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. Mn(2+) 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 Mn(2+) were almost always additive. Chelating agents inhibited the Mn(2+)-catalysed reaction, but had either no effect or a slight accelerating effect on the peroxidase-catalysed reaction. It is concluded that Mn(2+) does not function as cofactor in the peroxidase-catalysed oxidation.