Iushmanov V E, Gol'dfel'd M G, Kol'tover V K, Mikoian V D
Mol Biol (Mosk). 1984 Mar-Apr;18(2):421-6.
Mn2+-ion is linked to isolated chloroplast coupling factor CF-1 via the ATP bridge in the catalytically competent ternary complex as deduced from water proton relaxation rate measurements. Two essential SH-groups in CF-1 protein were modified with nitroxyl mercuric derivative as spin label. The substrate complex Ca2+-ATP is shown to induce the structural transition near the active site to the state with a stronger immobilized spin label. The distances between the paramagnetic metal ions and nitroxyl bound to the protein SH-group were evaluated as being in the range of 5-8,5 A for Cu2+ and 14-22 A for Mn2+.
根据水质子弛豫速率测量结果推断，在具有催化活性的三元复合物中，锰离子（Mn2+）通过ATP桥与分离的叶绿体偶联因子CF-1相连。CF-1蛋白中的两个必需巯基用硝酰汞衍生物作为自旋标记进行了修饰。底物复合物Ca2+-ATP被证明可诱导活性位点附近的结构转变，形成自旋标记固定更强的状态。与蛋白质巯基结合的顺磁性金属离子和硝酰之间的距离经评估，铜离子（Cu2+）为5-8.5埃，锰离子（Mn2+）为14-22埃。
