Abstract
Cyclopropylamine radical cations have been implicated in the mechanism of inactivation of monoamine oxidase and cytochrome P-450 by cyclopropylamines. The key step in the proposed mechanism is illustrated for the parent compound in Scheme I and consists of the ring opening of the aminium radical cation 1 to the carbon-centered radical 2 which subsequently attacks the active site of the enzyme. Here they present ESR evidence for this ring-opening reaction and report that 2 is not converted to the nitrogen-centered radical 3 whereas the corresponding reaction for the neutral radical proceeds to completion at similar temperatures. These results provide a firm basis for the radical cation mechanism of enzyme inactivation, in keeping with the structural evidence that the inactivator is bound to the enzyme through carbon rather than nitrogen.
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