Models of Effects of N-H to S Hydrogen Bonding in Fe-S Proteins

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1his project, in the Inorganic, Bioinorganic and Organometallic Chemistry Program, will involve the synthesis and characterization of new iron thiolate complexes that incorporate N-H to S hydrogen bonds, which are designed to serve as models for iron-sulfur proteins. The objective of the study is to determine the effect of such hydrogen bonds on the redox potential of the iron thiolate complexes. The results are expected to provide significant insight into the way in which the redox potentials are controlled in the biological molecules. Characterization of the thiolate complexes will involve electrochemistry (cyclic voltammetry), infrared and Raman scattering spectroscopies, and x-ray crystallography. %%% Proteins that contain iron-sulfur clusters are involved in a variety of electron transfer processes that occur in biological systems. The precise driving force (redox potential) for these clusters varies in subtle ways that are not yet understood. It has been hypothesized that hydrogen bonding to other portions of the protein is responsible for "tuning" of the redox potential. The objective of this research is to design and synthesize models for the iron-sulfur clusters that will allow for a systematic test of this hypothesis.