A stable tyrosyl radical in monoamine oxidase A

S E J Rigby, R M G Hynson, R R Ramsay, A W Munro, N S Scrutton

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46 Citations (Scopus)

Abstract

We present spectroscopic evidence consistent with the presence of a stable tyrosyl radical in partially reduced human monoamine oxidase (MAO) A. The radical forms following single electron donation to MAO A and exists in equilibrium with the FAD flavosemiquinone. Oxidative formation of the tyrosyl radical in MAO is not reliant on neighboring metal centers and uniquely requires reduction of the active site flavin to facilitate oxidation of a tyrosyl side chain. The identified tyrosyl radical provides the key missing link in support of the single electron transfer mechanism for amine oxidation by MAO enzymes.

Original languageEnglish
Pages (from-to)4627-4631
Number of pages5
JournalJournal of Biological Chemistry
Volume280
Issue number6
DOIs
Publication statusPublished - 11 Feb 2005

Keywords

  • ELECTRON-SPIN-RESONANCE
  • BENZYLAMINE ANALOGS
  • FLAVIN SEMIQUINONE
  • INHIBITORS ALTER
  • REDOX PROPERTIES
  • HUMAN LIVER
  • OXIDATION
  • MECHANISM
  • CATALYSIS
  • AMINE

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