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Article

An atypical catalytic mechanism involving three cysteines of thioredoxin.

The Journal of biological chemistry - 22 Aug 2008

Koh Cha San, Navrot Nicolas, Didierjean Claude, Rouhier Nicolas, Hirasawa Masakazu, Knaff David B, Wingsle Gunnar, Samian Razip, Jacquot Jean-Pierre, Corbier Catherine, Gelhaye Eric

Abstract excerpt

Unlike other thioredoxins h characterized so far, a poplar thioredoxin of the h type, PtTrxh4, is reduced by glutathione and glutaredoxin (Grx) but not NADPH:thioredoxin reductase (NTR). PtTrxh4 contains three cysteines: one localized in an N-terminal extension (Cys(4)) and two (Cys(58) and Cys(61)) in the classical thioredoxin active site ((57)WCGPC(61)). The property of a mutant in which Cys(58) was replaced by...

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PMID: 18552403
DOI: 10.1074/jbc.M802093200

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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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