Shumyantseva V V, Bykhovskaya E A, Kolyada L N, Archakov A I
Institute of Biomedical Chemistry, Moscow, Russia.
Biochem Biophys Res Commun. 1994 Apr 29;200(2):722-5. doi: 10.1006/bbrc.1994.1510.
To create a semi-artificial monomolecular oxygenase system, FAD or FMN were covalently bound to cytochrome P450 2B4 as electron donor centers and bleomycin to NADPH-cytochrome P450 reductase as a generator of active oxygen species. The most catalytically active was the conjugate of cytochrome P450 with FMN, able to initiate the reactions of dimethylaniline and aminopyrine demethylation along with the reaction of aniline p-hydroxylation. The conjugate of cytochrome P450 with FAD oxidized these substrates at a much slower rate. The bleomycin-reductase complex was capable of demethylating dimethylaniline and aminopyrine but failed to oxidize aniline.
为创建一个半人工单分子加氧酶系统，将黄素腺嘌呤二核苷酸（FAD）或黄素单核苷酸（FMN）作为电子供体中心共价连接到细胞色素P450 2B4上，并将博来霉素连接到NADPH-细胞色素P450还原酶上作为活性氧物种的产生剂。细胞色素P450与FMN的共轭物催化活性最高，能够引发二甲基苯胺和氨基比林的去甲基化反应以及苯胺对羟基化反应。细胞色素P450与FAD的共轭物氧化这些底物的速度要慢得多。博来霉素-还原酶复合物能够使二甲基苯胺和氨基比林去甲基化，但不能氧化苯胺。
