Selenium is a trace element in the human body, found primarily in the form of selenocysteine and selenomethionine. Selenium-containing proteins, such as glutathione peroxidases and thioredoxin reductases, are known to play an integral role in several physiologically regulated processes. Interestingly, evidence of a diselenide bond, resulting from the oxidation of two selenocysteine residues, has not yet been found in mammalian systems and reports on synthetic selenoproteins indicate that thioredoxin, the predominant cellular reductant, cannot fully reduce the oxidized product. We seek to better understand the biological significance and potential applications of selenium’s intrinsic redox activity. Our efforts thus far have focused on the electrochemical behavior of selenocystine under physiological conditions with parallel analysis performed on the well-studied sulfur analogue, cystine. <br/>

Exploring the physiological role of selenium redox chemistry

249th National Meeting (2015)

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