Purification and characterization of a benzene hydroxylase from rat liver mitochondria

• Published in: Biochimica et biophysica acta Vol. 1035; no. 2; pp. 223 - 229
• Main Authors: Karaszkiewicz, James W., Kalf, George F.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 17.08.1990
• Subjects: Animals; Benzene - metabolism; Benzene hydroxylase; Chromatography; Chromatography, Affinity; Chromatography, Gel; Chromatography, High Pressure Liquid; Durapatite; Electrophoresis, Polyacrylamide Gel; Hydroxyapatites; Indicators and Reagents; Kinetics; Mitochondria, Liver - enzymology; Mitochondrion; Mixed Function Oxygenases - isolation & purification; Mixed Function Oxygenases - metabolism; Molecular Weight; Phenol; Rat liver; Rats; Substrate Specificity; Mitochondrion; Benzene hydroxylase; Benzene metabolism; p.s.i; Phenol; SKF-525A; DTE; Rat liver; mtDNA; Hepes; HPLC
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(90)90121-C

An enzyme has been purified to electrophoretic homogeneity from rat liver mitoplasts which metabolizes benzene to phenol. The enzyme has a M r of 52 000 and requires NADPH, adrendoxin, and adrenodoxin reductase for activity, Benzene hydroxylase activity could be inhibited by carbon monoxide and SKF-525A, and by specific inhibitors of microsomal benzene metabolism. The purified enzyme also oxidized phenol to catechol. The data suggest that a cytochrome P-450 of microchondrial origin is involved in benzene metabolism, and provide another example of a role for the mitochondrion in xenobiotic activation.