Electronic Structures of ET Active Sites and their Contributions to Reactivity

斯坦福大学化学系爱德华·I·所罗门教授的研究得到了化学系的支持，他使用各种光谱方法结合电子结构计算来获得对铜和铁的硫电子转移(ET)蛋白质的新见解。这项研究的目的是确定几何和电子结构对生物系统中远程快速ET的贡献，以及蛋白质在激活金属位点功能中的作用。正在研究的活性中心在催化N_2、N_2O和二氧化碳的还原、生物技术、温室气体的环境调节以及医疗和健康应用方面都是重要的，包括铁和铜的代谢和相关的疾病状态。了解生物系统中的快速ET以及蛋白质在激活金属功能部位中的作用将提供对生物技术和环境调控中重要的活性部位的基本见解。此外，这项研究还适用于铁和铜的代谢以及相关的疾病状态。这项工作中开发的光谱方法将适用于生物和催化中各种重要的金属位置。参与这项研究的博士后助理、研究生和本科生在前沿无机化学课程中接受了一系列光谱方法、量子化学、无机化学和酶学方面的出色培训。

Professor Edward I. Solomon of the Chemistry Department at Stanford University is supported by the Division of Chemistry for his research that employs a variety of spectroscopic methods combined with electronic structure calculations to obtain new insights into copper and iron sulfur electron transfer (ET) proteins. This research is aimed at defining geometric and electronic structure contributions to long range rapid ET in biological systems and the role of the protein in activating the metal site for function. The active sites being studied are important in the catalysis of N2, N2O, and CO2 reduction, in biotechnology, in environmental regulation of green house gases, and in medical and health applications, including Fe and Cu metabolism and related disease states. Understanding rapid ET in biological systems as well as the role of the protein in activating the metal site for function will provide fundamental insights into active sites that are important in biotechnology and environmental regulation. Additionally, the research has applicability to iron and copper metabolism and related disease states. The spectroscopic methodologies developed in this work will apply to a variety of important classes of metal sites in biology and catalysis. Postdoctoral associates, graduate students and undergraduates involved in this research receive excellent training in a range of spectroscopic methods, quantum chemistry, inorganic chemistry and enzymology in a forefront inorganic chemistry program.