Glutathione-hemin complex as a cytochrome P-450 model characterization of the complex and its aromatic oxidation activities

A new cytochrome P-450 model that simulates the unusual spectral and substrate-oxidation properties of cytochrome P-450 is proposed. The complex, consisting of glutathione(GSH), hemin and pyridine(py), exhibits similar optical and EPR spectra to cytochrome P-450 in ferric low-spin state. On omission of py, a ferric high-spin state was produced. On exposure of the GSH-hemin-py complex to CO, a characteristic absorption band appeared at 450nm, like that typical of cytochrome P-450. Two types of spectral changes were observed when aminopyrine or phenobarbital (Type I) and aniline or quinoline (Type II) were added to the GSH-hemin complex. Hydroxylation, dealkylation and aromatic methyl migration activities were observed with the GSH-hemin complex.