Premium
Tyrosyl Radical Formation and Propagation in Flavin Dependent Monoamine Oxidases
Author(s) -
Dunn Rachel V.,
Munro Andrew W.,
Turner Nicholas J.,
Rigby Stephen E. J.,
Scrutton Nigel S.
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000184
Subject(s) - flavin group , monoamine oxidase , cofactor , radical , chemistry , monoamine neurotransmitter , enzyme , labelling , biochemistry , monoamine oxidase a , stereochemistry , serotonin , receptor
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.