Mg2+ inhibits formation of 4Ca(2+)-calmodulin-enzyme complex at lower Ca2+ concentration. 1H and 113Cd NMR studies.

Our previous 1H NMR studies indicated that when mastoparan (MP) is added to Ca(2+)-half-saturated calmodulin (2Ca(2+)-CaM) in the absence of Mg2+ ions, Ca2+ ions transfer from the C-terminal-half domain of CaM not interacting with MP to the N-terminal-half domain of CaM interacting with MP at lower MP concentrations (Ohki, S., Yazawa, M., Yagi, K., and Hikichi, K. (1991b) J. Biochem. (Tokyo) 110, 737-742). As a consequence, the active form of 4Ca(2+)-CaM.MP complex is formed. In the present study, we studied the effect of Mg2+ ions on Ca2+ transfer. In the presence of Mg2+ ions, such Ca2+ transfer does not occur. The effects of Mg2+ ions are also studied by observing 113Cd NMR in the presence of M13, the 26-residue peptide of the CaM-binding region of myosin light chain kinase. The 113Cd NMR results show that Mg2+ ions prevent to form the active complex. Mg2+ plays an important role as an inactivating factor to CaM.