HEME PROTEIN MODEL STUDIES UTILIZING RUTHENIUM PORPHYRINS

该项目的长期目标是更好地了解 使用钌卟啉和 钌取代的肌红蛋白和血红蛋白作为模型系统， 天然存在的蛋白质 对氧结合的广泛理解 血红蛋白将提供信息，以更好地处理遗传疾病 包括血红蛋白。 该项目的具体目标有两个方面。 首先，配体交换动力学，电化学，和光谱， 将研究一系列钌（II）卟啉，以确定 配体与钌卟啉的键合模式。 这很重要 了解这些钌卟啉是如何起作用的， 加入到血红蛋白中。 第二，一系列钌取代 血红素蛋白质将被制备，并研究它们的CO和O2亲和力。 为了了解更多关于天然配体结合的机制， 血红蛋白。

The long range objectives for this project are to better understand the mechanism of ligand binding in heme proteins using ruthenium porphyrins and ruthenium substituted myoglobin and hemoglobin as model systems for the naturally occurring proteins. A broad understanding of oxygen binding in hemoglobin will provide information to better deal with genetic diseases involving hemoglobin. The specific aims of the project are two fold. First, the ligand exchange kinetics, electrochemistry, and spectroscopy of a series of ruthenium(II) porphyrins will be studied in order to determine the mode of bonding of ligands to ruthenium porphyrins. This is important to an understanding of how these ruthenium porphyrins function when incorporated into hemoglobin. Second, a series of ruthenium substituted heme proteins will be prepared and their CO and O2 affinities studied in order to learn more about the mechanism of ligand binding in native hemoglobin.