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Title: Metabolism of benzene and phenol by a reconstituted purified phenobarbital induced rat liver mixed function oxidase system

Abstract

Cytochrome P-450 and the electron-donor, NADPH-cytochrome c reductase were isolated from phenobarbital induced rat liver microsomes. Both benzene and its primary metabolite phenol, were substrates for the reconstituted purified phenobarbital induced rat liver mixed function oxidase system. Benzene was metabolized to phenol and the polyhydroxylated metabolites; catechol, hydroquinone and 1,2,4 benzenetriol. Benzene elicited a Type I spectral change upon its interaction with the cytochrome P-450 while phenol's interaction with the cytochrome P-450 produced a reverse Type I spectra. The formation of phenol showed a pH optimum of 7.0 compared with 6.6-6.8 for the production of the polyhyrdoxylated metabolites. Cytochrome P-450 inhibitors, such as metyrapone and SKF 525A, diminished the production of phenol from benzene but not the production of the polyhydroxylated metabolites from phenol. The radical trapping agents, DMSO, KTBA and mannitol, decreased the recovery of polyhydroxylated metabolites, from /sup 14/C-labeled benzene and/or phenol. As KTBA and DMSO interacted with OH. There was a concomitant release of ethylene and methane, which was measured. Desferrioxamine, an iron-chelator and catalase also depressed the recovery of polyhydroxylated metabolites. In summary, benzene and phenol were both substrates for this reconstituted purified enzyme system, but they differed in binding to cytochrome P-450, pH optima andmore » mode of hydroxylation.« less

Authors:
Publication Date:
Research Org.:
Rutgers--the State Univ., New Brunswick, NJ (USA)
OSTI Identifier:
6619142
Alternate Identifier(s):
OSTI ID: 6619142
Resource Type:
Thesis/Dissertation
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BENZENE; METABOLISM; MIXED-FUNCTION OXIDASES; CHEMICAL ACTIVATION; PHENOL; CARBON 14 COMPOUNDS; CYTOCHROMES; LIVER; MICROSOMES; PHENOBARBITAL; ANESTHETICS; ANTICONVULSANTS; AROMATICS; AZINES; BARBITURATES; BODY; CELL CONSTITUENTS; CENTRAL NERVOUS SYSTEM DEPRESSANTS; DIGESTIVE SYSTEM; DRUGS; ENZYMES; GLANDS; HETEROCYCLIC COMPOUNDS; HYDROCARBONS; HYDROXY COMPOUNDS; HYPNOTICS AND SEDATIVES; LABELLED COMPOUNDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANIC OXYGEN COMPOUNDS; ORGANOIDS; ORGANS; OXIDOREDUCTASES; OXYGENASES; PHENOLS; PIGMENTS; PROTEINS; PYRIMIDINES 550201* -- Biochemistry-- Tracer Techniques

Citation Formats

Griffiths, J.C.. Metabolism of benzene and phenol by a reconstituted purified phenobarbital induced rat liver mixed function oxidase system. United States: N. p., 1986. Web.
Griffiths, J.C.. Metabolism of benzene and phenol by a reconstituted purified phenobarbital induced rat liver mixed function oxidase system. United States.
Griffiths, J.C.. Wed . "Metabolism of benzene and phenol by a reconstituted purified phenobarbital induced rat liver mixed function oxidase system". United States. doi:.
@article{osti_6619142,
title = {Metabolism of benzene and phenol by a reconstituted purified phenobarbital induced rat liver mixed function oxidase system},
author = {Griffiths, J.C.},
abstractNote = {Cytochrome P-450 and the electron-donor, NADPH-cytochrome c reductase were isolated from phenobarbital induced rat liver microsomes. Both benzene and its primary metabolite phenol, were substrates for the reconstituted purified phenobarbital induced rat liver mixed function oxidase system. Benzene was metabolized to phenol and the polyhydroxylated metabolites; catechol, hydroquinone and 1,2,4 benzenetriol. Benzene elicited a Type I spectral change upon its interaction with the cytochrome P-450 while phenol's interaction with the cytochrome P-450 produced a reverse Type I spectra. The formation of phenol showed a pH optimum of 7.0 compared with 6.6-6.8 for the production of the polyhyrdoxylated metabolites. Cytochrome P-450 inhibitors, such as metyrapone and SKF 525A, diminished the production of phenol from benzene but not the production of the polyhydroxylated metabolites from phenol. The radical trapping agents, DMSO, KTBA and mannitol, decreased the recovery of polyhydroxylated metabolites, from /sup 14/C-labeled benzene and/or phenol. As KTBA and DMSO interacted with OH. There was a concomitant release of ethylene and methane, which was measured. Desferrioxamine, an iron-chelator and catalase also depressed the recovery of polyhydroxylated metabolites. In summary, benzene and phenol were both substrates for this reconstituted purified enzyme system, but they differed in binding to cytochrome P-450, pH optima and mode of hydroxylation.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Wed Jan 01 00:00:00 EST 1986},
month = {Wed Jan 01 00:00:00 EST 1986}
}

Thesis/Dissertation:
Other availability
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