Crystallographic and Computational Electron Density of d Orbitals of Azo-Schiff Base Metal Complexes Using Conventional Programs.

The crystal structures of two azobenzene derivative Schiff base metal complexes (new CHCuNO of -1 and known CHMnNO of 2/c abbreviated as Cu and Mn, respectively) were (re-)determined experimentally using conventional X-ray analysis to obtain electron density using a PLATON program. Cu affords a four-coordinated square planar geometry, while Mn affords a hexa-coordinated distorted octahedral geometry whose apical sites are occupied by an acetate ion and water ligands, which are associated with hydrogen bonds. The π-π or CH-π and hydrogen bonding intermolecular interactions were found in both crystals, which were also analyzed using a Hirshfeld surface analysis program.

Crystal structure and Hirshfeld surface analysis of (aqua-κ)(methanol-κ)[-(2-oxido-benzyl-idene)threoninato-κ ,,']copper(II).

In the title complex mol-ecule, [Cu(CHNO)(CHO)(HO)], the Cu atom is coordinated in a distorted square-pyramidal geometry by a tridentate ligand synthesized from l-threonine and salicyl-aldehyde, one methanol mol-ecule and one water mol-ecule. In the crystal, the mol-ecules show intra- and inter-molecular O-H⋯O hydrogen bonds. The Hirshfeld surface analysis indicates that the most important contributions to the packing are H⋯H (49.

Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex.

A salen-type Schiff base Zn(II) complex included in human serum albumin (HSA) protein was examined by UV-Vis, circular dichroism (CD), and fluorescence (PL) spectra. The formation of the composite material was also estimated by a GOLD program of ligand-protein docking simulation. A composite cast film of HSA and Zn(II) complex was prepared, and the effects of the docking of the metal complex on the degradation of protein molecules by mid-infrared free electron laser (IR-FEL) were investigated.

Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation.

An infrared free electron laser (IR-FEL) can decompose aggregated proteins by excitation of vibrational bands. In this study, we prepared hybrid materials of protein (human serum albumin; HSA) including several new Schiff base Zn(II) complexes incorporating amino acid (alanine and valine) or dipeptide (gly-gly) derivative moieties, which were synthesized and characterized with UV-vis, circular dichroism (CD), and IR spectra. Density functional theory (DFT) and time dependent DFT (TD-DFT) calculations were also performed to investigate vibrational modes of the Zn(II) complexes.