Engineering Fe Site Into Host Proteins

该奖项在无机，生物无机和有机 化学计划与仪器的资金从办公室 多学科活动支持实验室的研究 耶鲁大学的约翰·卡拉多纳教授。 这项研究涉及一个 半合成设计方法来探测蛋白质对 Fe/S立方体的还原电位和电子转移活性 铁硫蛋白与含铁超氧化物中的铁位 歧化酶（SOD）。 选择性突变的蛋白质已经被设计出来 通过计算机方法和生物技术构建。 的SOD 蛋白具有催化活性。 这些蛋白质将被 通过一系列物理方法系统地确定 研究了氢键、局域电荷和偶极对 蛋白质中金属中心的电子转移活性。 这项研究利用了金属研究的新成果 通过将铁位点整合到宿主蛋白质中而在蛋白质中形成中心。 的 目的是构建具有功能的金属蛋白活性位点， 已知结构的宿主蛋白质。 这允许高度控制 金属中心的环境，这系统地证明了 研究蛋白质对金属位点活性的影响。

This award in the Inorganic, Bioinorganic and Organometallic Chemistry program with instrumentation funding from the Office of Multidisciplinary Activities supports research in the laboratory of Professor John Caradonna at Yale University. The research involves a semisynthetic design approach to probe the protein effects on the reduction potential and electron transfer activity of the Fe/S cube in iron-sulfur proteins and the iron site in iron-containing superoxide dismutase (SOD). Selectively mutated proteins have already been designed by computer methods and constructed by biological techniques. The SOD protein exhibits catalytic activity. The proteins will now be characterized by an array of physical methods to systematically determine the effects of hydrogen bonding, localized charges and dipoles on the electron transfer activities of the metal centers in the proteins. This research utilizes a new achievement in the study of metal centers in proteins by incorporating iron sites into host proteins. The objective is to construct functional metalloprotein active sites inside host proteins of known structure. This allows a high degree of control of the environment of the metal center, which provdes for systematically studying the effects of the protein on the metal site's activity.