Models for cytochrome P-450 under physiological condition.
- 1 January 1976
- journal article
- letter
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 24 (7) , 1686-1688
- https://doi.org/10.1248/cpb.24.1686
Abstract
Optical properties of models for the ligation in cytochrome P-450 system were investigated by interaction of hemin with biologically significant thiol compounds such as cysteine and cysteine methyl ester, in the presence of such bases as pyridine, imidazol and histidine under physiological condition. Cysteine binds to Fe3+ porphyrin to form axial S-Fe-N coordination in the presence of a base, and Fe3+ porphyrin is easily reduced to Fe2+ porphyrin by an excess thiol. Under exposure of CO of these systems, the characteristic absorption band at 450 nm was observed, which is typical with cytochrome P-450.cntdot.CO complex. The model used nicely represents the reaction involved in the vicinity of heme moiety of cytochrome P-450 under physiological condition.This publication has 0 references indexed in Scilit: