Adiabatic compressibility of myoglobin. Effect of axial ligand and denaturation.

An ultrasonic technique has been employed to study the adiabatic compressibility of three metmyoglobin derivatives (aquomet-, fluoromet- and azidometmyoglobin) at neutral pH, and aquometmyoglobin as a function of pH in the frequency range of 1-10 MHz at 20 degrees C. No difference was observed in the adiabatic compressibility of the various derivatives. This indicates that the binding of different axial ligands to myoglobin does not affect significantly the conformational fluctuations of the protein. The finding is consistent with the results of the hydrogen exchange rate experiment, indicating that both types of measurements are useful for the study of protein dynamics. Upon acid-induced denaturation, the adiabatic compressibility of myoglobin drops from 5.3 X 10(-12) cm2/dyn to 0.5 X 10(-12) cm2/dyn. Plausible reasons for such a decrease are discussed.