OBLIGATORY REQUIREMENT OF CYTOCHROME-B-5 IN THE PARA-NITROANISOLE O-DEMETHYLATION REACTION CATALYZED BY CYTOCHROME-P-450 WITH A HIGH-AFFINITY FOR CYTOCHROME-B-5

被引：63
作者：
SUGIYAMA, T
MIKI, N
YAMANO, T
机构：
[1] Department of Biochemistry, Osaka University Medical School Nakanoshima, Kita-ku, Osaka, Osaka
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 90卷 / 03期
关键词：
D O I：
10.1016/0006-291X(79)91886-2
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：
The role of cytochrome b5 in the p-nitroanisole O-demethylation was studied with a reconstituted system containing a unique cytochrome P-450, isolated from rabbit liver microsomes as a species with a high affinity for cytochrome b5. The maximal activity was obtained in the complete system consisting of cytochrome P-450, NADPH-cytochrome P-450 reductase, NADH-cytochrome b5 reductase, and Triton X-100 in addition to cytochrome b5. The omission of cytochrome b5 from the complete system entirely abolished the activity. These results clearly show that cytochrome b5 is obligatory in the reconstitute p-nitroanisole O-demethylation system, and this cytochrome P-450 probably interacts with cytochrome b5 in such a way that the second electron is transferred from cytochrome b5 and thus exhibits the demethylase activity. © 1979.
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页码：715 / 720
页数：6
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