Complex formation with the activator RACo affects the corrinoid structure of CoFeSP.
Complex formation with the activator RACo affects the corrinoid structure of CoFeSP.
复制标题
与活化剂 RACo 形成复合物会影响 CoFeSP 的类咕啉结构
DOI：
10.1021/bi300795n
复制
发表时间：
2012
期刊：
影响因子：
2.9
通讯作者：
Hildebrandt
中科院分区：
文献类型：
--
作者：
Meister;Hennig;Jeoung;Lendzian;Dobbek;Hildebrandt
参与还原性CO2转化的corrinoid [Fe-S]蛋白（CoFeSP）的激活需要通过[Fe-S]蛋白RACo还原Co（II）中心，根据两种蛋白的还原电位，这将对应于上坡电子转移。在我们的共振拉曼光谱工作中，我们证明，作为一个构象门的corrinoid减少，复杂的形成Co（II）FeSP和RACo具体改变的corrinoid辅因子的结构，通过修改的Co（II）中心与轴向配体的相互作用。在各种缺失突变体的基础上，可以预测伴侣蛋白上潜在的相互作用结构域。
Activation of the corrinoid [Fe-S] protein (CoFeSP), involved in reductive CO2conversion, requires the reduction of the Co(II) center by the [Fe-S] protein RACo, which according to the reduction potentials of the two proteins would correspond to an uphill electron transfer. In our resonance Raman spectroscopic work, we demonstrate that, as a conformational gate for the corrinoid reduction, complex formation of Co(II)FeSP and RACo specifically alters the structure of the corrinoid cofactor by modifying the interactions of the Co(II) center with the axial ligand. On the basis of various deletion mutants, the potential interaction domains on the partner proteins can be predicted.