ESR studies on the radical cation mechanism of the ring opening of cyclopropylamines
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.
- Research Organization:
- Univ. of Tennessee, Knoxville
- OSTI ID:
- 6970253
- Journal Information:
- J. Am. Chem. Soc.; (United States), Journal Name: J. Am. Chem. Soc.; (United States) Vol. 109:2; ISSN JACSA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
400201* -- Chemical & Physicochemical Properties
AMINES
CATIONS
CHARGED PARTICLES
CHEMICAL REACTIONS
DATA
ELECTRON SPIN RESONANCE
EXPERIMENTAL DATA
INFORMATION
IONS
MAGNETIC RESONANCE
NUMERICAL DATA
ORGANIC COMPOUNDS
RADICALS
RESONANCE
TEMPERATURE DEPENDENCE