A SYSTEMATIC STUDY OF REORGANIZATION ENERGY

重组能源的系统研究

• 批准号: 6997536
• 负责人: AMANDA L ECKERMANN
• 金额: $ 4.83万
• 依托单位: NORTHWESTERN UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2005
• 资助国家: 美国
• 起止时间: 2005-07-22 至 2006-07-21
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6997536
• 关键词: acidity /alkalinity; avidin; binding sites; bioenergetics; biotin; chemical kinetics; computer simulation; electrochemistry; electrolytes; electron transport; macromolecule; metal complex; metalloproteins; oxidation reduction reaction; postdoctoral investigator; ruthenium; solvents; spectrometry; temperature; thermodynamics

DESCRIPTION (provided by applicant): The goal of this project is to study outer-sphere reorganization energy of a redox center by systematically changing the environment using proteins. These environmental variations cause detectable changes in the electrochemical response which can be correlated to changes in the reorganization energy. The metal complex-protein interaction will be studied by varying the proximity of the metal complex to the protein by changing the length of the linking group between the binding ligand and the metal center. Further, the effects of solvent, pH and electrolyte will be investigated. Finally, well-known proteins with a specific variety of binding sites will be used to determine what role the binding site dimensions play. The metal complexes will be characterized by standard spectroscopic techniques prior to protein binding. Examination of the electrochemical properties following binding will yield the reorganization energy. The interactions will also be simulated using computerized modeling programs. There are clear connections of this methodology to the study of the fundamental energetics of small molecules binding to macromolecules, pertinent to such areas as drug discovery and molecular recognition.

描述（由申请人提供）：该项目的目标是通过使用蛋白质系统地改变环境来研究氧化还原中心的外层重组能。这些环境变化导致电化学响应发生可检测的变化，这可以与重组能的变化相关。将通过改变结合配体和金属中心之间的连接基团的长度来改变金属络合物与蛋白质的接近度来研究金属络合物-蛋白质相互作用。此外，还将研究溶剂、pH 值和电解质的影响。最后，具有特定多种结合位点的众所周知的蛋白质将用于确定结合位点尺寸所起的作用。在蛋白质结合之前，金属络合物将通过标准光谱技术进行表征。结合后电化学性质的检查将产生重组能。还将使用计算机建模程序来模拟交互作用。这种方法与小分子与大分子结合的基本能量学研究有明显的联系，涉及药物发现和分子识别等领域。