Prof. Ying-Wu Lin
University of South China, China
Title: Rational design of functional metalloenzymes in myoglobin for some applications
Abstract:
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.
Biography:
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.