Abstract
Superoxide dismutase (SOD) is a ubiquitous enzyme of aerobic organisms that protects against the toxic effects of dioxygen metabolism. SOD catalyzes the dismutation of the superoxide radical, O- 2, to molecular oxygen and hydrogen peroxide through the alternate reduction and oxidation of the active site metal ion (Cu, Mn, or Fe)1: Open image in new window Cu, Zn SOD occurs almost entirely in eukaryotic cells, while Mn or Fe SODs occur predominantly in prokaryotes and mitochondria. The catalytic rate of SOD is very rapid (2 × 109 M-1sec-1),2 suggesting the evolution of an optimal active site for the recognition and chemical catalysis of the substrate by the enzyme. This remarkably high catalytic rate makes the enzyme a simple model system in which to study the role of electrostatic forces in molecular recognition.
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