Molecular simulations

Characterization of metal-ligand complexation

Complex formation is one of the most important interactions between actinide and natural compounds. Various spectroscopic techniques are available to characterise their interactions, such as UV-Vis, FTIR, XRD, EXAFS, NMR, and TRLFS. To complement the experimental techniques, we use quantum chemical calculations such as Density Functional Theory (DFT) or Møller-Plesset Perturbation Theory (e.g. MP2) to reproduce the experimental results and to support the analysis of the spectra.

5f element chemistry

The presence of 5f electrons makes the unique character of actinide series yet the role of 5f electrons in the bonding between actinide and ligand is not fully elucidated. Sophisticated quantum chemical calculations are used to understand more about the chemical bonds in actinide complexes at various levels such as quantum theory of atoms in molecules (QTAIM).

Photochemistry and luminescence

The photochemistry of uranium(VI) has not only attracted the interest of chemists and physicists. Uranium glass was once a popular household item in Europe and its use dates back to 79 AD in the Roman Empire. Uranyl(VI) photochemistry forms the basis for the detection of uranium(VI) and the determination of its speciation by laser-induced luminescence spectroscopy. We study the photoreduction and photoinduced luminescence of uranium(VI) using time-dependent density functional theory (TD-DFT) and complete active space self consistent field (CASSCF) calculations.

Actinide/lanthanide binding with protein

We study the interactions of lanthanides (Ln3+) and actinides (An³⁺, An⁴⁺, AnO₂²⁺) with peptides and proteins of various sizes, from short peptides (~10 amino acids) to complete proteins such as calmodulin, transferrin, ferritin and albumin. Their interactions could be either specific or non-specific, as revealed by classical molecular dynamics (MD) simulations using 12-6 and/or 12-6-4 Lennard-Jones parameters on metals. We also use fragment molecular orbital (FMO) methods to study the interactions with metal and amino acid residues.