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Article

Reactivities of quinone-free DsbB from Escherichia coli.

The Journal of biological chemistry - 23 Sept 2005

Inaba Kenji, Takahashi Yoh-Hei, Ito Koreaki

Abstract excerpt

DsbB is a disulfide oxidoreductase present in the Escherichia coli plasma membrane. Its cysteine pairs, Cys41-Cys44 and Cys104-Cys130, facing the periplasm, as well as the bound quinone molecules play crucial roles in oxidizing DsbA, the protein dithiol oxidant in the periplasm. In this study, we characterized quinone-free forms of DsbB prepared from mutant cells unable to synthesize ubiquinone and menaquinone....

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PMID: 16027117
DOI: 10.1074/jbc.M506189200

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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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