Participation of low molecular weight electron carriers in oxidative protein folding

Research output: Contribution to journalReview article

5 Citations (Scopus)


Oxidative protein folding is mediated by a proteinaceous electron relay system, in which the concerted action of protein disulfide isomerase and Ero1 delivers the electrons from thiol groups to the final acceptor. Oxygen appears to be the final oxidant in aerobic living organisms, although the existence of alternative electron acceptors, e.g. fumarate or nitrate, cannot be excluded. Whilst the protein components of the system are well-known, less attention has been turned to the role of low molecular weight electron carriers in the process. The function of ascorbate, tocopherol and vitamin K has been raised recently. In vitro and in vivo evidence suggests that these redox-active compounds can contribute to the functioning of oxidative folding. This review focuses on the participation of small molecular weight redox compounds in oxidative protein folding.

Original languageEnglish
Pages (from-to)1346-1359
Number of pages14
JournalInternational journal of molecular sciences
Issue number3
Publication statusPublished - Mar 2009


  • Ascorbate
  • Endoplasmic reticulum
  • Ero1
  • Glutathione
  • Oxidative folding
  • Protein disulfide isomerase
  • Small-molecule catalysts
  • Tocopherol
  • Vitamin k

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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