MODELING COPPER PROTEIN--NITROGEN OXIDE INTERACTIONS

各种形式的简单形式之间的生物相互转化 简单的含氮化合物是基本上重要的过程， 全球氮循环 金属蛋白在许多 微生物在实现这些转化中起关键作用， 因此在控制简单的含氮化合物的平衡中是重要的 地球上的分子 这些物质的相对浓度不平衡， 环境中的化合物会对生态系统产生重大影响 和人类健康，从而为研究 控制金属蛋白的作用。 含铜酶是 在反硝化中很重要，反硝化是生物学中的一个中心过程， 氮循环，其中几类微生物利用氧化 氮化合物作为呼吸作用中的末端电子受体。 具体来说，酶中的铜中心参与了几个步骤， 硝酸盐（NO3-）和亚硝酸盐（NO2-）转化为气态产物 (NO、N2 O和/或N2）。 虽然已经有 在了解这些活性位点结构方面的进展， 酶，各种假设的途径的可接受性， 它们所起的复杂化学作用尚未确定。 在 此外，普遍缺乏基础化学知识， 铜-NxOy物种阻碍了更好地理解如何 氮氧化物与生物铜中心结合并被其活化。 拟议的研究旨在通过集中精力解决这一缺陷， 关于合成，有趣的物理和光谱表征，以及 详细研究了铜-氮氧化物络合物的反应性， 模型的含铜酶的活性位点的重要性， 生物氮循环 将特别强调 NO、NO2-、N2 O3的单核Cu（I）和Cu（II）络合物的构建 - 和N2 O2 -2-由多齿、仿生和空间上 受阻配体 类似物活性中心特征的描绘 蛋白质活性位点将通过深入研究 这些合成模型化合物的结构和反应化学。

Biological interconversions between the various forms of simple forms of simple nitrogen compounds are fundamentally significant processes within the global nitrogen cycle. Metalloproteins within numerous microorganisms play a key role in effecting these transformations and are thus important in controlling the balance of simple nitrogen-containing molecules on earth. Imbalances in the relative concentrations of such compounds in the environment can have significant effects on ecosystems and human health, thus providing impetus for the study of how the controlling metalloproteins operate. Copper-containing enzymes are important in denitrification, a central process in the biological nitrogen cycle whereby several classes of microorganisms utilize oxidized nitrogen compounds as terminal electron acceptors in respiration. Specifically, copper centers in enzymes are involved in several steps in the conversion of nitrate (NO3-) and nitrite (NO2-) to gaseous products (NO, N20 and/or N2). Although there have been advances in understanding aspects of the active site structures of such enzymes, the plausibility of various postulated pathways for the complicated chemistry that they perform has not been determined. In addition, a general lack of knowledge of the fundamental chemistry of copper-NxOy species has hindered attempts to better under-stand how nitrogen oxides bind to and am activated by biological copper centers. The proposed research is designed to address this deficiency by focusing on the synthesis, fun physical and spectroscopic characterization, and detailed study of the reactivity of copper-nitrogen oxide complexes that model the active sites of copper-containing enzymes important in the biological nitrogen cycle. Particular emphasis will be placed on the construction of mononuclear Cu(I) and Cu(II) complexes of NO, N02-, N203 -, and N202-2- supported by multidentate, biomimetic, and sterically hindered ligands. Delineation of the active site features of analogous protein active sites will be accomplished through in-depth studies of the structures and reaction chemistry of these synthetic model compounds.