Studies into the quantitative structure act! Vlty relationships of rate s
of I-methyl-4-phenyl-l,2,3,6-tetrahydropyridine oxidation
catalyzed by monoamine oxidases A and B were performed to
elucidate active site substrate conformation and oxidation
mechanisms. Plotting experimental kinetic activity against molecular
properties obtained by experiment and by computational chemistry
methods demonstrated correlations with lipophilic, steric, and
electronic factors. Compounds studied were 4-aryloxy analogs, 4-
aromatic heterocycle analogs, and 4-phenyl analogs. The conformer
with phenyl ring to tetrahydropyridine dihedral angles similar to a
low energy conformer of I-methyl-4-(2'-methyl-phenyl)-1,2,3,6-
tetrahydropyridine is the most active conformer. Results indicate
that rate limiting single electron transfer mechanisms are more
viable than hydrogen atom abstraction mechanisms. Results indicate
that binding or dissociation is the rate limiting step for aryloxy-analog
oxidation catalyzed by monoamine oxidase B whereas the
catalytic event itself is the rate limiting step for the other analogs.
Several equations were developed to describe quantitative structure
activity relationships of oxidation rates.
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