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

1他的项目，在无机，生物无机和有机 化学课程，将涉及合成和 表征了新的铁硫醇盐络合物， 结合N-H到S氢键，其设计目的是 作为铁硫蛋白的模型。 的目的 研究是为了确定这种氢键对 铁硫醇盐络合物的氧化还原电位。 结果 有望为我们提供重要的洞察力， 其中氧化还原电位在生物中被控制， 分子。 硫醇盐络合物的表征将 涉及电化学（循环伏安法）、红外和 拉曼散射光谱和X射线晶体学。 %%% 含有铁硫簇的蛋白质参与了一个 生物体内发生的各种电子转移过程 系统. 这些的精确驱动力（氧化还原电位） 星系团以微妙的方式变化着，这些方式还不为人所知。 它 已经假设与其他部分的氢键 蛋白质的“调谐”负责氧化还原 潜力 本研究的目的是设计和 合成铁硫簇的模型， 对这一假设进行系统的检验。

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.