56 Scopus citations

Abstract

Methionine oxidation is known to alter functional properties of a transient A-type potassium channel expressed in Xenopus oocytes. We show here that nitric oxide (NO) slows down the K+ channel inactivation time course by oxidizing a critical methionine residue in the inactivation ball domain of the channel protein. We also demonstrate that the channel protein is protected from methionine oxidation by the enzyme methionine sulfoxide reductase and the antioxidant vitamin C. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)48-52
Number of pages5
JournalFEBS Letters
Volume442
Issue number1
DOIs
StatePublished - Jan 8 1999

Keywords

  • A-type potassium channel
  • Antioxidant
  • Methionine oxidation
  • Nitric oxide
  • Xenopus oocyte

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