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.

血红素蛋白的分子结构和动力学研究将是 使用激光激发共振拉曼光谱进行。 一 提取结构的理论和计算框架 光谱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过氧化物酶将系统地研究与网站- 定向突变体 分子四级结构变化的动力学 血红蛋白将用紫外共振拉曼光谱进行研究。 细胞色素氧化酶中的电子转移和构象偶联 可以用瞬态吸收和拉曼技术来研究。 这些 这些研究有望帮助揭示 氧代谢通过运动与生物功能联系在一起， proteins.