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Article

Purification, crystallization and preliminary crystallographic data for rat cytosolic selenocysteine 498 to cysteine mutant thioredoxin reductase.

Acta crystallographica. Section D, Biological crystallography - 1 Sept 2000

Zhong L, Persson K, Sandalova T, Schneider G, Holmgren A

Abstract excerpt

Mammalian cytosolic thioredoxin reductase is a homodimer of 55 kDa subunit containing an essential penultimate selenocysteine residue. An active analogue of the rat enzyme in which cysteine replaces selenocysteine has been expressed in Escherichia coli cells at high levels and purified to homogeneity. The pure enzyme contains one FAD per subunit and shows spectral properties identical to that of the wild-type...

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Identifiers

PMID: 10957643
DOI: 10.1107/s0907444900009458

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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