RUI: Photochemical and Kinetic Studies of Iron-Only Hydrogenase Model Compounds

在这项由化学系化学催化计划资助的项目中，索诺马州立大学的卡门工作将研究纯铁氢酶模型化合物中分子氢的催化可逆氧化机理。方法是首先合成酶活性中心的二聚铁络合物模型，然后用这些分子来检验光活化这些络合物中的CO的假设，以产生酶活性中心不受抑制的形式的模型，以及CO的配位被溶剂分子占据的假设。将进行的一系列实验包括：光产物反应的共依赖动力学，动力学溶剂效应，确定活化参数的温度研究，监测光产物与分子氢反应的光谱分析，以及量子产率的测定。更广泛的影响包括对本科生进行研究方法培训，将相关材料纳入讲座和实验室课程，并通过出版物和在会议上的陈述广泛传播研究成果。这项工作将加深我们对利用和产生氢的生物酶的理解。这项工作的潜在长期影响可能涉及开发有效的方法来产生氢气作为清洁燃料来源，并在燃料电池中使用氢气。

In this project funded by the Chemical Catalysis Program of the Chemistry Division, Carmen Works of Sonoma State University will study the mechanism of catalyzed reversible oxidation of molecular hydrogen in model compounds of iron-only hydrogenases. The approach is to first synthesize dimeric iron complex models of the enzyme active site, and then to use these molecules to test the hypothesis that light labilizes CO in these complexes to produce a model for the uninhibited form of the enzyme active site and that the coordination site of CO is occupied by a solvent molecule. The series of experiments to be performed include: CO dependent kinetics of the reactions of the photoproduct, kinetic solvent effects, temperature studies to determine activation parameters, spectroscopic analysis to monitor reactions of the photoproduct with molecular hydrogen, and quantum yield determinations. The broader impacts involve training undergraduate students in research methods, incorporating relevant materials into lecture and laboratory courses, and broadly disseminating the research results via publications and presentations at conferences. This work will deepen our understanding of biological enzymes that utilize and generate hydrogen. Potential longer term impacts of the work could involve developing efficient methods to generate hydrogen as a clean fuel source and to use hydrogen in fuel cells.