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Ranguelova K, Bonini MG, Mason RP: (Bi) sulfite Oxidation by Cu,Zn-Superoxide Dismutase: Sulfite-Derived, Radical-Initiated Protein Radical Formation. Environ Health Perspect. 2010 Mar 26.
Background: Sulfur dioxide, formed during the combustion of fossil fuels, is a major air pollutant near large cities. Its two ionized forms in aqueous solution, sulfite and (bi) sulfite, are widely used as preservatives and antioxidants to prevent food and beverage spoilage. It is well known that (bi) sulfite can be oxidized by peroxidases with the formation of the very reactive sulfur trioxide anion radical (*SO3-). This free radical further reacts with oxygen to form peroxymonosulfate (-O3SOO*) anion radical and sulfate (SO4*-) anion radical. Objective: To explore the critical role of these radical intermediates in further oxidizing biomolecules, we examined the ability of copper,zinc-superoxide dismutase (Cu,Zn-SOD) to initiate this radical chain reaction using human serum albumin (HSA) as a model target. Methods: We used electron paramagnetic resonance, optical spectroscopy, oxygen uptake and immuno-spin trapping to study the protein oxidations driven by sulfite-derived radicals. Results: We found that when Cu,Zn-SOD was reacted with (bi) sulfite, the *SO3- radical was produced with the concomitant reduction of SOD-Cu (II) to SOD-Cu (I). Further, we demonstrated that sulfite oxidation mediated by Cu,Zn-SOD induced the formation of radical-derived DMPO spin-trapped human serum albumin radicals. Conclusions: Our present study suggests that protein oxidative damage resulting from (bi) sulfite oxidation promoted by Cu,Zn-SOD could be involved in oxidative damage and tissue injury in (bi) sulfite-exacerbated allergic reactions. |
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