恶臭假单胞菌苯双加氧酶系统中铁硫蛋白的特性
Properties of the iron--sulphur proteins of the benzene dioxygenase system from Pseudomonas putida.
作者信息
Crutcher S E, Geary P J
出版信息
Biochem J. 1979 Feb 1;177(2):393-400. doi: 10.1042/bj1770393.
Abstract
A purification procedure was developed to stabilize the iron-sulphur proteins of the benzene dioxygenase system from Pseudomonas putida. The intermediate electron-carrying protein has a mol. wt. of 12300 and possesses one (2Fe--2S) cluster, whereas the terminal dioxygenase has a mol.wt. of 215300 and possesses two (2Fe--2S) clusters. The order and stoicheiometry of electron transfer and of the whole system are described.
摘要
已开发出一种纯化程序，以稳定来自恶臭假单胞菌的苯双加氧酶系统的铁硫蛋白。中间电子传递蛋白的分子量为12300，含有一个（2Fe-2S）簇，而末端双加氧酶的分子量为215300，含有两个（2Fe-2S）簇。描述了电子转移以及整个系统的顺序和化学计量。
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