Cluster Transformations Relevant to Nitrogenase Cofactor

这项授予普林斯顿大学的启动资金支持了以下研究： Sonny C.教授李你 研究重点是改进 了解铁钼辅因子的结构化学 通过研究金属硫簇核心在固氮酶中的作用 重新安排 已知某些反应会将常见的 铁硫几何形状成簇轴承结构的亲和力， 辅因子 将这种化学作用应用于新的簇类以构建 具有类似于 铁钼辅因子 团簇，其是以下的几何异构体： 辅因子是特定的目标，目标是实现集群， 与辅因子具有基本拓扑同源性。 这项研究促进了对基本结构的理解， 铁硫簇的化学，导致化学进展 了解固氮酶。 固氮酶催化 将大气中的二氮还原为氨，这是一种对 固定氮的生物有效性。

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.