Abstract
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.
Highlights
Reported 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
Summary
Monoamine oxidase (MAO) is a mitochondrial flavindependent oxidoreductase enzyme which oxidizes a range of important amines to imines, for example, the neurotransmitters serotonin, histamine, and noradrenaline.[1]. Two mechanistic postulates have been developed to account for the requisite increase in acidity of the relevant a-amino CÀH bond: the formation of a covalent flavin–amine conjugate,[7] and the formation of an aminium radical cation[8] after single-electron transfer from amine to flavin.
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