DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA Oxidation

Kenji Inaba, Yohhei Takahashi, Koreaki Ito*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


DsbB is an Eacherichia 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 red-shift was observed stably for the DsbA(C33S)-DsbB complex as well as transiently by stopped flow rapid scanning spectroscopy during the reaction between wild-type DsbA and DsbB. Mutation and reconstitution experiments established that the unpaired Cys at position 44 of DsbB is primarily responsible for the chromogenic transition of ubiquinone, and this property correlates with the functional arrangement of amino acid residues in the neighborhood of Cys 44. We propose that the Cys44-induced anomaly in ubiquinone represents its activated state, which drives the DsbB-mediated electron transfer.

Original languageEnglish (US)
Pages (from-to)6761-6768
Number of pages8
JournalJournal of Biological Chemistry
Issue number8
StatePublished - Feb 20 2004

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


Dive into the research topics of 'DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA Oxidation'. Together they form a unique fingerprint.

Cite this