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Article

DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.

The Journal of biological chemistry - 20 Feb 2004

Inaba Kenji, Takahashi Yoh-hei, Fujieda Nobutaka, Kano Kenji, Miyoshi Hideto, Ito Koreaki

Abstract excerpt

DsbB is an Escherichia coli plasma membrane protein that reoxidizes the Cys30-Pro-His-Cys33 active site of DsbA, the primary dithiol oxidant in the periplasm. Here we describe a novel activity of DsbB to induce an electronic transition of the bound ubiquinone molecule. This transition was characterized by a striking emergence of an absorbance peak at 500 nm giving rise to a visible pink color. The ubiquinone...

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PMID: 14634016
DOI: 10.1074/jbc.M310765200

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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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DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.PMID 14634016Read ↗

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