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)


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.


Horseradish Peroxidase Glutathione Peroxidase Thiyl Radical Sulfinic Acid Superoxide Dismu 
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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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