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Nonenzymatic reduction of brucine N‐oxide by the heme group of cytochrome P450
Author(s) -
Takekawa Koji,
Sugihara Kazumi,
Kitamura Shigeyuki,
Tatsumi Kiyoshi
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203421
Subject(s) - brucine , chemistry , cytochrome b5 , heme , microsome , cytochrome , hemeprotein , methemoglobin , stereochemistry , biochemistry , hemoglobin , enzyme , strychnine
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.