Takekawa K, Sugihara K, Kitamura S, Tatsumi K
Institute of Pharmaceutical Science, Hiroshima University School of Medicine, Japan.
Biochem Mol Biol Int. 1997 Aug;42(5):977-81. doi: 10.1080/15216549700203421.
Evidence showing that cytochrome P450-mediated reduction of brucine N-oxide to brucine by rat liver microsomes proceeds nonenzymatically in the presence of both a reduced pyridine nucleotide and FAD is presented. The microsomal N-oxide reduction appears to proceed in two steps: The first step is reduction of FAD by NADPH or NADH either enzymatically or nonenzymatically. The second step is nonenzymatic reduction of the tertiary amine N-oxide by the reduced flavin and is nonenzymatically catalyzed by the heme group of cytochrome P450.