ArticleRSC advances2024
Can selenenyl sulfides be a substrate of glutathione reductase enzyme? A theoretical insight.
Article in RSC advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Glutathione reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) to glutathione. As selenium is a congener of sulfur, the possibility of reducing selenenyl sulfide (RSeSG) at the catalytic site of GR has been investigated using density functional theory. Calculations on the redox potential and the Se-S bond strength of some studied RSeSG compounds with a phenyl selenide backbone suggested that the unsubstituted and amine-based selenenyl sulfide intermediates could have a promising tendency to be reduced at the catalytic site of GR.
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