OXIDATION OF GLUTATHIONE BY THE MYELOPEROXIDASE SYSTEM

  • 1 January 1982
    • journal article
    • research article
    • Vol. 31  (4) , 353-360
Abstract
Oxidation of glutathione (GSH) by the [human] myeloperoxidase (MPO) system was studied. the combination of MPO, H2O2 and a halide ion oxidized GSH. This occurred at a H2O2 concentration too low to oxidize GSH by itself. The MPO-mediated oxidation of GSH required the simultaneous presence of MPO, H2O2 and a halide ion. The system had an acid pH optimum of pH 5.5-6.0. Iodide was more effective than bromide, which in turn was more effective than chloride. The oxidative product was GSSG [oxidized glutathione], since it could be reduced back to GSH by glutathione reductase and NADPH. The MPO-mediated oxidation of GSH may be 1 mechanism by which this system damages microorganisms.