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

Fe-S 蛋白质中 N-H 与 S 氢键作用的模型

• 批准号: 9203455
• 负责人: Marc Walters
• 金额: $ 21.5万
• 依托单位: New York University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1992
• 资助国家: 美国
• 起止时间: 1992-08-15 至 1996-01-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9203455&HistoricalAwards=false
• 关键词: Models; Effects; Hydrogen; Bonding; Fe

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.

1他的项目属于无机、生物无机和有机金属化学项目，将涉及新型硫醇铁络合物的合成和表征，该络合物包含 N-H 至 S 氢键，旨在作为铁硫蛋白的模型。 该研究的目的是确定此类氢键对硫醇铁络合物氧化还原电位的影响。 预计这些结果将为生物分子中氧化还原电位的控制方式提供重要的见解。 硫醇盐复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。 %%% 含有铁硫簇的蛋白质参与生物系统中发生的各种电子转移过程。 这些簇的精确驱动力（氧化还原电位）以微妙的方式变化，但目前尚不清楚。 据推测，与蛋白质其他部分的氢键作用负责“调节”氧化还原电位。 这项研究的目的是设计和综合铁硫簇的模型，以便系统地检验这一假设。