Structural snapshots from the oxidative half-reaction of a copper amine oxidase: Implications for O2 activation

  • Bryan J. Johnson
  • , Erik T. Yukl
  • , Valerie J. Klema
  • , Judith P. Klinman
  • , Carrie M. Wilmot

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Background: Copper amine oxidases activate O2 either at the copper center or aminoquinol cofactor. Results: Catalytic intermediates from the oxidative half-reaction are structurally and spectroscopically characterized. Conclusion: The mechanism of O2 activation may depend on accessibility dictated by two conformers of the quinone cofactor. Significance: Structural changes that inform on catalytic mechanism have been revealed in the ubiquitous copper amine oxidases.

Original languageEnglish (US)
Pages (from-to)28409-28417
Number of pages9
JournalJournal of Biological Chemistry
Volume288
Issue number39
DOIs
StatePublished - Sep 27 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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