Creation of Novel Functional Protein by Self-hydroxylation

点击翻译按钮获取中文摘要

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.