PURIFICATION AND CHARACTERIZATION OF A BENZENE HYDROXYLASE FROM RAT-LIVER MITOCHONDRIA

被引:4
作者
KARASZKIEWICZ, JW [1 ]
KALF, GF [1 ]
机构
[1] THOMAS JEFFERSON UNIV,JEFFERSON MED COLL,DEPT BIOCHEM & MOLEC BIOL,1020 LOCUST ST,PHILADELPHIA,PA 19107
关键词
(Rat liver); Benzene hydroxylase; Benzene metabolism; Mitochondrion; Phenol;
D O I
10.1016/0304-4165(90)90121-C
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 microchondrial origin is involved in benzene metabolism, and provide another example of a role for the mitochondrion in xenobiotic activation. © 1990.
引用
收藏
页码:223 / 229
页数:7
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