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作 者:Yuto Kuroda Ryotaro Miyazaki Daiki Shimonishi Daisuke Nakane Takashiro Akitsu Yuto Kuroda;Ryotaro Miyazaki;Daiki Shimonishi;Daisuke Nakane;Takashiro Akitsu(Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan)
机构地区:[1]Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
出 处:《Journal of Materials Science and Chemical Engineering》2023年第3期34-44,共11页材料科学与化学工程(英文)
摘 要:In this study, we exhibited an amino acid (arginine and threonine) derivative Schiff base copper(II) complexes incorporating an azobenzene moiety as a photoresponsive site and conjugated it to egg white lysozyme, a well-known protein, to change ligand conformation under binding to lysozyme. Among several spectroscopic investigations, ESR clearly showed that the nitrogen atom of the amino acid residue of lysozyme was bound to the paramagnetic copper(II) ion of the complex, and UV light irradiation confirmed photoisomerization of the azobenzene moiety of the ligand to cis-form. The binding mode was considered by means of spectroscopic as well as computational methods, whereas complete crystallographic verification was still a preliminary stage.In this study, we exhibited an amino acid (arginine and threonine) derivative Schiff base copper(II) complexes incorporating an azobenzene moiety as a photoresponsive site and conjugated it to egg white lysozyme, a well-known protein, to change ligand conformation under binding to lysozyme. Among several spectroscopic investigations, ESR clearly showed that the nitrogen atom of the amino acid residue of lysozyme was bound to the paramagnetic copper(II) ion of the complex, and UV light irradiation confirmed photoisomerization of the azobenzene moiety of the ligand to cis-form. The binding mode was considered by means of spectroscopic as well as computational methods, whereas complete crystallographic verification was still a preliminary stage.
关 键 词:AZOBENZENE Schiff Base Copper Amino Acid LYSOZYME Artificial Metalloprotein
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