Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

The active-site cysteines of DsbA, the periplasmic disulfide-bond-forming enzyme of Escherichia coli, are kept oxidized by the cytoplasmic membrane protein DsbB. DsbB, in turn, is oxidized by two kinds of quinones (ubiquinone for aerobic and menaquinone for anaerobic growth) in the electron-transpor...

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Bibliographic Details
Main Authors: Kadokura, Hiroshi, Bader, Martin, Tian, Hongping, Bardwell, James C. A., Beckwith, Jon
Format: Artigo
Language:Inglês
Published: The National Academy of Sciences 2000
Subjects:
Biological Sciences
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC27118/
https://ncbi.nlm.nih.gov/pubmed/11005861
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