Studies on the Mechanism of the Chlorination Reactions Catalyzed by Chloroperoxidase and by Horseradish Peroxidase With Chlorite

Chloroperoxidase catalyzes the dismutation of chlorite-forming chloride, chlorine dioxide, chlorate, and oxygen as products. Chloroperoxidase also catalyzes the decomposition of chlorine dioxide. Chloride, chlorate, and oxygen are the products of the decomposition of chlorine dioxide. The optimum pH for the enzymic decomposition of both chlorite and chlorine dioxide is approximately 2.75. At this pH, 1 mole of chlorine dioxide is dismutated to 0.3 mole of chloride, 0.7 mole of chlorate, and 0.17 mole of oxygen. At the same pH, the complete decomposition of 1 mole of chlorite yields 0.4 mole of chloride, 0.6 mole of chlorate, and 0.13 mole of oxygen. Kinetic parameters for the chlorite reaction have been determined. The K(,m) value for chlorite obtained from various kinetic plots was about 10 mM. The catalytic rate constant for the formation of chlorine dioxide from chlorite was about 70,000 s('-1).

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

1982

Author dc:creator

• Shahangian, Shahram

• Chemistry, Biochemistry

Identifier

(UMI)AAI8218561

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70509