Dresden 2014 – scientific programme

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MA: Fachverband Magnetismus

MA 19: Poster I

MA 19.3: Poster

Tuesday, April 1, 2014, 13:00–15:30, P1

[Cu₂^II(NGuaS)₂Cl₂]: Antiferromagnetic coupling and optical response, a broken symmetry DFT analysis — •Matthias Witte, Uwe Gerstmann, Eva Rauls, and Wolf Gero Schmidt — University Paderborn, Germany

Copper enzymes are of utter importance for biochemical processes in nature. Their capability of hydroxylating phenols to catechols, for example, is essential for the tyrosinase process. Hence understanding their electronic structure and rationalizing their spectroscopic fingerprints are primary goals for theoretical chemistry. However the computation of their structural and electronic properties turns out to be quite challenging and typically smaller model systems are investigated showing similar functionalities. Gerald Henkel and co-workers succeeded in the previously unknown chloride-induced disulfide thiolate interconversion, leading from the copper(I) disulfide complex cation [Cu₂^I(NGuaS)₂]²⁺ to the electrically neutral copper(II) thiolate species [Cu₂^II(NGuaS)₂Cl₂]. [1] We analyse the electronic groundstate which is antiferromagnetically coupled by the use of density functional theory. We employ the B3LYP hybrid functional and an atom-centered cc-pVDZ basis set. The optical spectra are calculated using the TDDFT approach. In order to rationalize the antiferromagnetic coupled groundstate we analyze the electronic structure in detail and trace it to a more favorable Coulomb interaction.

[1] A. Neuba et al., A Halide-Induced Copper(I) Disulfide/Copper(II) Thiolate Interconversion, Angewandte Chemie International Edition, 51, 1714 (2012)