Formation of compound I by the reaction of catalase with peroxoacetic acid
- 1 November 1972
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 130 (2), 411-415
- https://doi.org/10.1042/bj1300411
Abstract
1. The formation of Compound I by the reactions of bacterial and ox liver catalases with peroxoacetic acid was examined. In both cases the process occurs almost entirely by reaction of catalase with un-ionized peroxoacetic acid molecules. The result suggests an important role for the bound peroxidic proton in the enzyme–substrate interaction. 2. The peroxidatic properties of the Compounds I formed when peroxoacetic acid was used were examined by studying the oxidations of ethanol and formate; the results closely resemble those previously reported when H2O2 and alkyl hydroperoxides were used. 3. Compound I formed with bacterial catalase and peroxoacetic acid is remarkably stable in the absence of added donor and the preparation has considerable potential for detailed studies of the nature of this intermediate.Keywords
This publication has 9 references indexed in Scilit:
- The Peroxidase Activity of DeuteroheminEuropean Journal of Biochemistry, 1971
- Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.Physiological Reviews, 1970
- Dissociation of catalase. A correlation between changes in sedimentation and spectroscopic properties accompanying dissociation of bacterial catalase in alkaline solutionBiochemical Journal, 1970
- Catalatic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic action of ferrihaemsBiochemical Journal, 1970
- Peroxidatic activity of catalaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- The catalase–hydrogen peroxide system. A theoretical appraisal of the mechanism of catalase actionBiochemical Journal, 1968
- The catalase–hydrogen peroxide system. Role of sub-units in the thermal deactivation of bacterial catalase in the absence of substrateBiochemical Journal, 1968
- Primary compounds of catalase and peroxidaseBiochemical Journal, 1961
- The enzyme-substrate compounds of bacterial catalase and peroxidesBiochemical Journal, 1950