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Article

Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli.

Biochemistry - 27 May 1997

Hennecke J, Sillen A, Huber-Wunderlich M, Engelborghs Y, Glockshuber R

Abstract excerpt

The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and required for efficient disulfide bond formation in the bacterial periplasm. The enzyme consists of a thioredoxin-like domain and a second, alpha-helical domain which is inserted into the thioredoxin motif. Reduction of th...

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Identifiers

PMID: 9174355
DOI: 10.1021/bi963017w

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-9174355-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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