Design of functional metalloenzymes have addressed much attention recently. Heme proteins are a major class and play diverse functions in biological systems, such as O₂ delivery, electron transfer and catalysis. Myoglobin (Mb) is an ideal model protein for heme protein design. In the last decade, we have rationally designed some functional heme enzymes in Mb by developing several strategies, such as by using post-translational modifications (PTM), domain swapping, design of metal-binding site, construct intramolecular disulfide bond, and introduction of non-native cofactors (Fig. 1). The designed artificial metalloenzymes include artificial nitrite reductase, hydrolase, dye-decolorizing peroxidases and dehaloperoxidases, with the catalytic efficiency close to or even exceeding those of native enzymes. Moreover, we have solved the X-ray crystal structure of some artificial enzymes, which provides valuable insights into the structure and function relationship, as well as potential applications.

Ying-Wu Lin received his PhD in 2006 under the supervision of Prof. Zhong-Xian Huang at Fudan University, China. From 2008 to 2010, he did postdoctoral research under supervision of Prof. Yi Lu at University of Illinois at Urbana-Champaign, USA. In 2013, as supported by JSPS fellowship, he did dimeric heme protein design in Nara Institute of Science and Technology, Japan, under supervision of Prof. Shun Hirota. In 2013, he was also promoted to be a full professor of University of South China (USC), Hengyang. Prof. Lin now is the leader of an innovation team, and his current interests focus on rational design of functional heme proteins for applications, as supported by the double first class construct program of USC. Selected publications include Nature, PNAS, JACS, Angew Chem, Coord Chem Rev, ACS Catalysis and Chem Commun.