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

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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).