Glutathione Peroxidase-Like Activity of Simple Selenium Compounds. Peroxides and the Heterocyclic N-Oxide Resazurin Acting as O-Atom Donors
| Autor: | Walter A. Prütz |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
biology Radical Glutathione peroxidase Cytochrome c Selenol chemistry.chemical_element Substrate (chemistry) Glutathione Selenenic acid Photochemistry Medicinal chemistry General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound chemistry biology.protein Selenium |
| Zdroj: | Zeitschrift für Naturforschung C. 50:209-219 |
| ISSN: | 1865-7125 0939-5075 |
| DOI: | 10.1515/znc-1995-3-409 |
| Popis: | Selenite and selenocystamine [(CyaSe)2] efficiently activate the decomposition of H2O2 y 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 μmol H2O2/min per μmol 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 γ-radiolytically from (CyaSe)2, exhibits an absorption peak at 243 nm and is removed by H2O2 with a rate constant of 9.7x102 ᴍ-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. |
| Databáze: | OpenAIRE |
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