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Article

Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis.

Biochemistry - 4 Feb 2014

Lothrop Adam P, Snider Gregg W, Flemer Stevenson, Ruggles Erik L, Davidson Ronald S, Lamb Audrey L, Hondal Robert J

Abstract excerpt

Mammalian thioredoxin reductase (TR) is a pyridine disulfide oxidoreductase that uses the rare amino acid selenocysteine (Sec) in place of the more commonly used amino acid cysteine (Cys). Selenium is a Janus-faced element because it is both highly nucleophilic and highly electrophilic. Cys ortho...

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Identifiers

PMID: 24490974
DOI: 10.1021/bi4007258
PMCID: PMC3931472

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24490974-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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