Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions

Yang Yu, Arnab Mukherjee, Mark J. Nilges, Parisa Hosseinzadeh, Kyle D. Miner, Yi Lu

Research output: Contribution to journalArticle

Abstract

Tyrosine is a conserved redox-active amino acid that plays important roles in heme-copper oxidases (HCO). Despite the widely proposed mechanism that involves a tyrosyl radical, its direct observation under O2 reduction conditions remains elusive. Using a functional oxidase model in myoglobin called F33Y-CuBMb that contains an engineered tyrosine, we report herein direct observation of a tyrosyl radical during both reactions of H 2O2 with oxidized protein and O2 with reduced protein by electron paramagnetic resonance spectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.

Original languageEnglish (US)
Pages (from-to)1174-1177
Number of pages4
JournalJournal of the American Chemical Society
Volume136
Issue number4
DOIs
StatePublished - Jan 29 2014

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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