Abstract
Superoxide dismutase (SOD) and superoxide reductase (SOR) enzymes defend organisms from the toxic superoxide radical. Superoxide is directly damaging to biological systems, and adventitious superoxide reduction generates the highly reactive hydroxyl radical. SOD enzymes, which are classified by their metal-dependencies (Fe, Mn, Ni, or Cu/Zn), disproportionate superoxide to dioxygen and hydrogen peroxide at diffusion-controlled rates. Experimental and computational investigations have offered important insights into the mechanisms by which SODs achieve such rapid reaction rates. The Fe-dependent SOR enzyme mediates only the superoxide reduction reaction. Experimental studies of SOR have shown how proteins control the decay pathways of enzymatic intermediates.
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