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

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。 Rieske蛋白的Fe-S簇包含两个与Fe1连接的组氨酸。这一特性使得它不仅可能参与电子传递，还可能参与各种化学反应中的质子传递，如氧化磷酸化、光合成、生物降解等。由于这两个组氨酸是氧化还原电位的关键残基，这两个组氨酸的PKA被证明影响氧化还原电位。我们的方法是观察超精细变化，以获得专门从核磁共振光谱获得的详细信息。为了知道这些信息，我们还需要找到方法来指定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络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).