Coordination of protoporphyrin IX-iron-complexes to hem-regulated proteins studied by EPR-spectroscopy and X-ray crystallography (C08)

为了最终确定我们的细菌蛋白中血红素调控基序（HRM）的综合理化数据库，我们将合成基于tyrr的HRM肽，并通过各种光谱方法（主要是紫外/可见光谱和epr光谱）分析它们与自旋中心血红素的配合物。这将是C8的主要目标，揭示调控血红素蛋白相互作用的分子和功能细节。在上一个资助期内，我们已经成功地鉴定、生产和纯化了血红素调节的细菌蛋白。现在我们将使用x射线晶体学、PELDOR光谱、肽表位扫描、酶分析和体内研究来关注这个问题，即与自旋中心血红素的相互作用如何调节我们的细菌靶蛋白的功能。

To finalize our comprehensive physicochemical database of heme regulatory motifs (HRM) in bacteri-al proteins, Tyr-based HRM peptides will be synthesized and their complexes with the spin center heme will be analyzed by various spectroscopic methods, primarily UV/vis- and EPR-spectroscopy. It will be the main goal of C8 to unravel the molecular and functional details of regulatory heme-protein interactions. In the last funding period, we have successfully identified, produced and purified heme-regulated bacterial proteins. Now we will use X-ray crystallography, PELDOR spectroscopy, peptide epitope scans, enzymatic assays and in vivo studies to focus on the question, how the interaction with the spin center heme tunes the function of our bacterial target proteins.