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Stappen, C.V., Deng, Y., Liu, Y., Heidari, H., Wang, J.-X., Zhou, Y., Ledray, A.P. and Lu, Y. (2022) Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere. Chemical Reviews, 122, 11974-12045.
https://doi.org/10.1021/acs.chemrev.2c00106

has been cited by the following article:

• TITLE: Coordination and Photoisomerization of Azobenzene-Amino Acid Schiff Base Copper(II) Complexes to Lysozyme

  AUTHORS: Yuto Kuroda, Ryotaro Miyazaki, Daiki Shimonishi, Daisuke Nakane, Takashiro Akitsu

  KEYWORDS: Azobenzene, Schiff Base, Copper, Amino Acid, Lysozyme, Artificial Metalloprotein

  JOURNAL NAME: Journal of Materials Science and Chemical Engineering, Vol.11 No.3, March 31, 2023

  ABSTRACT: 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.