RAMAN AND TIME-RESOLVED RAMAN STUDIES OF HEME PROTEINS

血红素蛋白的拉曼和时间分辨拉曼研究

• 批准号: 2139508
• 负责人: James Robert Kincaid
• 金额: $ 13.96万
• 依托单位: MARQUETTE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1984
• 资助国家: 美国
• 起止时间: 1984-07-01 至 1995-09-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2139508
• 关键词: RAMAN; TIME; RESOLVED; STUDIES; HEME

Heme proteins are involved in a large number of physiologically important processes, including: delivery of oxygen to the tissues; derivation of stored energy from oxidation of nutrients; protective destruction of potentially dangerous peroxides and activation and elimination of toxic pollutants and carcinogens. Despite this remarkable functional diversity, all of these species employ the heme group as the active com- ponent. Identification of the factors responsible for this varied function would be of obvious benefit for attaining an understanding of the behavior in normal and abnormal states. The long term objective of this research program is the elucidation of the molecular mechanisms by which these various proteins interact with the common heme group to effectively regulate its reactivity. In order to clarify the molecular basis of functional behavior, a number of powerful spectroscopic techniques are employed to probe key interactions between the heme and the protein-and to determine the effect of subtle structural perturbations on the electronic structure and reactivity of the active sites and other key sites within-the protein. The principal spectroscopic methods to be employed during this phase of the work are resonance Raman and time-resolved resonance Raman (in both the visible and ultraviolet regions) which exploit novel rapid-mixing devices to yield structural information for short-lived intermediates. This approach applied to native and systematically modified proteins represents a realistic attempt to elucidate the important molecular control mechanisms responsible for such remarkable functional diversity.

血红素蛋白质参与了大量的生理上重要的 过程，包括：向组织输送氧气; 从营养物质的氧化储存能量;保护性破坏 具有潜在危险的过氧化物以及有毒物质的活化和消除 污染物和致癌物。 尽管这一显著的功能性 多样性，所有这些物种都采用血红素基团作为活性化合物， 成分。 确定造成这种情况的因素各不相同 功能将有明显的好处，以达到理解 正常和异常状态下的行为。 这项研究计划的长期目标是阐明 这些不同的蛋白质相互作用的分子机制 常见的血红素基团，以有效地调节其反应性。 为了 为了阐明功能行为的分子基础， 强大的光谱技术被用来探测关键的相互作用 血红素和蛋白质之间的联系， 电子结构和反应性的结构扰动 蛋白质内的活性位点和其他关键位点。 校长 在这一阶段的工作中采用的光谱方法是 共振拉曼和时间分辨共振拉曼（在可见光和可见光中 和紫外线区域），其利用新颖的快速混合装置， 产生短寿命中间体的结构信息。 这种方法适用于天然和系统修饰的蛋白质 代表了一个现实的尝试，以阐明重要的分子 控制机制负责这种显着的功能多样性。