RECONSTITUTION OF CYTOCHROME P4502B4 (LM2) ACTIVITY WITH CAMPHOR AND LINALOOL MONOOXYGENASE ELECTRON-DONORS

被引：19

作者：

BERNHARDT, R ^{[1
]}

GUNSALUS, IC ^{[1
]}

机构：

[1] UNIV ILLINOIS, DEPT BIOCHEM, URBANA, IL 61801 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 187卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)81494-9

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 P4502B4 (LM2) monooxygenase was shown to bind the P450cam and P450lin redoxins with respective dissociation constants of ca. 500 and 100 μM. When the redoxin reductases are added, the heterogeneous complexes demethylate benzphetamine with HCHO yields and Vmax similar to results with the homologous microsomal reductase. Implications of evolutionary conserved P450 redox electron donor binding site residues are discussed. © 1992 Academic Press, Inc.

引用

页码：310 / 317

页数：8

共 31 条

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