HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF RESPIRATORY PROTEINS FROM T THERMOP

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 研究中心，而研究中心不一定是研究者所在的机构。 两种蛋白质，Rieske铁硫和细胞色素ba 3，从嗜热真细菌，嗜热栖热菌，参与呼吸，建议在高分辨率和多个氧化态和pH值水平进行研究。 氧化的Rieske蛋白在pH 8.5下溶解，产生部分质子化形式的结构，这使我们深入了解H+易位的机制。 然而，pH 8.5时的超高分辨率（< 1）结构、低pH和高分辨率时的还原态质子化结构对于定义机械特征也至关重要。 新的ba 3结构的氰基复合物和还原，羰基化的形式，在高分辨率，应该产生额外的信息，关于这种蛋白质的功能。

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.