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Article

DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.

The Journal of biological chemistry - 21 Jul 1995

Kishigami S, Kanaya E, Kikuchi M, Ito K

Abstract excerpt

Formation of disulfide bonds in Escherichia coli envelope proteins is facilitated by the Dsb system, which is thought to consist of at least two components, a periplasmic soluble enzyme (DsbA) and a membrane-bound factor (DsbB). Although it is believed that DsbA directly oxidizes substrate cysteines and DsbB reoxidizes DsbA to allow multiple rounds of reactions, direct evidence for the DsbA-DsbB interaction has...

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PMID: 7615498
DOI: 10.1074/jbc.270.29.17072

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.PMID 7615498Read ↗

Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli.Semantic proximity Read ↗

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

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

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Semantic proximity Read ↗

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Semantic proximity Read ↗

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Semantic proximity Read ↗

Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.Semantic proximity Read ↗

Identification of a segment of DsbB essential for its respiration-coupled oxidation.Semantic proximity Read ↗

Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.Semantic proximity Read ↗

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Semantic proximity Read ↗

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.Semantic proximity Read ↗

An in vivo pathway for disulfide bond isomerization in Escherichia coli.Semantic proximity Read ↗

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