A comparison of horseradish peroxidase and manganese ions as catalysts for the oxidation of dihydroxyfumaric acid
- 1 April 1968
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 107 (4) , 581-587
- https://doi.org/10.1042/bj1070581
Abstract
With horseradish peroxidase as catalyst the main product was dihydroxytartrate, but small amounts of glycolaldehyde, mesoxalic semialdehyde, mesoxalate and possibly glyoxal were also formed. Mn2+ catalysis gave rise only to mesoxalate and oxalate. When oxygen uptake was followed by a manometric method the rate of the peroxidase-catalysed reaction was proportional to oxygen concentration and marked inhibition by cyanide was obtained only at low buffer concentration. The catalytic effects of peroxidase and Mn2+ were almost always additive. Chelating agents inhibited the Mn2+-catalysed reaction, but had either no effect or a slight accelerating effect on the peroxidase-catalysed reaction. It is concluded that Mn2+ does not function as cofactor in the peroxidase-catalysed oxidation.This publication has 4 references indexed in Scilit:
- OXIDASE AND PEROXIDASE REACTIONS IN THE PRESENCE OF DIHYDROXYMALEIC ACIDJournal of Biological Chemistry, 1952
- PROCEDURES FOR THE MICROESTIMATION OF NITROGENOUS PHOSPHATIDE CONSTITUENTSJournal of Biological Chemistry, 1951
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951
- The 2:4-dinitrophenylhydrazones of some ketonic acids of biological importanceBiochemical Journal, 1932