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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