Mössbauer spectroscopic methods to study iron-sulfur assembly, disassembly and catalysis

在这个项目的框架内，我们希望通过穆斯堡尔谱来澄清铁硫中心的功能相关，电子和结构性质。在实验室中使用传统的穆斯堡尔谱，我们确定新发现的蛋白质中的铁硫中心，研究底物与酶活性铁硫中心的结合，并研究整个细胞中Fe-S中心的组装。使用穆斯堡尔谱在高磁场中，我们确定特别是抗磁性Fe-S中心和它们与配体的相互作用，如NO.与基于同步加速器的核非弹性散射（NIS）的帮助下，也称为核共振振动光谱（NRVS），铁硫中心的振动进行了实验研究。用量子化学方法计算了振动模式的结构模型。在第一个资助期的第一次成功实验之后，我们希望继续将这种方法应用于模型复合物的单晶以及更复杂的铁硫蛋白质，如固氮酶。

Within the framework of this project, we want to contribute to the clarification of function-relevant, electronic and structural properties of iron-sulfur centers by means of Mössbauer spectroscopy. Using conventional Mössbauer spectroscopy in the laboratory, we identify iron-sulfur centers in newly discovered proteins, study the binding of substrates to enzymatically active iron-sulfur centers, and investigate the assembly of Fe-S centers in whole cells. Using Mössbauer spectroscopy in high magnetic fields we identify in particular diamagnetic Fe-S centers and their interaction with ligands such as NO. With the help of synchrotron-based Nuclear Inelastic Scattering (NIS), also called Nuclear Resonance Vibrational Spectroscopy (NRVS), vibrations of the iron-sulfur centers are experimentally investigated. Using quantum chemical methods based on structural models the vibrational modes are calculated. After first successful experiments during the 1st funding period we want to continue applying this methodology to single crystals of model complexes as well as to more complex iron-sulfur proteins such as nitrogenase.