Abstract
The dependence of the magnetic relaxation rates of1H and19F on temperature, frequency, pH and N -3 concentration, were measured in solutions of Manganese-containing superoxide dismutase ofBacillus stearothermophilus, and were compared to activity measurements, in order to obtain some information on the structure and dynamics at Mn(III) present in the active site of the enzyme. The experimental data lead us to hypothesize the presence of two binding sites in the coordination sphere of the enzyme bound Mn(III), which are accessible to water and anions and have different chemical and spectroscopic properties. NMR measurements carried out in the presence of competitive inhibitors and the pH dependence of both NMR relaxation rates suggest that F-, N -3 and OH- ions bind to one site, while a water molecule binds to the other one. The stability constant values of the complexes between these anions and the enzyme are reported. The influence of the anions on activity and the pH dependence of NMR parameters are discussed.
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Abbreviations
- MnSOD:
-
Manganese containing superoxide dismutase
References
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Viglino, P., Orsega, E.F., Argese, E. et al. The active site of Manganese-containing superoxide dismutase fromBacillus stearothermophilus studied by1H and19F magnetic relaxation. Eur Biophys J 15, 225–230 (1987). https://doi.org/10.1007/BF00577070
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DOI: https://doi.org/10.1007/BF00577070