Open AccessStudies in peroxidase action I —The oxidation of aniline
Author(s) -
P. J. G. Mann,
B. C. Saunders
Publication year - 1935
Publication title -
proceedings of the royal society of london. series b, biological sciences
Language(s) - English
Resource type - Journals
eISSN - 2053-9193
pISSN - 0080-4649
DOI - 10.1098/rspb.1935.0075
Subject(s) - peroxidase , substrate (aquarium) , chemistry , guaiacol , aniline , pyrogallol , enzyme , oxidative enzyme , organic chemistry , biochemistry , biology , ecology
The production of colours by the action of the enzyme peroxidase on various amino and phenolic compounds has been recorded from time to time, but such reactions have, in general, been regarded merely as tests for the presence of peroxidase, and the nature of the coloured products has been determined only in a few instances. The fairly wide distribution of the enzyme, more particularly in plants, suggests that it has considerable biological importance, but the role that it plays in metabolic processes has not yet been elucidated. From the work of Elliott (1932,a, b ), it would appear that the enzyme is not concerned with general oxidative katabolism since it does not attack the majority of amino-acids, fatty acids, and carbohydrates. On the other hand, where the products of oxidation have been investigated, they have proved to be, in general, of higher molecular weight than the substrate. Thus, for example, guaiacol is oxidized to tetraguaiacol (Bertrand, 1903), pyrogallol to purpurogallin (Willstätter and Heiss, 1923), ando -phenylene diamine to 2:3-diamino-diphenazine (Chodat, 1925). It may well be an inherent property of the molecule which is causing condensation in the above cases, and it does not therefore necessarily follow that the enzyme is facilitating coupling of the substrate molecules as well as causing oxidation.