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Article

Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.

The Journal of biological chemistry - 22 Aug 2008

Jönsson Thomas J, Tsang Allen W, Lowther W Todd, Furdui Cristina M

Abstract excerpt

The reversible oxidation of the active site cysteine in typical 2-Cys peroxiredoxins (Prx) to sulfinic acid during oxidative stress plays an important role in peroxide-mediated cell signaling. The catalytic retroreduction of Prx-SO(2)(-) by sulfiredoxin (Srx) has been proposed to proceed through two novel reaction intermediates, a sulfinic phosphoryl ester and protein-based thiosulfinate. Two scenarios for the...

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Identifiers

PMID: 18593714
DOI: 10.1074/jbc.C800124200
PMCID: PMC2517003

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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