A model system of cytochrome P-450: Hydroxylation of aniline by iron- or hemin-thiol compound systems.
- 1 January 1979
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 27 (9) , 2171-2176
- https://doi.org/10.1248/cpb.27.2171
Abstract
Hydroxylation of aniline by several Fe(II)-thiol and hemin-thiol complexes was studied as a model system for drug metabolism by cytochrome P-450 in liver microsomes. Cysteine, cysteine methylester, cysteamine, N-acetyl-cysteine, .alpha.-mercaptopropionic acid, .beta.-mercaptopropionic acid, thiosalicylic acid and o-aminobenzenethiol were tested as thiolcompounds. In these systems, p- and o-aminophenol were the major products and m-aminophenol was not detected. The hydroxylation was affected by reaction time, pH, the type of thiol compound and the concentrations of thiol compound, aniline, Fe(II) and hemin. The aniline-hyroxylating activity of the hemin-thiol system was 6-20 times that of the Fe(II)-thiol system at pH 4. The Fe(II)-thiol and hemin-thiol systems may be useful chemical models for studies of the structure and function of cytochrome P-450.This publication has 1 reference indexed in Scilit:
- Polarity in aromatic hydroxylation by hemin-thiol model systems for cytochrome P-450Biochemical Pharmacology, 1976