43Ca and 67Zn NMR study of Ca2+, Zn2+-thermolysin complexes |
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Authors: | Toru Shimizu Masahiro Hatano |
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Affiliation: | Chemical Research Institute of Non-Aqueous Solutions Tohoku University, Kathira, Sendai 980 Japan |
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Abstract: | 43Ca NMR spectroscopy of Ca2+-thermolysin complexes reveals that the structure and/or exchange rate of Ca2+ bound to the regulative-site of the enzyme are not essentially changed by adding Zn2+ or an inhibitor, L-leucine hydroxamate, both of which may be bound to the active-site of the enzyme. It is shown that the chemical exchange mechanism dominates the 43Ca NMR of Ca2+ bound to the enzyme on the basis of temperature-dependences of the NMR. In contrast with the 43Ca NMR findings, first application of 67Zn NMR to the Zn2+-thermolysin complexes offers convincing evidences that the structure and/or exchange rate of Zn2+ bound to the active-site of the enzyme are remarkably changed by adding Ca2+ or the inhibitor, L-leucine hydroxamate. |
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