HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF RESPIRATORY PROTEINS FROM T THERMOP

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 嗜热真细菌中与呼吸有关的两种蛋白质Rieske Fe-S和细胞色素Ba3被建议在高分辨率、多种氧化状态和pH水平下进行研究。氧化后的Rieske蛋白在pH 8.5下被溶解，得到部分质子化形式的结构，这为H移位的机制提供了深入的认识。然而，在pH 8.5时的超高分辨率(&lt；1？)结构、低pH值和高分辨率下的还原状态质子化结构对于定义机械特征也是至关重要的。在高分辨率下，氰基复合体和还原的碳化形式的新颖的Ba3结构应该会产生关于这种蛋白质功能的额外信息。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Two proteins, Rieske iron-sulfur and cytochrome ba3, from the thermophilic eubacterium, Thermus thermophilus, involved in respiration are proposed to be studied at high resolution and in multiple oxidation states and pH levels. The oxidized Rieske protein has been solved at pH 8.5 yielding the structure of the partially protonated form, which gives insight into the mechanism of H+ translocation. However, the ultra-high resolution (< 1 ¿) structure at pH 8.5, the low pH and reduced state protonated structures at high resolution are also vital to define mechanistic features. Novel ba3 structures of the cyano complex and the reduced, carbonylated form, at high resolution, should yield additional information regarding this protein's function.