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Biochim Biophys Acta. 2004 Nov 11;1694(1-3):111-9.

Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.

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Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830, North University Dr., Ann Arbor, MI 48109-1048, USA.


Disulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cysteine pairs is achieved by the transfer of disulfides from the highly oxidizing DsbA/DsbB catalytic machinery to substrate proteins. The oxidizing power utilized by this system comes from the membrane-embedded electron transport system, which utilizes molecular oxygen as a final oxidant. Proofreading of disulfide bond formation is performed by the DsbC/DsbD system, which has the ability to rearrange non-native disulfides to their native configuration. These disulfide isomerization reactions are sustained by a constant supply of reducing power provided by the cytoplasmic thioredoxin system, utilizing NADPH as the ultimate electron source.

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