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Article

Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductase.

Biochemistry - 4 Feb 2014

Lothrop Adam P, Snider Gregg W, Ruggles Erik L, Patel Amar S, Lees Watson J, Hondal Robert J

Abstract excerpt

Mammalian thioredoxin reductase (TR) is a pyridine nucleotide disulfide oxidoreductase that uses the rare amino acid selenocysteine (Sec) in place of the more commonly used amino acid cysteine (Cys) in the redox-active tetrapeptide Gly-Cys-Sec-Gly motif to catalyze thiol/disulfide exchange reactions. Sec can accelerate the rate of these exchange reactions (i) by being a better nucleophile than Cys, (ii) by being...

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Identifiers

PMID: 24422500
DOI: 10.1021/bi400658g
PMCID: PMC3957198

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Source receipt: pubmed, retrieved 7 Sept 2026.

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