Baur J R, Graves M C, Feinberg B A, Ragsdale S W
Department of Chemistry, University of Wisconsin-Milwaukee.
Biofactors. 1990 Jul;2(3):197-203.
Ferredoxins (Fds) constitute an important class of nonheme iron-sulfur proteins. One of the most studied Fds is the [8Fe-8S] Fd from Clostridium pasteurianum. The gene for this Fd has previously been cloned and sequenced. We report the expression of this Fd in Escherichia coli, and the characterization and comparison of this recombinant protein to the native Fd. We have found that the purified recombinant protein has the same enzymatic, redox, magnetic and electronic properties as the native Fd isolated from C. pasteurianum, which indicates that the two [4Fe-4S] clusters present in the Fd were correctly formed in E. coli.
铁氧化还原蛋白(Fds)构成了一类重要的非血红素铁硫蛋白。研究最多的铁氧化还原蛋白之一是来自巴斯德梭菌的[8Fe-8S]铁氧化还原蛋白。该铁氧化还原蛋白的基因此前已被克隆和测序。我们报道了这种铁氧化还原蛋白在大肠杆菌中的表达,以及该重组蛋白与天然铁氧化还原蛋白的特性表征和比较。我们发现,纯化后的重组蛋白具有与从巴斯德梭菌中分离出的天然铁氧化还原蛋白相同的酶学、氧化还原、磁性和电学性质,这表明铁氧化还原蛋白中存在的两个[4Fe-4S]簇在大肠杆菌中正确形成。