Regio- and stereochemical studies on the .alpha.-carbon oxidation of (S)-nicotine by cytochrome P-450 model systems

Abstract
Results from previous studies indicate that rabbit liver microsomal cytochrome P-450 catalyzes the C-5'' two-electron oxidation of (S)-nicotine stereoselectivity with preferential loss of the pro-(E)-hydrogen atom trans to the pyridine ring. We now have examined the regio- and stereochemical features of the oxidation of (S)-nicotine by peroxides in the presence of various hemoproteins and by electrochemical and photochemical methods. None of these systems gave rise to the stereochemicl outcomes observed with the cytochrome P-450 mediated reaction. The results of these studies are interpreted as additional evidence for the formation of a highly ordered complex between (S)-nicotine and cytochrome P-450 that directs the regio- and diasterioselective .alpha.-carbon oxidation of this substrate.

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