Creation of Novel Functional Protein by Self-hydroxylation

近年来，报道了许多芳香族氨基酸的自羟化反应，芳香族氨基酸位于单核和双核铁、铜结合部位附近。在本研究中，我们使用含有三个或四个组氨酸结合基序(3-His或4-His基序)的Cupin家族蛋白作为金属结合支架。在将一种酪氨酸引入Ile49或Trp56位置的突变体中，发现了800 nm左右的非自然存在的异常光谱物种。因此，本研究提出的修饰方法对于构建新型生物电子器件和人工金属酶催化多电子转移反应的新型功能蛋白具有重要意义。

Recently, many self-hydroxylation reactions have reported, which occurred of aromatic amino acids lying close to mononuclear and dinuclear iron and copper binding site. In this study, we utilized cupin family protein bearing three or four histidine binding motif (3-His or 4-His motif) as metal binding scaffold. In the mutant introduced one tyrosine into the location of Ile49 or Trp56, non-natural occurring unusual spectral species around 800 nm have been found. Thus, the modification method presented in this study is very powerful to construct new functional protein for novel devices of bioelectronics and artificial metalloenzyme to be able to catalyze multielectron transfer reactions.