Spectral studies on the oxidation of organic sulfides (thioanisoles) by horseradish peroxidase compounds I and II.
Using both rapid-scan and conventional spectrophotometry, oxygenation of p-substituted thioanisoles by horseradish peroxidase compounds I and II was investigated at pH 5, 7 and 9. The pH-jump technique was applied to the compound II reactions at acidic and neutral pH. The rate of oxidation of the sulfides is dependent on pH, concentration of substrate and on the different substituents in the para position of the benzene ring. Our results, based on transient state observations of the enzyme intermediates, are in agreement with the results of Kobayashi, S., Minoru, N., Kimura, T. and Schaap, A.P. (Biochemistry (1987) 26, 5019-5022), obtained using 18O-labelling and studies of product formation, in which formation of a sulfur cation radical from compound I is proposed. We consider two reaction mechanisms for the compound II reaction: one a one-electron oxidation of the thioanisole, analogous to the compound I reaction, and the other, the attack of the hydroxyl radical originating from compound II on the sulfur-cation radical.
Pérez
U
U
Department of Chemistry, University of Alberta, Edmonton, Canada.
Dunford
H B
HB
D000840:Anisoles / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D013057:Spectrum Analysis; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D013440:Sulfides / Q000378:metabolism*
D000840:Anisoles; D013438:Sulfhydryl Compounds; D013440:Sulfides; D006735:Horseradish Peroxidase; D010544:Peroxidases