Spectroscopy of Fe-S Cluster Proteins -- Information for Structure and Function

Fe-S 簇蛋白的光谱——结构和功能信息

• 批准号: 10523030
• 负责人: Stephen P. Cramer
• 金额: $ 49.27万
• 依托单位: SETI INSTITUTE
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2026-07-31
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/10523030
• 关键词: Address; Binding; Binding Proteins; Biochemistry; Biological Models; Biological Process; Biology; Catalysis; Chemistry; Communities; Complement; Consumption; Crystallization; DNA; Disease; Electron Transport; Elements; Environment; Enzymes; Exhibits; Exposure to; Ferredoxin; Future; Goals; Health; Hemoglobin; Home; Hydrogen; Hydrogenase; Image; In Situ; Infrared Rays; Interferometry; International; Investigation; Iron; Joints; Lasers; Learning; Length; Ligation; Lighting; Love; Malignant Neoplasms; Measurement; Measures; Metabolic Control; Metals; Methods; Microscopy; Modeling; Motion; Myoglobin; Nature; Nitrogenase; Nuclear; Organic solvent product; Organism; Oxidation-Reduction; Play; Process; Production; Property; Protein Dynamics; Proteins; Research; Resolution; Roentgen Rays; Role; Rubredoxins; Sampling; Societies; Source; Spectrum Analysis; Speed; Structure; System; Techniques; Technology; Temperature; Time; Transport Reaction; Vision; Work; X ray diffraction analysis; absorption; aqueous; biological systems; catalyst; cold temperature; cryostat; design; electronic structure; experimental study; extreme temperature; falls; flexibility; hyperthermophile; insight; instrumentation; nanoparticle; nanosecond; nickel-iron hydrogenase; novel; novel strategies; oxygen transport; photolysis; pressure; programs; protein function; protein structure; quantum; repaired; small molecule; stressor; synchrotron radiation; tool; vibration

GM65440 Renewal Resubmission Project Summary The element iron plays an enormous role in biology, including electron transport reactions (ferredoxins), oxygen transport and storage (hemoglobin and myoglobin), catalysis (nitrogenase, P-450, hydrogenase, and thousands of other enzymes), small molecule sensing (especially O2, CO, and NO), and DNA processing and repair. The health-relatedness of a better understanding of the structure and function of biological Fe is clear. The general theme of research in the Cramer lab involves the use spectroscopy as a tool for characterization of metals in biological systems. Much of this work involves the application of synchrotron radiation x-ray sources. Thanks to enormous improvements of these sources, experiments with exquisite sensitivity can now be conducted on dilute Fe samples. These include the technique Nuclear Resonance Vibrational Spectroscopy (NRVS), which is sensitive to the motion of 57Fe in a sample. Another new technique, nuclear-resonant time-domain interferometry (NR-TDI) can probe motion of all atoms in a sample. The x-ray experiments at international facilities are complemented by IR and Raman measurements at the home lab. The goals for the next 4 years can be divided into 3 main themes: · better understanding of the catalytic intermediates of the enzymes that process hydrogen – [NiFe] and [FeFe] hydrogenases, · information about structural changes that occur when Fe-S cluster proteins sense their environment, including mitoNEET and NAF-1, two health-related proteins which sense and communicate pH and redox status, and · characterization of protein dynamics in extremophiles (organisms that live at extremes of temperature, pressure, pH and other stressors) using the protein rubredoxin as a model system and using NRVS and NR-TDI to respectively measure the motion of Fe or the entire protein. The overall vision of this research program is to use spectroscopic methods to better understand how iron is used in important proteins, in ways that complement the information that can be gathered from diffraction and microscopy. In the course of research on specific topics, spectroscopic techniques such as NRVS will be further developed for the bioinorganic community. The novel NR-TDI technique will be assessed as a complementary probe of dynamical information about proteins.

GM65440 续展重新提交项目摘要 铁元素在生物学中发挥着巨大作用，包括电子传递反应 （铁氧还蛋白）、氧运输和储存（血红蛋白和肌红蛋白）、催化 （固氮酶、P-450、氢化酶和数千种其他酶）、小分子传感 （特别是 O2、CO 和 NO）以及 DNA 加工和修复。 对生物铁的结构和功能的了解更加清楚。 克莱默实验室的研究总体主题涉及使用光谱学作为工具 这项工作的大部分涉及生物系统中金属的表征。 由于这些源的巨大改进， 现在可以对这些稀铁样品进行高灵敏度的实验。 包括核磁共振振动光谱 (NRVS) 技术，该技术非常灵敏 另一种新技术，核共振时域技术。 干涉测量 (NR-TDI) 可以探测样品中所有原子的运动。 家庭实验室的红外和拉曼测量对国际设施进行了补充。 未来4年的目标可分为3个主题： · 更好地了解处理氢的酶的催化中间体 – [NiFe]和[FeFe]氢化酶， · 有关 Fe-S 簇蛋白感知其自身状态时发生的结构变化的信息 环境，包括 mitoNEET 和 NAF-1，这两种健康相关蛋白质可感知和 传达 pH 值和氧化还原状态，以及 · 极端微生物（生活在极端条件下的生物体）的蛋白质动力学特征 使用蛋白质红氧还蛋白作为模型 系统并使用 NRVS 和 NR-TDI 分别测量 Fe 或整个的运动 蛋白质。 该研究计划的总体愿景是利用光谱方法更好地 了解铁如何在重要蛋白质中以补充信息的方式使用 可以在特定研究过程中通过衍射和显微镜收集。 主题，光谱技术如 NRVS 将进一步开发用于生物无机物 新型 NR-TDI 技术将作为补充探针进行评估。 有关蛋白质的动态信息。