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Article

A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo.

Nature chemical biology - 1 Sept 2017

Mizrachi Dario, Robinson Michael-Paul, Ren Guoping, Ke Na, Berkmen Mehmet, DeLisa Matthew P

Abstract excerpt

Escherichia coli DsbB is a transmembrane enzyme that catalyzes the reoxidation of the periplasmic oxidase DsbA by ubiquinone. Here, we sought to convert membrane-bound DsbB into a water-soluble biocatalyst by leveraging a previously described method for in vivo solubilization of integral membrane proteins (IMPs). When solubilized DsbB variants were coexpressed with an export-defective copy of DsbA in the...

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Identifiers

PMID: 28628094
DOI: 10.1038/nchembio.2409
PMCID: PMC5562517

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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