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Handing, K., Niedzialkowska, E., Shabalin, I., Kuhn, M.L., Zheng, H. and Minor, W. (2018) Characterizing Metal-Binding Sites in Proteins with X-Ray Crystallography. Nature Protocols, 13, 1062-1090.
https://doi.org/10.1038/nprot.2018.018

has been cited by the following article:

• TITLE: Preliminary Investigation of Copper(II) Ion Binding or Complex Coordination in Lysozeme Molecules

  AUTHORS: Kou Takahashi, Ryotaro Miyazaki, Daisuke Nakane, Temitayo O. Aiyelabola, Takashiro Akitsu

  KEYWORDS: Copper, Schiff Base, Lysozyme, Metal-Protein Binding, Computational Methods

  JOURNAL NAME: Journal of Materials Science and Chemical Engineering, Vol.12 No.4, April 30, 2024

  ABSTRACT: Hydrophobic Val derivative Schiff base copper(II) complexes and dipeptide (AlaAla, GlyGly) derivative Schiff base copper(II) complexes were introduced into egg white lysozyme. X-ray crystal structure analysis revealed amino acid derivative Schiff base copper(II) complexes were obtained. Herein we discuss primarily on the binding mode of copper(II) of the complexes obtained with egg white lysozyme. The electron density of copper(II) ions was confirmed by X-ray crystal structure analysis. The Val derivative Schiff base copper(II) complex was weakly bound at Arg114 of egg white lysozyme. In other copper(II) complexes, binding of copper(II) ions with dissociated ligands to various residues was observed. The binding sites of copper(II) ions were compared with computational scientific predictions.