来自假单胞菌属菌株NCIB 9816的萘双加氧酶组分铁氧化还原蛋白NAP的纯化及性质
Purification and properties of ferredoxinNAP, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816.
作者信息
Haigler B E, Gibson D T
机构信息
Center for Applied Microbiology, University of Texas, Austin 78712.
出版信息
J Bacteriol. 1990 Jan;172(1):465-8. doi: 10.1128/jb.172.1.465-468.1990.
Abstract
One of the three components of the naphthalene dioxygenase occurring in induced cells of Pseudomonas sp. strain NCIB 9816 has been purified to homogeneity. The protein contained 2 g-atoms each of iron and acid-labile sulfur and had an apparent molecular weight of 13,600. The evidence indicates that it is a ferredoxin-type protein that functions as an intermediate electron transfer protein in naphthalene dioxygenase activity.
摘要
在假单胞菌属菌株NCIB 9816的诱导细胞中出现的萘双加氧酶的三个组分之一已被纯化至同质。该蛋白质含有2克原子的铁和酸不稳定硫，表观分子量为13,600。证据表明它是一种铁氧化还原蛋白型蛋白质，在萘双加氧酶活性中作为中间电子传递蛋白发挥作用。
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