Tyrosyl Radical Formation and Propagation in Flavin Dependent Monoamine Oxidases

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 r...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2010-06, Vol.11 (9), p.1228-1231
Main Authors: Dunn, Rachel V, Munro, Andrew W, Turner, Nicholas J, Rigby, Stephen E.J, Scrutton, Nigel S
Format: Article
Language:English
Subjects:
Catalytic Domain
Electron Spin Resonance Spectroscopy
ENDOR spectroscopy
enzyme catalysis
ESR spectroscopy
Flavins - metabolism
Humans
Monoamine Oxidase - chemistry
Monoamine Oxidase - metabolism
Protein Isoforms - chemistry
Protein Isoforms - metabolism
radicals
reaction mechanisms
Tyrosine - analogs & derivatives
Tyrosine - metabolism
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Summary: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.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201000184