EFFECT OF PROTEIN MUTATION ON ACTIVE SITE STRUCTURE IN CYTOCHROME C

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。 FEK-Edge XAS数据将被测量在电子转移蛋白细胞色素c(Cytc)上。具有组氨酸-蛋氨酸(His-Met)铁配位作用的C型细胞色素在电子传递反应和酶中起着重要作用。轴向蛋氨酸配体在稳定蛋白质和维持低氧化还原电位方面起着重要作用。铜绿假单胞菌(PA)和亚硝酸单胞菌(Ne)cytc的蛋白质突变在其活性部位显示出不同的菱形(用电子顺磁共振波谱)，这与铁-S(Met)键的扰动有关。FE K-EDGE EXAFS数据将揭示随着蛋白质环境的变化，电子转移活性部位的特定几何结构的变化。

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. Fe K-edge XAS data will be measured on the electron transfer protein cytochrome c (cytc). The c-type cytochromes that have histidine-methionine (His-Met) iron coordination play important roles in electron-transfer reactions and in enzymes. The axial methionine ligand plays a major role in stabilizing the protein and maintaining a low redox potential. Protein mutations of Pseudomonas aeruginosa (Pa) and Nitrosomonas europeae (Ne) cytc show differences in rhombicity (using EPR spectroscopy) in their active site, which have been linked to perturbations in the Fe-S(Met) bond. Fe K-edge EXAFS data will shed light on specific geometric structure changes at the electron-transfer active site with changes in the protein environment.