The kinetics of the oxidation of sulfite and nitrite by horseradish peroxidase compounds I and I1 have been studied as a function of p H at 25' and ionic strength 0.11. The p H dependence of the rate of the reaction between compound I and sulfite over the p H range 2-7 is interpreted in terms of two ground state enzyme dissociations with pK, values of 5.1 and 3.3, and that for the compound I1 reaction with sulfite in terms of a single ground state enzyme dissociation with a pK, value of 3.9. Whereas the reaction between compound I and sulfite produces the native enzyme without the intermediate formation of compound 11, the reaction of compound I with nitrite yields compound 11. The second-order rate constants for the reactions of compounds I and I1 with nitrite increase linearly with increasing hydrogen ion concentration over the p H range 6-8.