Corpus ID: 1865672

Cytochrome P-450 difference spectra: effect of chemical structure on type II spectra in mouse hepatic microsomes.

  title={Cytochrome P-450 difference spectra: effect of chemical structure on type II spectra in mouse hepatic microsomes.},
  author={R. Mailman and A. Kulkarni and R. Baker and E. Hodgson},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  volume={2 3},
A comprehensive study of the relationship between chemical structure and binding was made with mouse hepatic microsomes. The generally reported type II spectrum (peak 424-435 nm, trough 390-410 nm) is correlated with the presence of a nitrogen atom in which sp 2 or sp 3 nonbonded electrons are "sterically accessible." Structural series showed that as substituents are placed closer to this nitrogen, spectral size is either reduced or eliminated. Other nucleophilic atoms with relatively free… Expand
The relationship between the binding of 2-n-alkylbenzimidazoles to rat hepatic microsomal cytochrome P-450 and the inhibition of monooxygenation.
From their inhibition properties it seems that even the short chain (C1-C4) substituted benzimidazoles also bind toi the Type I site and thus compete for the substrate binding site of cytochrome P-450. Expand
Iopronic acid interaction with hepatic microsomal cytochrome P-450: relationship between chemical structure and binding.
Summary The interaction of the cholecystographic agent Iopronic acid with cytochrome P-450 from rat liver microsomes has been examined in the light of the hydrophobic properties and of theExpand
Visible Spectra of Type II Cytochrome P450-Drug Complexes: Evidence that “Incomplete” Heme Coordination Is Common
The visible spectrum of a ligand-bound cytochrome P450 is often used to determine the nature of the interaction between the ligand and the P450. One particularly characteristic form of spectra arisesExpand
Some properties of an inhibitory cytochrome P-450 metabolic-intermediate complex existing in a spin-state equilibrium.
The aberrant functional properties of the metabolic adduct appear to reflect complex molecular organization of this compound, as is evidenced by the unique position of the Soret region absorption maximum at 407 nm, which hints at the presence of a mixture of high- and low-spin forms. Expand
Steric factors in the inhibitory interaction of imidazoles with microsomal enzymes.
It appears that both binding and inhibition depend on the accessibility of the non-bonded electrons on the nitrogen atom at position — 3 of the ring. Expand
Hepatic microsomes from freshwater fish--I. In vitro cytochrome P-450 chemical interactions.
  • D. L. Fabacher
  • Biology, Medicine
  • Comparative biochemistry and physiology. C: Comparative pharmacology
  • 1982
Spectral data suggest that hepatic microsomal cytochrome P-450 of freshwater fish exists in different forms, since the spectral size of chemical interactions as related to the carbon monoxide spectrum and the ratio of type II to type I binding were not alike. Expand
An unusual effect of N-octylamine on the cytochrome b5 spectrum of insect and mammalian microsomes.
Microsomes from rat and mouse liver, but not those from housefly abdomens, exhibit similar unusual spectral interactions with n-octylamine when supplemented with the soluble factor from the hornworm. Expand
Spectral characterization of microsomal cytochrome P-450 from the midgut of the tobacco hornworm, Manduca sexta J.
The study of type II optical difference spectra using several ligands revealed that the basic requirements for this perturbation are the same as in other animal species, namely, a sterically accessible sp2 or sp3 nitrogen atom. Expand
The occurrence of multiple forms of cytochrome P-450 in hepatic microsomes from untreated rats and mice.
The data indicate that liver microsomes from untreated rats and mice contain more than one cytochrome P-450 and that of these cytochromes may be located in different parts of the endoplasmic reticulum. Expand
Effects of induction on the metabolism and cytochrome P-450 binding of harman and other beta-carbolines.
The metabolism of harman by liver microsomes from non-induced, phenobarbitone (PB)-induced and 3-methylcholanthrene (MC)-induced mice was investigated and the major metabolite formed with each microsomal preparation was identified as 6-hydroxyharman. Expand