NMR studies of the interaction between Bacillis subtilis neutral proteinase and inorganic metal compounds

The interaction between Bacillis subtilis neutral proteinase (B.S.NP) and inorganic metal compounds (CoCl2, NiCl2) was investigated by H-1 NMR spectroscopy. It has been shown that the Zn(II) ion in the active center of the native enzyme may directly interact with external CoCl2 and NiC2, producing Co(II)- and Ni(II)-substituted derivatives, and their H-1 NMR spectra were obtained for the first time. From the H-1 NMR spectra, the coordinated structure of the active center in the native enzyme was described