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Copper-zinc superoxide dismutase (SOD) is considered one of the most important mammalian antioxidant defenses and plays a relevant role due to its main function in catalyzing the dismutation of superoxide anion to oxygen and hydrogen peroxide. However, interaction between SOD and H 2 O 2 produced a strong copper-bound oxidant (Cu(II) • OH) that seems able to contrast the self-inactivation of the enzyme or oxidize other molecules through its peroxidase activity. The bicarbonate presence enhances the peroxidase activity and produces the carbonate anion radical (CO 3  •- ). CO 3  •- is a freely diffusible reactive species capable of oxidizing several molecules that are unwieldy to access into the reactive site of the enzyme. Cu(II) • OH oxidizes bicarbonate to the CO 3  •- , which spreads out of the binding site and oxidizes hypotaurine and cysteine sulfinic acid to the respective sulfonates through an efficient reaction. These findings suggest a defense role for sulfinates against the damage caused by CO 3  •- . The effect of hypotaurine and cysteine sulfinic acid on the CO 3  •- -mediated oxidation of the peroxidase probe ABTS to ABTS cation radical (ABTS •+ ) has been studied. Both sulfinates are able to inhibit the oxidation of ABTS mediated by CO 3  •- . The effect of hypotaurine and cysteine sulfinic acid against SOD inactivation by H 2 O 2 (~42% protection of enzyme activity) has also been investigated. Interestingly, hypotaurine and cysteine sulfinic acid partially avoid the H 2 O 2 -mediated SOD inactivation, suggesting that the two sulfinates may have access to the SOD reactive site and preserve it by reacting with the copper-bound oxidant. In this way hypotaurine and cysteine sulfinic acid not only intercept CO 3  •- which could move out from the reactive site and cause oxidative damage, but also prevents the inactivation of SOD.

advances in experimental medicine and biology

Carbonate Anion Radical Generated by the Peroxidase Activity of Copper-Zinc Superoxide Dismutase: Scavenging of Radical and Protection of Enzyme by Hypotaurine and Cysteine Sulfinic Acid