Spectroscopic Studies of Blue Copper and Iron Sulfur Electron Transfer Active Sites

斯坦福大学的所罗门教授将进行 研究旨在阐明光谱的某些 金属蛋白在无机，生物无机 组织者计划。 感兴趣的蛋白质是那些 含有蓝铜和铁硫位点， 要获得的信息是更详细的描述， 它们的电子结构和电子贡献 结构的电子转移反应性，这些活性 网站. 使用的光谱方法包括偏振 吸收，变温磁性圆二色性， 单晶多频EPR，共振拉曼，可变 能量PES和X射线吸收。 这些实验方法 将与配体场和SCF-X α-SW结合 计算。这些技术将应用于研究 Fe（II）、Fe（III）、Cu（I）和 Cu（II）。从这些研究中获得的信息将 允许评估电子结构对 不寻常的还原电位和电子的快速速率 传递真实的蛋白质。 此外，一个类似的集合 将对各种突变体进行实验， 修改蓝铜蛋白，以测试扣除 来自模型研究。 %%% 一系列复杂的光谱技术将 以了解活性位点的键合 两类含金属蛋白质的结合 这些蛋白质 含有铜-硫或铁-硫中心， 在大多数生物体中， 运输链。 所采取的办法将需要 详细的实验和理论研究的简单模型， 活性位点，以及一系列的实验研究， 修饰的铜蛋白。 获得的信息将导致 来理解金属点的键合 控制这些反应的速率和能量 proteins.

Professor Solomon of Stanford University will conduct studies designed to elucidate the spectroscopy of certain metalloproteins under support from the Inorganic, Bioinorganic and Organometallic Program. The proteins of interest are those that contain Blue Copper and Iron Sulfur sites, and the information to be obtained is a more detailed description of their electronic structures and the contributions of electronic structure to the electron-transfer reactivity of these active sites. Spectral methods to be used include polarized absorption, variable-temperature magnetic circular dichroism, single crystal multifrequency EPR, resonance Raman, variable energy PES, and X-ray absorption. These experimental methods will be combined with ligand field and SCF-Xalpha-SW calculations. These techniques will be applied in studies of simple coordination complexes of Fe(II), Fe(III), Cu(I) and Cu(II). The information obtained from these studies will then allow evaluation of the influence of electronic structure on the unusual reduction potentials and rapid rates of electron transfer of the real proteins. In addition, an analogous set of experiments will be conducted on a variety of mutant and modified blue copper proteins in order to test the deductions derived from the model studies. %%% A diverse array of sophisticated spectroscopic techniques will be used in order to learn about the bonding at the active sites of two classes of metal-containing proteins. These proteins contain either copper-sulfur or iron-sulfur centers, are found in most organisms, and function in the physiological electron transport chains. The approach to be taken will entail detailed experimental and theoretical study of simple models of the active sites, as well as experimental study of a series of modified copper proteins. The information obtained will lead to an understanding of how the bonding at the metal sites controls the rates and energetics of reactions of these proteins.