Electronic Structures of ET Active Sites and their Contributions to Reactivity

Stanford University, Stanford CA

Investigators

Abstract

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.