FUNCTIONAL ANALOGUES OF HEMERYTHRIN

描述：（申请人的摘要）分子氧对于 大多数生命形式的生存。 生物体吸收分子氧的方式是 含金属的蛋白质。 高等生物利用铁元素 一种血红素（血红蛋白、肌红蛋白），用于吸收和运输分子氧。 其他生物体使用邻近的铜离子来提供相同的功能。 蛋白质的生物学研究以及类似物的化学研究 这两类分子氧载体的金属结合位点中， 提供了氧分子如何结合的详细理解， 从金属中释放出来。 第三种主要的双氧转运蛋白是 血红蛋白，含有两个非血红素铁原子， 分子氧 几种半胱氨酸的分子结构 已经知道了一段时间，并且已经建立了双氧结合 但这一过程中许多重要而微妙的细节仍有待解答。 作为 对其他蛋白质的研究表明， 解决这些问题的方法是合成分子氧的小类似物， 结合位点 到目前为止，还没有制备出这种血红蛋白类似物 尽管再现了许多物理特性的优秀模型， 已对血红蛋白进行了表征。 Hemerythrin的作用机制 结合分子氧是非常微妙的，没有合成先例。 氧化过程中存在许多不为人知的元素。 这 本发明的建议是针对合成的金属结合位点的类似物， 血红蛋白。 这些类似物结合了许多在 蛋白 该设计足够灵活，以允许 确定控制分子氧结合的因素， 蛋白 因此，该项目将提供对 分子水平的机制。 这些信息不仅对 对蛋白质作用的短期理解， 利用分子氧作为燃料的一般含义 长期.

DESCRIPTION: (Applicant's abstract) Molecular oxygen is crucial for the survival of most forms of life. Living organisms absorb molecular oxygen by way of metal containing proteins. Higher organisms use iron coordinated to a heme (hemoglobin, myoglobin) to absorb and transport molecular oxygen. Other organisms use proximal copper ions to serve the same function. Biological studies on the proteins as well as chemical studies on analogues of the metal binding sites of these two classes of dioxygen carriers have provided a detailed understanding of how molecular oxygen is bound and released from the metals. The third major dioxygen transporting protein is hemerythrin which contains two non-heme iron atoms which serve to bind molecular oxygen. The molecular structures of a variety of hemerythrins have been known for some time and the dioxygen binding has been established but many important, subtle details of the process remain to be answered. As has been shown for the other proteins, one of the most effective ways of addressing these questions is to synthesize small analogues of the dioxygen binding site. So far no such analogues of hemerythrin have been prepared although excellent models which reproduce many of the physical properties of hemerythrin have been characterized. The mechanism by which hemerythrin binds dioxygen is extraordinarily subtle and has no synthetic precedent. Many poorly understood elements are present in the oxidation process. This proposal is directed at synthesizing analogues of the metal binding site of hemerythrin. These analogues incorporate many of the features found in the protein. The design is sufficiently flexible so as to allow for the identification of the factors which control molecular oxygen binding in the protein. The project will, therefore, provide detailed understanding of the mechanism at the molecular level. Such information is important not only in the short term understanding of the action of the protein but also has wide general implications in the harnessing of molecular oxygen as a fuel in the long term.