Premium
Catalytic Amine Oxidation under Ambient Aerobic Conditions: Mimicry of Monoamine Oxidase B
Author(s) -
Murray Alexander T.,
Dowley Myles J. H.,
PradauxCaggiano Fabienne,
Baldansuren Amgalanbaatar,
Fielding Alistair J.,
Tuna Floriana,
Hendon Christopher H.,
Walsh Aron,
LloydJones Guy C.,
John Matthew P.,
Carbery David R.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201503654
Subject(s) - monoamine oxidase , flavin group , chemistry , catalysis , amine gas treating , biogenic amine , amine oxidase , serotonin , monoamine oxidase b , monoamine neurotransmitter , monoamine oxidase a , electron paramagnetic resonance , oxidase test , biochemistry , enzyme , combinatorial chemistry , organic chemistry , physics , receptor , nuclear magnetic resonance
The flavoenzyme monoamine oxidase (MAO) regulates mammalian behavioral patterns by modulating neurotransmitters such as adrenaline and serotonin. The mechanistic basis which underpins this enzyme is far from agreed upon. Reported herein is that the combination of a synthetic flavin and alloxan generates a catalyst system which facilitates biomimetic amine oxidation. Mechanistic and electron paramagnetic (EPR) spectroscopic data supports the conclusion that the reaction proceeds through a radical manifold. This data provides the first example of a biorelevant synthetic model for monoamine oxidase B activity.