title: How the Proximal Pocket May Influence the Enantiospecificities of Chloroperoxidase-Catalyzed Epoxidations of Olefins.
abstract: Chloroperoxidase-catalyzed enantiospecific epoxidations of olefins are of significant biotechnological interest. Typical enantiomeric excesses are in the range of 66%-97% and translate into free energy differences on the order of 1 kcal/mol. These differences are generally attributed to the effect of the distal pocket. In this paper, we show that the influence of the proximal pocket on the electron transfer mechanism in the rate-limiting event may be just as significant for a quantitatively accurate account of the experimentally-measured enantiospecificities.
authors: Department of Chemistry and Biochemistry, Florida International University, 11200 SW 8th St., Miami, FL 33199, USA. omorozov@fiu.edu.
authors: Alexander N
authors: AN
authors: Morozov
authors: Department of Chemistry and Biochemistry, Florida International University, 11200 SW 8th St., Miami, FL 33199, USA. chatfiel@fiu.edu.
authors: David C
authors: DC
authors: Chatfield
mesh_terms: D000475:Alkenes / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D002711:Chloride Peroxidase / Q000378:metabolism*; D004852:Epoxy Compounds / Q000737:chemistry / Q000378:metabolism; D006860:Hydrogen Bonding; D013237:Stereoisomerism
chemical_list: D000475:Alkenes; D004852:Epoxy Compounds; D002711:Chloride Peroxidase
keywords: Compound I; catalytic reactivity; chloroperoxidase; cytochrome P450; density functional theory; epoxidation; helix dipole; heme-thiolate enzymes; hydrogen bonding; proximal pocket