PROTEIN COMPLEXES INVOLVED IN ELECTRON TRANSFER AND BACTERIAL CHEMOTAXIS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 我们的目标是了解生物学中远程电子转移(ET)的结构基础。多肽链的大量构象和化学状态允许自然调节金属中心的反应性和蛋白质内部和蛋白质之间的直接电子流动。我们开发和应用了新的光化学方法来研究蛋白质单晶中的ET，其中的结构可以通过X射线结晶学来精确确定。设计的固定供体和受体取向的晶体系统允许通过将晶体中的速率测量与高分辨率结构确定相结合来探索介入蛋白质和水结构对ET的影响。目前，在细胞色素c过氧化物酶(CCP)和细胞色素c(CC)之间的络合物的晶体中直接确定ET率。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We aim to understand the structural basis for long-range electron transfer(ET) in biology. The vast number of conformational and chemical states available to the polypeptide chain allows nature to tune the reactivity of metal centers and direct electron flow within and between proteins. We have developed and applied new photochemical methods for studying ET in single protein crystals, where structure can be precisely defined by X-ray crystallography. Designed crystal systems that fix donor and acceptor orientation allow effects of intervening protein and water structure on ET to be probed by combining rate measurements in the crystals with high-resolution structure determinations. ET rates are currently being determined directly in crystals of complexes between cytochrome c peroxidase (CcP) and cytochrome c (Cc).