Purification and characterization of a benzene hydroxylase from rat liver mitochondria.
An enzyme has been purified to electrophoretic homogeneity from rat liver mitoplasts which metabolizes benzene to phenol. The enzyme has a Mr 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 mitochondrial origin is involved in benzene metabolism, and provide another example of a role for the mitochondrion in xenobiotic activation.
Karaszkiewicz
J W
JW
Department of Biochemistry and Molecular Biology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, PA 19107.
Kalf
G F
GF
D000818:Animals; D001554:Benzene / Q000378:metabolism; D002845:Chromatography; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D007202:Indicators and Reagents; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D051381:Rats; D013379:Substrate Specificity
D006882:Hydroxyapatites; D007202:Indicators and Reagents; D017886:Durapatite; D006899:Mixed Function Oxygenases; C019765:benzene 1,2-dioxygenase; D001554:Benzene