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P. Weinberger, R. Schamschule, A. Parusel, G. Köhler, W. Linert:
"Enzyme-mimetic model compounds: conformational analysis and far-IR study of Cu(TAAB)²⁺";
Journal of Inorganic Biochemistry, 79 (2000), 53 - 57.

Many enzymes occurring in nature like superoxide dismutase are systems rather too big to be accessible for vibrational and quantum chemical 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 superoxide dismutase-mimetic complex Cu(TTAB)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-IR 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.

conformational analysis; Cu[TAAB]²⁺; far-infrared; normal-coordinate analysis; semi-empirical calculations

http://publik.tuwien.ac.at/files/PubDat_212379.pdf