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

Richard Mailman, A. P. Kulkarni, R. C. Baker, E. Hodgson

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

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 sp2 or sp3 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 steric access may also cause a modified type II binding, i.e. a bathochromic shift. Data are also presented to show that minor structural changes affect both size and type of spectrum. (Journal received: November 1975)

Original languageEnglish (US)
Pages (from-to)301-308
Number of pages8
JournalDrug Metabolism and Disposition
Volume2
Issue number3
StatePublished - Dec 1 1974

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Microsomes
Cytochrome P-450 Enzyme System
Nitrogen
Liver
Electrons

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmaceutical Science

Cite this

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Cytochrome P 450 difference spectra. Effect of chemical structure on type II spectra in mouse hepatic microsomes. / Mailman, Richard; Kulkarni, A. P.; Baker, R. C.; Hodgson, E.

In: Drug Metabolism and Disposition, Vol. 2, No. 3, 01.12.1974, p. 301-308.

Research output: Contribution to journalArticle

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