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Article

Identification of a segment of DsbB essential for its respiration-coupled oxidation.

Molecular microbiology - 1 Jan 2001

Kobayashi T, Takahashi Y, Ito K

Abstract excerpt

In the Escherichia coli protein disulphide bond formation pathway, membrane-bound DsbB oxidizes periplasmic DsbA, the disulphide bond-introducing enzyme. The Cys-41-Val-Leu-Cys-44 motif in the first periplasmic domain of DsbB is kept strongly oxidized by the respiratory function of the cell. We now show that the characteristic dithiothreitol resistance of the Cys-41-Cys-44 bond was retained even when the flanked...

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Source

Identifiers

PMID: 11123697
DOI: 10.1046/j.1365-2958.2001.02229.x

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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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Identification of a segment of DsbB essential for its respiration-coupled oxidation.PMID 11123697Read ↗

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Mutational analysis of the disulfide catalysts DsbA and DsbB.Semantic proximity Read ↗

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