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Superoxide Dismutases: Studies of Structure and Mechanism

  • Irwin Fridovich
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

Superoxide dismutases are enzymes of defense which serve to protect respiring cells against a product of their own respiration. This is achieved by a catalytic scavenging of the superoxide radical which, surprisingly, is a rather commonplace intermediate of the reduction of oxygen. The reaction catalyzed is:
$$O_2^-+O_2^-+2{H^+ }H{}_2+O_2$$
Enhancing the rate of this particular reaction may appear to “be a peculiar undertaking for an enzyme, since this reaction is reasonably rapid, even in the absence of catalysis and since several transition metal cations serve as effective catalysts. Nevertheless superoxide dismutases are indispensable because they operate with ultimate efficiency and are present in abundance, whereas free transition metal cations are less effective and are not plentiful inside cells. It is a fact that all of the superoxide dismutase activity, which can be measured in crude extracts of such diverse materials as erythrocytes, mammalian liver or Escherichia coli, can be accounted for in terms of the superoxide dismutases which they contain. There is thus no significant superoxide dismutase activity in these extracts save that due to these enzymes.

Keywords

Superoxide Dismutase Imidazole Ring Superoxide Dismutase Activity Transition Metal Cation Intrachain Disulfide Bond 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Irwin Fridovich
    • 1
  1. 1.Department of BiochemistryDuke University Medical CenterDurhamUSA

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