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On the reactivity and ionization of the active site cysteine residues of Escherichia coli thioredoxin.

Biochemistry - 25 Jun 1996

Takahashi N, Creighton T E

Abstract excerpt

Within various proteins of the thioredoxin family, the stability of the disulfide bond formed reversibly between the two active site cysteine residues, one accessible and one buried, varies widely and is directly correlated with the pKa value of the accessible cysteine thiol group. If applicable to thioredoxin, its stable disulfide bond would imply that its accessible thiol group should have a high pKa value,...

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PMID: 8679592
DOI: 10.1021/bi960465v

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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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