BIOMIMETIC HEME CHEMISTRY

一系列新颖的合成卟啉配合物正在被 制备并在结构上表征为功能模型， 几种重要的血红素系统：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 一系列仿生氧化催化剂， 形状选择性和手性氧化。 这些正在被检查 用于制备手性天然产物，包括萜烯和 类固醇. 一系列肌红蛋白模拟物正在制备中， 结构特征和热力学/动力学参数 分子氧结合的能力。 一系列新的 制备了大环/卟啉夹心化合物， 铁衍生物已在其可逆性的背景下进行了分析 分子氧和一氧化碳的结合。 这些物质显示 结合值前所未有的低，但正常值（肌红蛋白样） 用于分子氧结合。 氧气的合成类似物 细胞色素氧化酶的结合/激活位点。 这是由一个含有铜的大环组成， 具有轴向咪唑键合在相对侧上的铁卟啉 的方面想 该复合物结合双氧形成过氧化物。

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.