Ascorbate-mediated electron transfer in protein thiol oxidation in the endoplasmic reticulum

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Addition of, or gulonolactone oxidase-dependent in situ generation of, ascorbate provoked the oxidation of protein thiols, which was accompanied by ascorbate consumption in liver microsomal vesicles. The maximal rate of protein thiol oxidation was similar upon gulonolactone, ascorbate or dehydroascorbate addition. Cytochrome P450 inhibitors (econazole, proadifen, quercetin) decreased ascorbate consumption and the gulonolactone or ascorbate-stimulated thiol oxidation. The results demonstrate that the ascorbate/dehydroascorbate redox couple plays an important role in electron transfer from protein thiols to oxygen in the hepatic endoplasmic reticulum, even in gulonolactone oxidase deficient species.

Original languageEnglish
Pages (from-to)539-543
Number of pages5
JournalFEBS letters
Issue number3
Publication statusPublished - Nov 5 1999



  • Ascorbate
  • Dehydroascorbate
  • Endoplasmic reticulum
  • Gulonolactone oxidase
  • Hydrogen peroxide
  • Protein thiol

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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