X-RAY AND CHEMICAL STUDIES OF METALLOPORPHYRINS

三维X射线晶体结构的测定方法将是 应用于测定金属卟啉的各个方面 立体化学。铁的卟啉与重要的一类有关。 生物分子是一种血红素蛋白，它携带着广泛的生物 功能包括氧的利用和运输，电子传递， 药物代谢和其他酶过程。总的目标是 这项研究是为了建立一个可能的立体化学特征 金属卟啉基团在其生物环境和模型中的特异性 选定的血液蛋白的假体群体行为。这些研究应该 提供对蛋白质结构可能如何调节的理解 金属卟啉几何构型，并允许进行多种工艺 使用相同的基本铁卟啉单元。金属卟啉到 被研究的包括铁(II)和铁(III)的各种轴向配合物 配基。细胞色素c和b的合成类似物将被研究以 探索是什么结构特征导致了它们的氧化还原特性。其他 复合体将利用旨在产生不同寻常的磁性的配体 研究蛋白质如何影响特定磁性状态的性质。 其他研究将集中在金属卟啉是否被氧化或还原。 核心和环与中心之间的电子通信 金属原子。这些物种有兴趣了解 过氧化物酶和过氧化氢酶的重要催化中间体。 潜在底物轴向相互作用的综合研究 亚硝酸盐和亚硫酸盐编辑酶的研究将继续进行。

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.