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P. Weinberger, R. Schamschule, W. Linert:
"Conformational analysis and far IR study of the enzyme-mimetic model compound Cu(TAAB)²⁺";
Poster: First International Conference: "Metals and Brain" - From Neurochemistry to Neurodegeneration, Padua, Italien; 20.09.2000 - 23.09.2000; in: "Scientific program/abstracts", (2000), S. 115.

Many enzymes occurring in nature like the superoxide dismutase are systems rather too big to be accessible for vibrational and quantumchemical investigations. Thus, enzyme-mimetic model compounds consisting of a biological active metal center surrounded by a macrocyclic ligand are used to shed light on binding properties of the active metal center. Far and mid-range IR spectroscopic investigations and a conformational analysis with the semi-empirical ZINDO/1 method of the superoxide dismutase-mimetic complex Cu[TAAB]²⁺ are performed (TAAB = [b,f,j,n][1,5,9,13]tetra-aza-cyclohexadecine (tetra-anhydroamino benzaldehyde)). A distorted tetrahedral copper(II) center with slightly twisted phenyl subunits is determined as the most stable conformation. Calculated mid and far infrared spectra are in good agreement with the experimental data and confirm the proposed structure. A harmonic normal-coordinate analysis is used to assign the vibrational modes of the observed spectra.