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Article

Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.

Antioxidants & redox signaling - 1 Jan 2000

Takahashi Yoh-Hei, Inaba Kenji, Ito Koreaki

Abstract excerpt

DsbB, an Escherichia coli plasma membrane protein, oxidizes DsbA, the protein dithiol oxidant in the periplasm, in conjunction with respiratory quinone molecules. While its two periplasmic regions, in particular the essential Cys41-Cys44 and the Cys104-Cys130 cysteine pairs, have been characterized in considerable detail, little or no information is available about the functional importance of its three...

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Identifiers

PMID: 16771666
DOI: 10.1089/ars.2006.8.743

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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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Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.PMID 16771666Read ↗

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

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

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

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

Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade.Semantic proximity Read ↗

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

DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.Semantic proximity Read ↗

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Reactivities of quinone-free DsbB from Escherichia coli.Semantic proximity Read ↗

Mechanism of the electron transfer catalyst DsbB from Escherichia coli.Semantic proximity Read ↗

Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB.Semantic proximity Read ↗

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