J. Wouters et al., EXPERIMENTAL AND THEORETICAL-STUDY OF REVERSIBLE MONOAMINE-OXIDASE INHIBITORS - STRUCTURAL APPROACH OF THE ACTIVE-SITE OF THE ENZYME, Journal of neural transmission. Supplementum, (41), 1994, pp. 313-319
Experimental and theoretical physico-chemical methods were used to inv
estigate the interaction between aryl-oxazolidinones and monoamine oxi
dase (MAO). Several arguments suggest that these compounds interact wi
th the flavin adenine dinucleotide (FAD) cofactor of MAO. The calculat
ion using ab initio molecular orbital methods of the electronic proper
ties of flavin and befloxatone, a reversible inhibitor of MAO A, led t
o a description of the interaction between aryl-oxazolidinones and the
cofactor of the enzyme. Structure activity relationship results revea
led additional sites of interaction with the protein core of MAO A. As
a result of this work, a model is proposed for the reversible inhibit
ion of MAO by oxazolidinones via long distance, reversible interaction
s with the FAD cofactor of the enzyme.