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

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Chinese Science Bulletin

Abstract

The interaction betweenBacillis subtilis neutral proteinase (B.S.NP) and inorganic metal compounds (CoCl2, NiCl2) was investigated by1H 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 NiCl2, producing Co(II)- and Ni(II)-substituted derivatives, and their1H NMR spectra were obtained for the first time. From the1H NMR spectra, the coordinated structure of the active center in the native enzyme was described.

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Authors and Affiliations

  1. Department of Chemistry and Chemical Engineering, Dalian University, 116622, Dalian, China

    Xuefang Zheng

  2. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 116023, Dalian, China

    Jiehan Hu, Guobao Cheng & Hongwei Gai

  3. Experimental Centre of Liaoning Normal University, 116021, Dalian, China

    Yongting Xu

Authors
  1. Xuefang Zheng
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  2. Jiehan Hu
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  3. Yongting Xu
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  4. Guobao Cheng
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  5. Hongwei Gai
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Correspondence to Jiehan Hu.

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Zheng, X., Hu, J., Xu, Y. et al. NMR studies of the interaction betweenBacillis subtilis neutral proteinase and inorganic metal compounds. Chin.Sci.Bull. 45, 1764–1766 (2000). https://doi.org/10.1007/BF02886262

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  • DOI: https://doi.org/10.1007/BF02886262

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