Studies on the cytochrome P-450 product complexes formed during the metabolism of N,N-dimethylaniline.
Biochim Biophys Acta
; 544(1): 185-99, 1978 Nov 15.
Article
em En
| MEDLINE
| ID: mdl-718995
ABSTRACT
The oxidative metabolism of N,N-dimethylaniline by partially solubilized cytochrome P-450 from rabbit liver was found to be associated with the formation of a 424- and 448-nm product adduct of the hemoprotein. From the effects of temperature, hydrogen ion concentration, n-octylamine, extraction of the enzyme preparations with organic solvents and pretreatment of the animals with inducers of drug metabolism on both the formation of the spectral species and the enzymic C- and N-oxidation of N,N-dimethylaniline it is concluded that the 424-nm spectral change is generated from an intermediate in the C-oxidation reaction, whereas formation of the 448-nm spectral perturbation is the result of binding to cytochrome P-450 of a metabolite arising from N-oxidation of the arylamine; N-dealkylation of the parent amine is not a obligatory intermediary step in 448-nm complex formation. The 448-nm ferrohemochrome is supposed to be formed through coordination of the N-oxidized intermediate via the oxygen atom. This type of interaction appears to require considerably stronger thermal activation as compared with the 424-nm complex. The 448-nm product adduct of cytochrome P-450 is unstable in the ferric state or in the presence of sodium dithionite.
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Base de dados:
MEDLINE
Assunto principal:
Microssomos Hepáticos
/
Sistema Enzimático do Citocromo P-450
/
Compostos de Anilina
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1978
Tipo de documento:
Article