1. A re-examination of the catalase–hydrogen peroxide reaction at high substrate concentrations, by using the quenched-flow technique, reveals a more complex kinetic behaviour than that previously reported. At constant reaction time the catalatic process obeys Michaelis–Menten kinetics, but the apparent Michaelis constant is markedly time-dependent, whereas the conventional catalase activity is independent of time. 2. The kinetics of the ‘time effect’ were analysed and it is suggested that the effect derives from the formation of an inactive species (thought to be catalase Compound II). The process shows Michaelis–Menten kinetics, with a Michaelis constant equal to that for the catalatic reaction in the limit of zero reaction time. 3. It has been confirmed that certain buffer components have marked inhibitory effects on the catalatic reaction and that, in unbuffered systems, catalatic activity is substantially independent of pH in the range 4·7–10·5.
- © 1968 The Biochemical Society