Glutathione peroxidase-like activity of simple selenium compounds. Peroxides and the heterocyclic N-oxide resazurin acting as O-atom donors.

Selenite and selenocystamine [(CyaSe)2] efficiently activate the decomposition of H2O2 by GSH and by other thiols, as demonstrated using a leuco crystal violet POD-based H2O2 assay which is applicable (unlike other assays) also in presence of thiols. The GPx-like activities were estimated to be 3.6 and 2.7 mumol H2O2/min per mumol SeO3(2-) and (CyaSe)2, respectively. Both selenium compounds also activate reduction of the heterocyclic N-oxide resazurin (RN-->O) to resorufin (RN) by GSH; H2O2 competes with reduction of this dye. GSSeH and CyaSeH, formed by interaction of GSH with SeO3(2-) and (CyaSe)2, respectively, are likely to be the active reductants. CyaSeH, generated gamma-radiolytically from (CyaSe)2, exhibits an absorption peak at 243 nm and is removed by H2O2 with a rate constant of 9.7 x 10(2) M-1 s-1, and slightly slower by hydroperoxides. We have no evidence for one-electron interactions between GSSeH or CyaSeH and H2O2, with formation of free radical intermediates, as previously proposed in the case of selenium-activated reduction of cytochrome c by GSH (Levander et al., Biochemistry 23, 4591-4595 (1973)). Our results can be explained by O-atom transfer from the substrate to the active selenol group, RSeH + H2O2 (RN-->O)-->RSeOH + H2O (RN), and recycling of RSeOH to RSeH (+ H2O) by GSH, analogous to the selenenic acid pathway of GPx. The substrate specificity appears to be different, however, in that GPx is unable to catalyse RN-->O reduction, and GSSeH hardly catalyses the decomposition of cumene- or t-butyl-hydroperoxide; CyaSeH, on the other hand, is active also with the hydroperoxides. RN-->O is reduced to RN also by certain oxidizing free radicals, e.g. by the thiyl CyaS.., O-atom transfer may in this case lead to the generation of reactive oxyl radicals.