The lass of enzymatic activity of lactate dehydrogenase was studied in several ascorbate, iron and hydrogen peroxide metal catalyzed oxidation solutions in which the initial concentration of each reactant was varied independently. Nonmonotonic concentration dependencies of enzymatic inactivation were observed for all three reactants, with minimum activity levels occurring in the 0.1 to 8 mM range. A first effort has been made to predict these concentration dependencies with a mathematical simulation model. The model consisted of the most commonly reported reactions and assumed that protein damage occurred through reaction with the hydroxyl radical. The simulation predicted nonmonotonic concentration dependencies of enzyme inactivation on each of the reactants. The predicted concentrations of the minima differed from the experimentally observed points by a factor of 2 to 4. Mathematically the minima occurred because each reactant was reported to react with hydroxyl radicals and form less reactive compounds. The plausibility that competition caused or contributed to the extrema was further explored-with experimental competition studies between peroxide and the radical scavenger dimethylsulfoxide. A point of maximum hydroxyl radical formation was observed with increasing peroxide concentration. This maxima corresponded to the point of maximum lactated dehydrogenase damage observed with increasing peroxide concentration.