Protein disulfide bond formation in prokaryotes

Hiroshi Kadokura, Federico Katzen, Jon Beckwith

Research output: Contribution to journalReview articlepeer-review

450 Citations (Scopus)


Disulfide bonds formed between pairs of cysteines are important features of the structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia coli to promote the formation of these covalent bonds and to ensure that the correct pairs of cysteines are joined in the final folded protein. These transfers of electrons consist, in the main, of cascades of disulfide bond formation or reduction steps between a series of proteins (DsbA, DsbB, DsbC, and DsbD). A surprising variety of mechanisms and protein structures are involved in carrying out these steps.

Original languageEnglish
Pages (from-to)111-135
Number of pages25
JournalAnnual Review of Biochemistry
Publication statusPublished - 2003


  • Electron transfer
  • Escherichia coli
  • Periplasm
  • Protein folding
  • Thioredoxin


Dive into the research topics of 'Protein disulfide bond formation in prokaryotes'. Together they form a unique fingerprint.

Cite this