Reduction and inactivation of superoxide dismutase by hydrogen peroxide.

Reactions of H(2)O(2) with superoxide dismutase were studied by e.p.r. (electron paramagnetic resonance) spectroscopy and other methods. In agreement with earlier work, the Cu(2+) of the enzyme is reduced by H(2)O(2), although the reaction does not go to completion and its kinetics are not simple. With dilute enzyme the time for half-reduction with 9mm-H(2)O(2) is about 150ms. It is suggested that the reaction is a one-electron reduction, involving liberation of O(2) (-). On somewhat more prolonged exposure to H(2)O(2), the enzyme is inactivated. For enzyme in dilute solution and over a limited range of H(2)O(2) concentrations, inactivation is first-order with respect to enzyme and reagent, with k=3.1m(-1).s(-1) at 20-25 degrees C. Inactivation is accompanied by marked changes in the e.p.r. and visible spectra and appears to be associated with destruction of one histidine residue per subunit. It is suggested that this histidine is close to the metal in the native enzyme and essential for its enzymic activity.