De Novo Design of Helical Electron Transfer Metalloproteins

McLendon博士得到了无机，生物无机和 有机化学计划进行实验研究 金属蛋白的电子转移 麦克伦登建议使用 三螺旋肽束来探测 蛋白质中的长程电子耦合。 在展示了 合成方法，使系统的蛋白质结构 作为变型，刚性连接的受体/供体部分可以在 已知距离 这项技术的进步将使检查 电子沿沿着转移的距离依赖。 第二 该提案的一个方面涉及氢键位点的衍生化 在螺旋上。 在螺旋没有明显扰动的情况下 结构或稳定性，拟议的修改将有助于确定 氢键在电子耦合中的作用。 此外，本发明还 侧链电子转移和芳香残基的影响 对电子转移速率的影响。 对金属蛋白中电子转移的理解受到限制， 化学家控制蛋白质结构的能力， 氧化还原介导官能团。 通过建立耦合 系统性蛋白质结构变异测量技术 方法，充分阐明这一现象的障碍可能是 克服

Dr. McLendon is supported by the Inorganic, Bioinorganic and Organometallic Chemistry Program to perform experimental studies of electron transfer in metalloproteins. McLendon has proposed to use three-helix peptide bundles to probe structural relationships in long-range electron coupling in proteins. Having demonstrated a synthetic methodology that allows systematic protein structural variations, rigidly linked acceptor/donor moieties may be introduced at known distances. This advancement in the art will allow the examination of distance dependence upon electron transfer along a helix. A second aspect of the proposal involves derivatization of hydrogen bonding sites on the helix. In the absence of significant perturbations to helix structure or stability, the proposed modification will help determine the role of hydrogen bonding pathways in electronic coupling. Additionally, electron transfer through side chains and the effect of aromatic residues on the rate of electron transfer will be investigated. Understanding electron transfer in metalloproteins has been limited by the ability of chemists to control protein structure, particularly access to redox mediating functional groups. By coupling established measurement techniques with systematic protein structural variation methods, roadblocks to the full elucidation of this phenomenon may be overcome.