Oxidation of Alkenes by Caldariomyces Fumago Chloroperoxidase

To elucidate factors involved in the control of CPO heme N-alkylation by terminal alkenes, the epoxidation of a series of monosubstituted and 1,1-disubstituted terminal alkenes by CPO was investigated. Terminal alkenes containing a 2-methyl substituent did not inactivate CPO even when the corresponding monosubstituted alkene inactivated the enzyme. The inverse correlation between the epoxidation enantioselectivity and the tendency to heme N-alkylation suggested that CPO inactivation by terminal alkenes is controlled by steric properties of the alkene and the enzyme active site. (Abstract shortened by UMI.).

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Dexter, Annette Faith

Contributors dc:contributor

• Hager, Lowell P.

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI9717270

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84876