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Article

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.

The EMBO journal - 1 Mar 1999

Kobayashi T, Ito K

Abstract excerpt

Escherichia coli DsbB has four essential cysteine residues, among which Cys41 and Cys44 form a CXXC redox active site motif and the Cys104-Cys130 disulfide bond oxidizes the active site cysteines of DsbA, the disulfide bond formation factor in the periplasm. Functional respiratory chain is required for the cell to keep DsbA oxidized. In this study, we characterized the roles of essential cysteines of DsbB in the...

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Identifiers

PMID: 10064586
DOI: 10.1093/emboj/18.5.1192
PMCID: PMC1171210

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.PMID 10064586Read ↗

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