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One- and Two-Electron Oxidation of Reduced Glutathione by Peroxidases

  • Ronald P. Mason
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 197)

Abstract

The oxidation of glutathione by horseradish peroxidase or lactoperoxidase forms a thiyl free radical, as demonstrated with the spin-trapping ESR technique. Reactions of this thiyl free radical result in oxygen consumption, which is inhibited by the radical trap 5,5-dimethyl-l-pyrroline-Noxide. In contrast to L-cysteine oxidation, glutathione oxidation is highly hydrogen peroxide-dependent. The oxidation of glutathione by glutathione peroxidase forms GSSG without forming a thiyl radical intermediate except in the presence of the thiyl radical-generating horseradish peroxidase.

Keywords

Horseradish Peroxidase Glutathione Peroxidase Thiyl Radical Sulfinic Acid Superoxide Dismu 
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 1986

Authors and Affiliations

  • Ronald P. Mason
    • 1
  1. 1.Laboratory of Molecular BiophysicsNational Institute of Environmental Health SciencesResearch Triangle ParkUSA

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