A new copper(II) coordination polymer was synthesized from the l-isoleucine-Schiff base and characterized by elemental analysis, Fourier transform infrared (FT-IR) spectroscopy, ultraviolet-visible (UV-vis) spectroscopy, single-crystal X-ray diffraction (XRD) analysis, electronic paramagnetic resonance, and thermogravimetric analysis. XRD analysis confirmed the square planar coordination geometry of metallic centers and a zipper-like polymer structure. Vibrational, electronic, and paramagnetic spectroscopies and thermal analysis were consistent with the crystal structure. A Hirshfeld surface (HS) and density functional theory (DFT) analyses were employed to gain additional insight into interactions responsible for complex packing. The quantitative examination of two-dimensional (2D) fingerprint plots revealed, among other van der Waals forces, the dominating participation of H···H and H···Cl interactions in the molecular packing. The use of computational methods provided great help in detailing the supramolecular interactions occurring in the crystal, which were mainly van der Waals attractions. The electronic transition analysis helped corroborate the electronic transitions observed experimentally in the absorption spectrum. The frequency and vibrational mode analysis gave a deeper insight into the characterization of the CuL_CL complex.

With the objective of studying the conformational and macrocyclic effects of selected metal chelates on their peroxidase activities, Cu²⁺ and Fe³⁺ complexes were synthesized with a macrocyclic derivative of ethylenediaminetetraacetic acid and o-phenylenediamine (abbreviated as edtaodH₂) and its new open-chain analogue (edtabzH₂). The Fe³⁺ complex of edtaodH₂ has a peroxidase-like activity, whereas the complex of edtabzH₂ does not. The X-ray study of the former shows the formation of a dimeric molecule {[Fe(edtaod)]₂O} in which each metal with an octahedral coordination is overposed over the macrocyclic cavity, as a result of rigid macrocyclic frame, to form an Fe–O–Fe bridge; the exposure of the central metal to the environment facilitates the capture of oxygen to drive the biomimetic activity. The peroxidase-inactive Fe³⁺ complex consists of a mononuclear complex ion [Fe(edtabz)(H₂O)]⁺, the metal ion of which is suited in a distorted pentagonal bipyramid to be protected from environmental oxygen. The copper(II) complexes, which have mononuclear structures with high thermodynamic stability compared with the iron(III) complexes, show no peroxidase activity. The steric effects play a fundamental role in the biomimetic activity.

In this study, we report the synthesis and comprehensive characterization of a novel binuclear copper(II) complex (LCu) featuring a Schiff base ligand derived from glycine. The complex was synthesized through a one-pot method and characterized using various techniques, including single-crystal X-ray diffraction (SCXRD), FTIR spectroscopy, thermal analysis, UV-Vis spectroscopy, and electron paramagnetic resonance (EPR). SCXRD analysis revealed a distinctive dimeric structure, with each copper center displaying a slightly distorted square pyramidal geometry. Spectroscopic techniques (FTIR, UV-Vis, EPR) corroborated the coordination environment of the copper ions. Computational studies, including non-covalent interaction (NCI) analysis and time-dependent density functional theory (TD-DFT) calculations, provided further insights into the electronic structure and stability of the complex. Catalytic tests of LCu were conducted in two key reactions: olefin cyclopropanation and C–S cross-coupling. The cyclopropanation reaction showed high yields, outstanding chemoselectivity, and exceptional trans diastereoselectivity, with a trans/cis ratio exceeding 1000 : 1. The C–S cross-coupling reaction also exhibited high conversion rates (over 93%) and yields (above 92%). These findings underscore the efficiency and versatility of LCu as a catalyst, with potential applications in sustainable synthetic processes.

Glutathione S-transferases are a family of detoxifying enzymes that catalyze the conjugation of reduced glutathione (GSH) with different xenobiotic compounds using either Ser, Tyr, or Cys as a primary catalytic residue. We identified a novel GST in the genome of the shrimp pathogen V. parahaemolyticus FIM- S1708⁺, a bacterial strain associated with Acute Hepatopancreatic Necrosis Disease (AHPND)/Early Mortality Syndrome (EMS) in cultured shrimp. This new GST class was named Gtt2. It has an atypical catalytic mechanism in which a water molecule instead of Ser, Tyr, or Cys activates the sulfhydryl group of GSH. The biochemical properties of Gtt2 from Vibrio parahaemolyticus (VpGSTT2) were characterized using kinetic and crystallographic methods. Recombinant VpGSTT2 was enzymatically active using GSH and CDNB as substrates, with a specific activity of 5.7 units/mg. Low affinity for substrates was demonstrated using both Michaelis–Menten kinetics and isothermal titration calorimetry. The crystal structure showed a canonical two-domain structure comprising a glutathione binding G-domain and a hydrophobic ligand H domain. A water molecule was hydrogen-bonded to residues Thr9 and Ser 11, as reported for the yeast Gtt2, suggesting a primary role in the reaction. Molecular docking showed that GSH could bind at the G-site in the vicinity of Ser11. G-site mutationsT9A and S11A were analyzed. S11A retained 30% activity, while T9A/S11A showed no detectable activity. VpGSTT2 was the first bacterial Gtt2 characterized, in which residues Ser11 and Thr9 coordinated a water molecule as part of a catalytic mechanism that was characteristic of yeast GTT2. The GTT2 family has been shown to provide protection against metal toxicity; in some cases, excess heavy metals appear in shrimp ponds presenting AHPND/EMS. Further studies may address whether GTT2 in V. parahaemolyticus pathogenic strains may provide a competitive advantage as a novel detoxification mechanism.