the ability of CPO to epoxidize alkenes in high regioselectivity and enantioselectivity as an efficient and environmentally benign alternative to traditional synthetic routes.

There has been little work on the nature of ligand binding, which probably controls the regio- and enantiospecifity of CPO. Consequently it is here that we focus our work. We report docking calculations and computer simulations aimed at predicting the enantiospecificity of CPO-catalyzed epoxidation of three model substrates. On the basis of this work candidate mutations to improve the efficiency of CPO are predicted. In order to accomplish these aims, a simulated annealing and molecular dynamics protocol is developed to sample potentially reactive substrate/CPO complexes.

Identifier

FI14031601

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