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Abstract
Longitudinal relaxation ( T 1) measurements for all lines (N(CH 3) 2, N(CH 3), (C(CH 3), phenyl) in the aminopyrine 1H-NMR spectrum were used to study the interaction of aminopyrine with purified microsomal cytochrome P-450 from livers of phenobarbital-treated rats. The paramagnetic contribution to the observed t 1 −1 values was determined from its dependence on aminopyrine concentration. The Solomon-Bloembergen equation was used to calculate between Fe 3+ and aminopyrine distances in the enzyme-substrate complex. For all protons these distances are about 8 Å.
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