Studies of the chlorinating intermediate of horseradish peroxidase

The chlorinating intermediate of horseradish peroxidase, Compound X, is the only know stable enzymatic halogenating intermediate known. The optical spectrum of Compound X is virtually identical to the optical spectrum of Compound II. Titration of Compound X by a single electron donor, potassium ferrocyanide reduces the Compound II type spectrum to a native type spectrum. Incubation of these titrated solutions with the chlorine acceptor, monochlorodimedone, MCD, shows that titrated Compound X retains a chlorine. The chlorinating properties of Compound X is therefore independent of the oxidation state of the iron. Furthermore, the optical spectra indicate that the chlorine moiety in Compound X is not associated with the heme prosthetic group. The location of the chlorine moiety in Compound X must therefore be associated with an amino acid residue. The identification of this modified residue as ASP-43 is proposed based on spectroscopic and kinetic evidence.

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

2011

Author dc:creator

• Suh, Young Jin

Contributors dc:contributor

• Hager, Lowell P.

• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1990 Suh, Young Jin

Language dc:language

eng

Identifier

AAI9114427
(UMI)AAI9114427

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21106