METAL-PROTEINS STUDIES BY FLUORESCENCE SPECTROSCOPY AND HALIDE ION NMR

通过荧光光谱和卤化物离子核磁共振研究金属蛋白质

• 批准号: 3937063
• 负责人: JOSEPH J PESEK
• 金额: --
• 依托单位: SAN JOSE STATE UNIVERSITY
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3937063
• 关键词: aminoacid; analytical method; chemical binding; drug design /synthesis /production; enzyme structure; fluorescence spectrometry; halocarbon compound; heavy metals; metal poisoning; metalloproteins; nuclear magnetic resonance spectroscopy

The study of metal ions in biochemical systems encompasses two significant aspects of enzyme reactions. First, the metalloenzymes and metal activated enzymes that require the presence of the metal in order for the enzyme to carry out its function and second, the enzyme systems which are disrupted or inhibited by the presence of certain metal ions (primarily the heavy metals). This study proposes to use the native fluorescence of the amino in enzymes to gather information about these two aspects of enzyme reactions. This means that no external probe will have to be added which may perturb the enzyme or disrupt the effect of the metal. The other method used in this study is halide ion NMR. This technique can be used to detect binding of the metal ion and to determine the accessibility to and local motion at the binding site. If successful, the techniques developed in this study will help to design new drugs for the treatment of heavy metal poisoning and would provide fundamental information about the role of the metal ion in metalloenzymes and metal activated biochemical systems.

生化系统中金属离子的研究包括两个 酶反应的重要方面。 首先， 金属酶和金属激活的酶，需要 金属的存在以使酶执行其 功能，其次，被破坏或 某些金属离子的存在抑制（主要是 重金属）。 这项研究建议使用天然荧光 酶中的氨基以收集有关这两个的信息 酶反应的各个方面。 这意味着没有外部探测 将必须添加可能会扰动酶或破坏 金属的效果。 这项研究中使用的另一种方法是 卤离子NMR。 该技术可用于检测结合 金属离子并确定对本地的可访问性 在结合位点运动。 如果成功，这些技术 在这项研究中开发的将有助于设计新药 治疗重金属中毒并将提供 有关金属离子在 金属酶和金属活化的生化系统。