CATALYTIC METALLO-BIOMIMETIC SITES IN POROUS HOSTS

本研究的目的是通过将金属配合物固定在多孔有机基质中来开发新型仿生催化剂。 该研究将强调加氧酶化学，特别是那些涉及C-H键活化和环氧化反应，以产生具有潜在药物重要性的光学纯分子。 所提出的系统将使用模板共聚方法，其中在聚合过程中发生的固定化位点的形成。 我们建议，这种方法是一种有效的方法来模拟金属网站中发现的蛋白质和系统可以被设计成模拟金属蛋白中发现的各种建筑特征，包括网站隔离的催化金属网站，孔隙度，和控制周围的金属络合物的微环境。 催化金属位点周围的独特微环境是在聚合过程中产生的，并在系统形成后由有机主体维持。 这些高度结构化的活性位点可用于调节外源配体与固定化金属络合物的结合（和随后的化学反应）。 因此，可以产生通常在溶液衍生的低分子量复合物中观察不到的仿生无机物质。 这项工作的长期目标是设计和合成含有蛋白质中发现的外源配体（底物）选择性的系统，但能够在大多数生物分子不稳定和无活性的条件下发挥作用。金属蛋白质进行的化学反应尚未在合成系统中实现。 这种化学多功能性至少部分来自蛋白质通过调节其微环境来调节其金属中心的反应性的能力。 因此，生物学上重要的金属蛋白的功能和功能障碍可以在其微环境变化的背景下理解。 这种类型的分析需要基本的反应性研究，其中可以如本文所述单独分析单个组分的影响。

The aim of this proposed research is to develop new biomimetic catalysts by immobilizing metal complexes in porous organic hosts. The research will emphasize oxygenase chemistry especially those reactions involving C-H bond activation and epoxidation to produce optically pure molecules of potential pharmaceutical importance. The proposed systems will be made using a template copolymerization methodology where the formation of the immobilized sites occurs during polymerization. We propose that this method is an effective way to model metal sites found in proteins and that systems can be designed to simulate various architectural features found in metalloproteins, including site isolation of catalytic metal sites, porosity, and control of the microenvironments around the metal complexes. The unique microenvironments around the catalytic metal sites are created during polymerization and are maintained by the organic hosts after systems are formed. These highly structured active sites can be used to regulate exogenous ligand binding (and subsequent chemistry) to the immobilized metal complexes. Thus biomimetic inorganic species can be produced that are not normally observed in solution-derived, low molecular weight complexes. The long-range objective of this work is to design and synthesize systems that contain exogenous ligand (substrate) selectivity found in proteins yet are able to function under conditions where most biomolecules are unstable and inactive. Metalloproteins perform chemical reactions that have yet to be achieved in synthetic systems. This chemical versatility follows at least in part from the ability of the proteins to regulate the reactivity of their metal centers by adjustments of their microenvironment. Thus the function and disfunction of biologically-important metalloproteins can be understood in the context of changes in their microenvironments. This type of analysis necessitates basic reactivity studies in which the effects of single components can be analyzed individually as described herein.