IRON-SULFUR PROTEIN ASSEMBLY

点击翻译按钮获取中文摘要

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. Iron-sulfur ([Fe-S]) clusters are simple inorganic groups found in various organisms. The proteins holding the [Fe-S] clusters can have various unique functions: electron transfer, gene regulation, environmental sensing, and substrate activation. In particular, among several [Fe-S] cluster assembly and transfer protein systems, IscU is a very fascinating protein because of its unique biological functions and flexible characteristics. To date, it is believed that IscU assembles the [2Fe-2S] cluster and transfers it to ferredoxins. However, the actual mechanisms involved in the cluster assembly and transfer have not been described previously in the molecular level. Therefore, by investigating IscU with the nuclear magnetic resonance (NMR) spectroscopy, we are expecting that the structural dynamics of IscU can be determined, which may explain the molecular mechanisms of IscU as well. In addition, we are trying to analyze the paramagnetic signals of holo-IscU and to investigate the characteristic pattern of coordinating the [Fe-S] cluster. This may elucidate many unknown properties of the interaction between IscU and the [Fe-S] cluster.