HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF RESPIRATORY PROTEINS FROM T THERMOP

T THERMOP 呼吸蛋白的高分辨率晶体学研究

• 批准号: 7597921
• 负责人: JAMES A FEE
• 金额: $ 0.14万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7597921
• 关键词: Complex; Computer Retrieval of Information on Scientific Projects Database; Eubacterium; Funding; Grant; Institution; Proteins; Research; Research Personnel; Resolution; Resources; Respiration; Rieske iron-sulfur protein; Source; Structure; Thermus thermophilus; United States National Institutes of Health; cytochrome ba3; insight; novel; oxidation; protein function; respiratory protein; ultra high resolution

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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 提议以高分辨率、多种氧化态和 pH 水平对来自嗜热真细菌（嗜热栖热菌）的两种参与呼吸的蛋白质 Rieske 铁硫和细胞色素 ba3 进行研究。 氧化的 Rieske 蛋白已在 pH 8.5 下溶解，产生部分质子化形式的结构，从而深入了解 H+ 易位的机制。 然而，pH 8.5 时的超高分辨率 (< 1 ¿) 结构、低 pH 值和高分辨率的还原态质子化结构对于定义机械特征也至关重要。 氰基络合物的新颖 ba3 结构和还原的羰基化形式在高分辨率下应该会产生有关该蛋白质功能的更多信息。