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

为了完成我们全面的细菌蛋白质中血红素调节基序(HRM)的物理化学数据库，我们将合成基于Tyr的HRM多肽，并将通过各种光谱方法分析它们与自旋中心血红素的络合物，主要是UV/VIS和EPR光谱。C8的主要目标将是揭开调节血红素-蛋白质相互作用的分子和功能细节。在过去的资助期间，我们成功地鉴定、生产和提纯了受血红素调节的细菌蛋白。现在，我们将使用X射线结晶学、PELDOR光谱、多肽表位扫描、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细菌目标蛋白的功能。

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.