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Preliminary Investigation of Copper(II) Ion Binding or Complex Coordination in Lysozeme Molecules
Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
Department of Chemistry, Faculty of Science, Obafemi Awolowo University, Ile-Ife, Nigeria
Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
- 1 Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
- 2 Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
- 3 Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
- 4 Department of Chemistry, Faculty of Science, Obafemi Awolowo University, Ile-Ife, Nigeria
- 5 Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan
Journal of Materials Science and Chemical Engineering·Volume 12 (2024)·Pages 98–103·Published 7 April 2024·DOI10.4236/msce.2024.124008
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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.
KeywordsCopperSchiff BaseLysozymeMetal-Protein BindingComputational Methods
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