Hayashi Takashi, Hisaeda Yoshio
Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 812-8581, Japan.
Acc Chem Res. 2002 Jan;35(1):35-43. doi: 10.1021/ar000087t.
The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. Particularly, the modification of two heme-propionates gives us an effective binding domain or binding site on the protein surface. This Account traces the design and construction of the highly ordered binding domain around the entrance of the heme pocket. The discussion includes the protein-small molecule or protein-protein recognition, electron transfer reaction within the complex, and enhancement of the chemical reactivity of the myoglobin with a substrate binding site. The synthetic approach to modifying a protein will be a new trend in engineering a novel function in naturally occurring hemoprotein.
用人工合成的辅基对肌红蛋白进行重组是一种向蛋白质中引入新化学功能的独特方法。特别地，对两个血红素丙酸酯的修饰在蛋白质表面为我们提供了一个有效的结合域或结合位点。本综述追溯了围绕血红素口袋入口处高度有序的结合域的设计与构建。讨论内容包括蛋白质 - 小分子或蛋白质 - 蛋白质识别、复合物内的电子转移反应，以及通过底物结合位点增强肌红蛋白的化学反应性。修饰蛋白质的合成方法将成为在天然存在的血红蛋白中设计新功能的一种新趋势。
