IRON AND MOLYBDENUM COMPLEXES: ENZYME ACTIVE SITES

这项建议涉及到合成，结构， 特定Fe/M/S的光谱和反应性能 (M=Mo，V，W)，Fe/S和Mn/O络合物。这些化合物 分别作为合成类比 Fe/M/S集中在固氮酶中，Fe2S2集中在 Rieske蛋白与水氧化所必需的MN4簇 在光合作用中。金属中心在世界经济中的重要地位 金属蛋白和金属酶功能良好 被认可了。生物化学氧化还原技术 出现在含有活性中心的金属上的底物是 密切参与关键的生命维持过程。 固氮酶(M=Mo，V)中Fe/M/S中心的合成类似物 将得到的具有Fe/M/S特征的光谱分析 与固氮酶相似的特性。一位成功的 固氮酶活性部位的模拟应允许 对生物催化转化(还原)的认识 氮气转化为氨。这种反应也可能对 我们对金属活化小分子的认识 大体上是复合体。专门设计的合成 模拟复合体为Fe2S2，Rieske蛋白中心 对于确定影响 这些中心的氧化还原电位。一种十肽的合成 还将进行Fe2S2中心的综合体。这个 十肽配基是用来提供氨基酸残基的 被认为存在于Rieske蛋白质中。比较 光谱研究有望提供有用的信息。 关于Rieske蛋白质中心。人们对此知之甚少 与水的氧化有关的Mn4中心的结构 在光合作用过程中。关于基本协调的研究 在此之前，需要对低聚核锰团簇进行化学研究 中国锰矿中心专用模拟复合体的设计 光系统II。

This proposal is concerned with the synthesis, structures, spectroscopic, and reactivity properties of specific Fe/M/S (M=Mo, V,W), Fe/S and Mn/O complexes. These compounds respectively are expected to serve as synthetic analogs for the Fe/M/S centers in the nitrogenases, the Fe2S2 centers in the Rieske proteins and the Mn4 cluster essential for water oxidation in photosynthesis. The great importance of metal centers in the function of metalloproteins and metalloenzymes is well recognized. The biochemical oxidation and reduction of substrates that occurs at metal containing active sites is intimately involved with crucial life sustaining processes. Synthetic analogs for the Fe/M/S center in nitrogenase (M=Mo, V) will be obtained with a Fe/M/S features, and spectroscopic characteristics similar to those in nitrogenase. A successful analog for the nitrogenase active site should allow for an understanding of the biological catalytic conversion (reduction) of dinitrogen to ammonia. This reaction also is potentially useful for our understanding of small molecule activation by metal complexes in general. The synthesis of specifically designed analog complexes for the Fe2S2, Rieske protein center will be important for the identification of the factors that affect the redox potentials of these centers. The synthesis of a decapeptide complex of the Fe2S2 center also will be carried out. The decapeptide ligand is designed to supply the amino acid residues thought to be present in the Rieske proteins. Comparative spectroscopic studies are expected to provide useful information regarding the Rieske protein centers. Very little is known about the structure of the Mn4 center involved in the oxidation of water during photosynthesis. Studies of the basic coordination chemistry of oligonuclear Mn clusters are needed prior to the design of specific analog complexes for the Mn center in photosystem II.