Chemical Approach to New Conversion of Hemoprotein Function

用人工合成的辅基重建肌红蛋白是一种独特的方法，可以将新的化学功能引入蛋白质中。在这个项目中，我们提出了两种方法的重组方法，以创建一个新的功能到肌红蛋白。一种是血红素丙酸酯侧链的修饰，另一种是血红素骨架的修饰。本文的主要研究成果如下：1.通过蛋白质表面上的人工界面构建蛋白质-蛋白质复合物;例如。重组肌红蛋白-细胞色素c复合物.在人工蛋白质复合物内监测光诱导电子转移。这是一个适合于阐明生物系统中复杂电子传递机制的模型.重组肌红蛋白在肌红蛋白表面添加底物结合位点后表现出过氧化物酶和/或过氧合酶活性。两个血红素丙酸酯侧链在肌红蛋白中的作用被证明是由缺少一个丙酸酯的特殊血红素重建的新肌红蛋白。结果表明，用二茂铁卟啉重构的肌红蛋白具有极高的氧亲和力，为制备功能化血红素蛋白开辟了一条新的途径。

The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. In this project, we proposed two approach to the reconstitutional method in order to create a new function into myoglobin. One is the modification of heme-propionate side chains, and another is the modification of heme framework. The summary of our recent results are shown as follows :1. Protein-protein complex via an artificial interface on the protein surface was constructed ; e.g.. reconstituted myoglobin - cytochrome c complex.2. Photoinduced electron transfer was monitored within the artificial protein complexes. It is a suitable model to elucidate the mechanism of the complicated electron transfer in biological systems.3. Reconstituted myoglobin exhibits peroxidase and/or peroxygenase activities upon the addition of substrate binding site on the myoglobin surface.4. The role of two heme-propionate side chains in the myoglobin was proved by new myoglobin reconstituted with the special heme lacking one of the propionates.5. It is found that myoglobin reconstituted with iron porphycene shows extremely high dioxygen affinity.The net results demonstrate that the reconstitutional method will serve as a new way in the creation of a unique functionalized hemoprotein.