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  • Title: NH-S hydrogen bonding in zinc enzyme model complex with S2N2 binding set studied by normal coordinate analysis of vibrational spectra.
    Author: Shi XF, Sun WY, Zhang L, Li CD.
    Journal: Spectrochim Acta A Mol Biomol Spectrosc; 2000 Feb 15; 56(3):603-13. PubMed ID: 10794475.
    Abstract:
    In order to provide theoretical evidence for the existence and effect of NH-S hydrogen bonding in the zinc enzyme model complex [Zn(S-2-C6H4NHCOC6H5)2(1-MeIm)2] (1-MeIm = 1-methylimidazole) in addition to the spectroscopic and crystallographic investigations, normal coordinate analysis (NCA) was carried out using a modified Urey-Bradley force field. The vibrational frequencies of the complex with and without the NH-S hydrogen bonding as well as the corresponding internal coordinates were obtained. The good agreement found between the calculated and observed frequencies in the presence of the NH-S hydrogen bond, supports the reliability of the analysis. The stretching force constant of the NH-S hydrogen bond obtained from the calculation is 0.18 mdyne per A. The calculation shows that the N-H bond is weakened by formation of the NH-S hydrogen bond. The results are indicative of the existence of the NH-S hydrogen bond in the complex.
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