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Probing Enzyme-Substrate Recognition and Catalytic Mechanism in Cu,Zn Superoxide Dismutase

  • John A. Tainer
  • Robert A. Hallewell
  • Victoria A. Roberts
  • Hans E. Parge
  • Elizabeth D. Getzoff
Part of the Basic Life Sciences book series (BLSC, volume 49)

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: 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.

Keywords

Superoxide Dismutase Complete Amino Acid Sequence Zinc Superoxide Dismutase CuZn Superoxide Dismutase High Catalytic Rate 
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 1988

Authors and Affiliations

  • John A. Tainer
    • 1
  • Robert A. Hallewell
    • 1
  • Victoria A. Roberts
    • 1
  • Hans E. Parge
    • 1
  • Elizabeth D. Getzoff
    • 1
  1. 1.Dept. of Molecular BiologyResearch Institute of Scripps ClinicLa JollaUSA

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