Abstract
The complex kinetic behaviour of p-methylbenzyl hydroperoxide in its inhibitory action on horse liver alcohol dehydrogenase was examined. The kinetic patterns are markedly different at very low (<10−8 M) and high (> 10−7 M) hydroperoxide concentrations. In both cases very low inhibition constants (4nM and 14nM, respectively) were found. A possihle mechanistic model based on these results is discussed.