Title : Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence.

Pub. Date : 2000 May 23

PMID : 10801974






1 Functional Relationships(s)
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1 In the oxidized enzyme, we demonstrated two nonflavin redox centers by chemical modification and peptide sequencing: one was a disulfide within the sequence -Cys(59)-Val-Asn-Val-Gly-Cys(64), identical to the active site of GR; the other was a selenenylsulfide formed from Cys(497)-SeCys(498) and confirmed by mass spectrometry. Disulfides glutathione-disulfide reductase Homo sapiens