RELATIONSHIPS BETWEEN REDOX POTENTIAL, HYPERFINE SHIFTS, AND THE PKA(S)

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 中心，不一定是研究者的机构。 Rieske蛋白的Fe-S簇含有两个与Fe 1连接的组氨酸。 这一特性使得它不仅可以参与电子传递，还可以参与氧化磷酸化、光合作用、生物降解等各种化学反应中的质子传递。由于两个组氨酸是决定氧化还原电位的关键残基，因此这两个组氨酸的pKa值对氧化还原电位有很大的影响。 我们的方法是观察超精细位移，以获得专门从NMR光谱学获得的详细信息。 为了了解这些信息，我们还需要找到方法来分配两个组氨酸和所有密切相关的核，如果它们在光谱中可观察到的话。 这些实验可能是研究配合物中电子输运和质子洗牌的关键。

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. The Fe-S cluster of the Rieske protein contains two ligated histidines with the Fe1. The special feature makes it highly possible to involve in not only in the electron transfer, but also in the proton transfer in various kinds of chemical reactions, such as oxidative phosphorylation, photosythesis, biodegradation etc. Since the two histidines are key residues of the redox potential, the pKa of these two are showed to affect the redox potential. Our approach is to watch for the hyperfine shift to get detailed information available exclusively from NMR spectroscopy. In order to know these information, we also need to find ways to assign the two histidines and all the closely related nuclei if they are observable in the spectra. These experiments may be keys to the electron transportation and the proton shuffle in the complex(es).