BIOMIMETIC HEME CHEMISTRY

一系列新颖的人工合成的卟啉配合物正在被 准备并在结构上表征为功能模型 几个重要的血红素系统：血红蛋白、肌红蛋白、细胞色素 P-450和细胞色素氧化酶。这种化学反应导致了一部小说 展示了一系列仿生充氧催化剂 构型选择性和手性氧化。这些都正在接受检查 用于制备手性天然产物，包括萜类和 类固醇。一系列肌红蛋白模拟物正在准备中， 结构表征和热力学/动力学参数 对于氧结合的影响正在被测量。一系列新的 制备了大环/卟啉夹心化合物，并对其进行了表征。 铁衍生物已经在其可逆性的背景下进行了分析 二氧化碳和一氧化碳的结合。这些物质表明 前所未有的低结合值但正常值(肌红蛋白样值) 用于氧气结合。一种氧的合成类似物 已在细胞色素氧化酶中制备了结合/活化部位。 这由一个包含铜的宏循环组成，位于 具有轴向咪唑键合在相反面上的铁卟啉 边上。这种络合物与氧气结合形成过氧化氢。

A series of novel, synthetic porphyrin complexes are being prepared and structurally characterized as functional models for several important heme systems: hemoglobin, myoglobin, cytochrome P-450, and cytochromec oxidase. This chemistry has led to a novel series of biomimetic oxygenation catalysts which exhibit shape-selectivity and chiral oxygenation. These are being examined for the preparation of chiral natural products, including terpenes and steroids. A series of myoglobin mimics are being prepared, structurally characterized and the thermodynamic/kinetic parameters for dioxygen binding are being measured. A new series of macrocycle/porphyrin sandwich compounds has been prepared and their iron derivatives have been analyzed in the context of their reversible binding of dioxygen and carbon monoxide. These substances show unprecedented low values of binding but normal values (myoglobin-like) for dioxygen binding. A synthetic analogue for the oxygen binding/activating site in cytochromec oxidase has been prepared. This consists of a macrocycle containing copper positioned over an iron porphyrin which has an axial imidazole bound on the opposite side. This complex binds dioxygen to form a peroxide.