Cluster Transformations Relevant to Nitrogenase Cofactor

普林斯顿大学的启动基金资助了Sonny C. Lee教授的研究。本研究的重点是通过研究金属-硫簇核重排来提高对氮酶中铁钼辅助因子的结构化学的理解。已知某些反应可将常见的铁硫几何形状转化为与辅因子具有结构亲和力的簇。这种化学反应被应用于新的簇类，以构建具有类似于铁钼辅因子的结构特征的更高核簇。作为辅助因子几何异构体的簇是特定的目标，其目标是获得与辅助因子具有实质性拓扑同源性的簇。该研究促进了对铁硫簇的基本结构化学的理解，导致对氮酶的化学理解取得进展。氮酶催化大气中的二氮还原为氨，这是一个对固定氮的生物可利用性至关重要的反应。

This starter grant award to Princeton University supports the research of Professor Sonny C. Lee. The research focuses on an improved understanding of the structural chemistry of the iron-molybdenum cofactor in nitrogenase enzymes through investigation of metal-sulfur cluster core rearrangements. Certain reactions are known to transform common iron-sulfur geometries into clusters bearing structural affinities to the cofactor. This chemistry is applied to new clusters classes to construct higher nuclearity clusters with structural features similar to the iron-molybdenum cofactor. Clusters which are geometric isomers of the cofactor are specific targets, with the goal of attaining clusters with substantial topological homology to the cofactor. The research advances understanding of the fundamental structural chemistry of iron-sulfur clusters, leading to progress toward a chemical understanding of nitrogenase. The nitrogenase enzymes catalyze the reduction of atmospheric dinitrogen to ammonia, a reaction critical to the biological availability of fixed nitrogen.