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 i norganic metal compounds (CoCl2, NiCl2) was investigated by H-1 NMR spectro scopy. It has been shown that the Zn(II) ion in the active center of the na tive enzyme may directly interact with external CoCl2 and NiC2, producing C o(II)- and Ni(II)-substituted derivatives, and their H-1 NMR spectra were o btained for the first time. From the H-1 NMR spectra, the coordinated struc ture of the active center in the native enzyme was described.