Chloroperoxidase-catalyzed oxidation of N-methyl-4-chloroaniline
Chloroperoxidase catalyzed the H2O2 oxidative conversion of N-methyl-4-chloroaniline to 4-chloronitrosobenzene, 4-chloroaniline and a mixture of complex products.
Chloroperoxidase-catalysed oxidation of 4-chloroaniline to 4-chloronitrosobenze.
The incubation of 4-chloroaniline with chloroperoxidase and H2O2 resulted in a rapid formation of 4-chloronitrosobenzene. This enzymic oxidation displayed a pH optimum at 4.4 with a Km of 8.1x10(-4)M and catalytic-centre activity of 312. The initial rate of the reaction was strongly affected by the presence of halide ions. 4-Chlorophenylhydroxylamine was even more rapidly converted into the nitroso compound. A reaction mechanism is proposed on the basis of currently accepted theory for the catalytic action of chloroperoxidae. A noteworthy aspect of this new reaction is the difference in the products previously reported for the action of classical peroxidases on anilines and the single nitroso product resulting from chloroperoxidase oxidation.
Studies in peroxidase action. 18. The oxidation of 4-chloraniline--further studies.
Abstract The main features of the peroxidation of 4-chloroaniline are the production of 2-amino-5-(4-chloroanilino-)benzoquinone-di-4-chloroanil in high yield and the elimination of chloride ion. Two intermediates, (N-(4-chlorophenyl-) p -phenylenediamine and 4-chloro-N 2 -(4-chlorophenyl-) o -phenylenediamine), have been proposed; and it has been shown that while the former may be an intermediate the latter is not: the latter gives rise to 2-amino-5-chlorobenzoquinone-di-4-chloroanil, a compound which we have detected in the 4-chloroaniline oxidation products. This compound is stable to the conditions of oxidation and is not the precursor of the main oxidation product. The relative yields of the oxidation products have been shown to depend on the initial concentration of 4-chloroaniline.