While several studies have investigated the rich redox chemistry of the cysteine/cystine couple, the electrochemistry of selenocysteine/selenocystine analogues is relatively unexplored, and direct voltammetric measurements of diselenide-containing proteins are yet to be reported. Interestingly, studies on synthetic selenoproteins indicate that thioredoxin, the predominant reductant present in the cell, is only capable of partially reducing diselenide bonds. These findings raise question as to whether some alternate reducing agent is employed to cleave the Se-Se bond naturally. We seek to decipher the mechanism of diselenide reduction, both electrochemically and in vivo, in order to understand the biological role of these rare and stable moieties. The influence of salt concentration and pH on the voltammetric profile of diselenides will be presented, and plausible physiological reduction pathways proposed.

Electrochemical characterization of naturally-occurring diselenide bonds

243rd National Meeting (2012)

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