HEME PROTEIN STRUCTURE AND DYNAMICS

血红素蛋白结构和动力学

• 批准号: 3283462
• 负责人: THOMAS G. SPIRO
• 金额: $ 34.37万
• 依托单位: PRINCETON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1979
• 资助国家: 美国
• 起止时间: 1979-04-01 至 1994-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3283462
• 关键词: Raman spectrometry; chemical models; conformation; cytochrome oxidase; electron transport; hemoglobin; hemoprotein; hemoprotein structure; laser spectrometry; ligands; molecular rearrangement; oxygen; peroxidases; porphyrin structure; protein structure function; respiratory oxygenation; site directed mutagenesis; ultraviolet spectrometry

Studies of molecular structure and dynamics in heme proteins will be carried out using laser-excited resonance Raman spectroscopy. A theoretical and computational framework for extracting structural information from the spectra will be implemented using recently developed porphyrin force fields and molecular graphics. Protein-heme interactions in cytochrome c peroxidase will be investigated systematically with site- directed mutants. The dynamics of quaternary structure change in hemoglobin will be explored wit ultraviolet resonance Raman spectroscopy. Electron transfer and conformational coupling in cytochrome oxidase will be investigated with transient absorption and Raman techniques. These studies are expected to help uncover the molecular mechanisms whereby oxygen metabolism is linked to biological function through the motions of proteins.

对血红素蛋白的分子结构和动力学的研究将是 使用激光激发的共振拉曼光谱法进行。 一个 提取结构的理论和计算框架 光谱的信息将使用最近开发的 卟啉力场和分子图形。 蛋白质血红素相互作用 在细胞色素C中，将系统地研究过氧化物酶 定向突变体。 第四纪结构的动态变化 血红蛋白将被探索紫外线共振拉曼光谱法。 细胞色素氧化酶中的电子转移和构象耦合将 通过瞬时吸收和拉曼技术进行研究。 这些 预计研究将有助于发现分子机制 氧代谢与生物学功能通过 蛋白质。