Communication

Tyrosyl Radical Formation and Propagation in Flavin Dependent Monoamine Oxidases

  1. Rachel V. Dunn Dr.1,
  2. Andrew W. Munro Prof.1,
  3. Nicholas J. Turner Prof.2,
  4. Stephen E. J. Rigby Dr.1,
  5. Nigel S. Scrutton Prof.1

Article first published online: 17 MAY 2010

DOI: 10.1002/cbic.201000184

Issue

ChemBioChem

ChemBioChem

Volume 11, Issue 9, pages 1228–1231, June 14, 2010

Additional Information

How to Cite

Dunn, R. V., Munro, A. W., Turner, N. J., Rigby, S. E. J. and Scrutton, N. S. (2010), Tyrosyl Radical Formation and Propagation in Flavin Dependent Monoamine Oxidases. ChemBioChem, 11: 1228–1231. doi: 10.1002/cbic.201000184

Author Information

  1. 1

    Faculty of Life Sciences, Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, M1 7DN Manchester (UK), Fax: (+44) 161-306-8918

  2. 2

    School of Chemistry, University of Manchester, 131 Princess Street, M1 7DN Manchester (UK)

Publication History

  1. Issue published online: 7 JUN 2010
  2. Article first published online: 17 MAY 2010
  3. Manuscript Received: 22 MAR 2010

Funded by

  • UK Biotechnology and Biological Sciences Research Council

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Keywords:

  • ENDOR spectroscopy;
  • enzyme catalysis;
  • ESR spectroscopy;
  • radicals;
  • reaction mechanisms
Thumbnail image of graphical abstract

MAO enzymes: Demonstration of the presence of tyrosyl radicals in partially reduced monoamine oxidases (MAO) was achieved by a combination of specific isotopic labelling and pulsed ENDOR techniques. Comparative studies between human MAO A and MAO N indicate that the equilibrium distribution of the radical species is not localised to the active site residues near the flavin cofactor.

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