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

他的项目在无机、生物无机和有机金属化学项目中，将涉及新的铁硫酸盐配合物的合成和表征，这些配合物包含N-H到S氢键，旨在作为铁硫蛋白质的模型。本研究的目的是确定这种氢键对硫代铁配合物氧化还原电位的影响。该结果有望为生物分子中氧化还原电位的控制方式提供重要的见解。硫酸盐配合物的表征将涉及电化学（循环伏安法）、红外和拉曼散射光谱以及x射线晶体学。含有铁硫团簇的蛋白质参与了生物系统中发生的各种电子转移过程。这些团簇的精确驱动力（氧化还原电位）以微妙的方式变化，目前尚不清楚。据推测，与蛋白质其他部分的氢键是“调节”氧化还原电位的原因。本研究的目的是设计和合成铁硫簇的模型，这将允许对这一假设进行系统的测试。

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.