Bertini I, Luchinat C, Piccioli M, Oliver M V, Viezzoli M S
Department of Chemistry, University of Florence, Italy.
Eur Biophys J. 1991;20(5):269-79. doi: 10.1007/BF00450562.
Human copper-cobalt superoxide dismutase in the reduced form has been investigated through 1H NMR techniques. The aim is to monitor the structural properties of this derivative and to compare them with those of reduced and oxidized native superoxide dismutases. The observed signals of the cobalt ligands have been assigned as well as the signals of the histidines bound to copper(I). The latter signals experience little pseudocontact shifts which allow a rough orientation of the magnetic susceptibility tensor in the molecular frame. The connectivities indicate that, although the histidine bridge is broken in the reduced form, the interproton distances between ligands of both ions are essentially the same.
已通过1H NMR技术对还原态的人铜钴超氧化物歧化酶进行了研究。目的是监测该衍生物的结构特性，并将其与还原态和氧化态的天然超氧化物歧化酶的结构特性进行比较。已确定了钴配体的观测信号以及与铜（I）结合的组氨酸的信号。后者的信号几乎没有赝接触位移，这使得可以在分子框架中粗略确定磁化率张量的方向。连接性表明，尽管组氨酸桥在还原态下断裂，但两种离子配体之间的质子间距离基本相同。
