Mechanism of the electron transfer catalyst DsbB from Escherichia coli.

doi:10.1093/emboj/cdg356

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Article

Mechanism of the electron transfer catalyst DsbB from Escherichia coli.

The EMBO journal - 15 Jul 2003

Grauschopf Ulla, Fritz Andrea, Glockshuber Rudi

Abstract excerpt

The membrane protein DsbB from Escherichia coli is essential for disulfide bond formation and catalyses the oxidation of the periplasmic dithiol oxidase DsbA by ubiquinone. DsbB contains two catalytic disulfide bonds, Cys41-Cys44 and Cys104-Cys130. We show that DsbB directly oxidizes one molar equivalent of DsbA in the absence of ubiquinone via disulfide exchange with the 104-130 disulfide bond, with a rate...

Topics

Bacterial Proteins
Catalysis
Cysteine
Disulfides
Electron Transport
Escherichia coli
Genetic Variation
Kinetics
Membrane Proteins
Protein Disulfide-Isomerases
Thermodynamics

Source

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Identifiers

PMID: 12853466
DOI: 10.1093/emboj/cdg356
PMCID: PMC165626

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