X-RAY AND CHEMICAL STUDIES OF METALLOPORPHYRINS

三维X射线晶体结构测定方法将 应用于测定金属卟啉的各个方面 立体化学 铁卟啉是一类重要的 生物分子，血红素蛋白，它进行了广泛的生物活性， 功能包括氧的利用和运输，电子运输， 药物代谢和其他酶促过程。 的总体目标 本研究旨在建立一种可能立体化学特征， 金属卟啉基团在其生物环境和模型特异性 所选血红素蛋白的辅基行为。 这些研究应 了解蛋白质结构如何调节 金属卟啉几何形状，并允许进行多种过程 使用相同的基本铁卟啉单元。 金属卟啉 研究包括铁（II）和铁（III）与各种轴向的配合物 配体。 将研究细胞色素c和B的合成类似物， 探索是什么结构特征导致了它们的氧化还原性质。 其他 配合物将利用配体设计，以产生不寻常的磁性 研究蛋白质如何影响特定的磁性状态。 其他研究将集中在具有氧化或还原的金属卟啉上， 核心和电子通信之间的环和中央 金属原子。 这些物种对于理解 过氧化物酶和过氧化氢酶的催化重要中间体。 研究潜在底物轴向相互作用的合成研究 亚硝酸盐和亚硫酸盐还原酶的研究。

The methods of three-dimensional X-ray crystal structure determination will be applied to determine various aspects of metalloporphyrin stereochemistry. The iron porphyrins are related to the important class of biomolecules, the hemoproteins, which carrry out a wide range of biological functions including oxygen utilization and transport, electron transport, drug metabolism, and other enzymatic processes. The overall objective of the research is to establish possible stereochemical features of a metalloporphyrin group in its biological environment and to model specific prosthetic group behavior of selected hemoproteins. These studies should provide an understanding of how protein structure might modulate metalloporphyrin geometry and allow a multitude of processes to be carried out using the same fundamental iron porphyrin unit. Metalloporphyrins to be studied include iron(II) and iron(III) complexes with a variety of axial ligands. Synthetic analogues of cytochrome c and b will be studied to probe what structural features lead to their redox properties. Other complexes will utilize ligands designed to produce unusual magnetic properties to examine how a protein can effect particular magnetic states. Other studies will focus on metalloporphyrins having oxidized or reduced cores and the electronic communication between the ring and the central metal atom. Such species are of interest in understanding the catalytically important intermediates of the peroxidases and catalases. Synthetic studies examining the axial interaction of potential substrates of nitrite and sulfite redactases will be pursued.