Kinetic characterization of the acid-alkaline transition in Dolabella auricularia ferric myoglobin using 1H-NMR saturation transfer experiments.

The acid-alkaline transition in ferric myoglobin of the mollusc, Dolabella auricularia, exerts the changes in both the coordination and spin states of the heme iron. Slower transition rate, compared to the NMR time scale, in this myoglobin allowed the observation of separate signals arising from the two forms, and pH titration yielded a pK value of 7.8. 1H-NMR saturation transfer experiments have been successfully used not only to provide the first signal assignments for the heme methyl proton resonances of the Met-hydroxyl form of the myoglobin, but also to determine the kinetics of the transition.