glutathione peroxidase-like activity of amino-substituted water-soluble cyclic selenides: a shift of the major catalytic cycle in methanol

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ID: 135504
2017
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Abstract
We previously reported that water-soluble cyclic selenides can mimic the antioxidative function of glutathione peroxidase (GPx) in water through a simple catalytic cycle, in which the selenide (>Se) is oxidized by H2O2 to the selenoxide (>Se=O) and the selenoxide is reduced by a thiol back to the selenide. In methanol, however, the GPx-like activity could not be explained by this simple scenario. To look into the reasons for the unusual behaviors in methanol, monoamino-substituted cyclic selenides with a variable ring size were synthesized, and the intermediates of the catalytic cycle were characterized by means of 77Se-NMR and LC–MS spectroscopies. In water, it was confirmed that the selenide and the selenoxide mainly contribute to the antioxidative function, though a slight contribution from the dihydroxy selenane (>Se(OH)2) was also suggested. In methanol, on the other hand, other active species, such as hydroxyselenonium (>Se+–OH) and hydroxy perhydroxy selenane (>Se(OH)(OOH)), could be generated to build another catalytic cycle. This over-oxidation would be more feasible for amino-substituted cyclic selenides, probably because the ammonium (NH3+) group would transfer a proton to the selenoxide moiety to produce a hydroxyselenonium species in the absence of an additional proton source. Thus, a shift of the major catalytic cycle in methanol would make the GPx-like antioxidative function of selenides perplexing.
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arai2017moleculesglutathione Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Kenta Arai, Ayako Tashiro, Yuui Osaka, Michio Iwaoka
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Journal Journal of ethnopharmacology
Year 2017
DOI
10.3390/molecules22030354
URL
http://www.mdpi.com/1420-3049/22/3/354
Keywords
antioxidant glutathione peroxidase selenoxideorganic chemistry

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