Superoxide dismutases-a review of the metal-associated mechanistic variations

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Abstract

uperoxide dismutases are enzymes that function to catalytically convert superoxide radical to oxygen and hydrogen peroxide. These enzymes carry out catalysis at near diffusion controlled rate constants via a general mechanism that involves the sequential reduction and oxidation of the metal center, with the concomitant oxidation and reduction of superoxide radicals. That the catalytically active metal can be copper, iron, manganese or, recently, nickel is one of the fascinating features of this class of enzymes. In this review, we describe these enzymes in terms of the details of their catalytic properties, with an emphasis on the mechanistic differences between the enzymes. The focus here will be concentrated mainly on two of these enzymes, copper, zinc superoxide dismutase and manganese superoxide dismutase, and some relatively subtle variations in the mechanisms by which they function.
Original languageUnknown
Pages (from-to)263-274
JournalBiochimica Et Biophysica Acta-Proteins And Proteomics
Volume1804
Issue number2
DOIs
Publication statusPublished - 1 Jan 2010

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