Electronic Structures of ET Active Sites and their Contributions to Reactivity

斯坦福大学化学系的Edward I. Solomon教授的研究得到了化学系的支持，他的研究采用了多种光谱方法结合电子结构计算来获得对铜和铁硫电子转移（ET）蛋白质的新见解。本研究旨在定义几何和电子结构对生物系统中长距离快速ET的贡献，以及蛋白质在激活金属位点功能中的作用。正在研究的活性位点在N2， N2O和CO2还原的催化，生物技术，温室气体的环境调节以及医疗和健康应用（包括铁和铜的代谢和相关疾病状态）中具有重要意义。了解生物系统中的快速ET以及蛋白质在激活金属位点功能中的作用，将为生物技术和环境调节中重要的活性位点提供基础见解。此外，本研究也适用于铁和铜的代谢及相关疾病状态。在这项工作中开发的光谱方法将适用于生物学和催化中各种重要类别的金属位点。参与这项研究的博士后、研究生和本科生在一系列光谱方法、量子化学、无机化学和酶学方面接受了优秀的培训。

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.