Myosin is an enzyme, utilizing ATP to produce conformational change, leading to force generation. Kinetics of myosin reverse recovery stroke depends on metal ion, complexed with ATP, the recovery stroke is slow for MgATP and fast for MnATP. Metal ion coordinates gamma phosphate of ATP in myosin active site, the recovery stroke correlates with release of abstracted phosphate, therefore magnesium “holds” phosphate tighter than manganese. Magnesium and manganese are similar ions in terms of their chemical properties and inner and outer shell complexation, hence we propose to use these ions to study the mechanism of phosphate release. Analysis of octahedral complexes of magnesium and manganese shows that the partial charge on magnesium is higher than on manganese, that makes magnesium a “hard”, difficult to polarize ion. We hypothesize that electrostatic interactions play a role in keeping and releasing abstracted gamma phosphate in the active site, stronger electric charge of magnesium ion holds gamma phosphate tighter. We used stable myosin-nucleotide analog complex (ADP-vanadate) and Raman spectroscopy to examine effect of metal ion on the frequency of Raman light scattering by vanadium ion, which replaces gamma phosphate in myosin active site. We obtained metal-dependent spectra of Raman light scattering, and interpreted the data in terms of interatomic distance between vanadium and its equatorial oxygen, coordinated by metal ion. Previous studies show that in vanadate's trigonal bipyramidal complex the length of equatorial and apical bonds are directly correlated; increased length of equatorial bond implies increased length of apical bond, which is formed with oxygen of ADP's beta phosphate. We conclude that the charge of metal ion, complexed with a nucleotide, plays an essential role in the process of phosphate release by myosin during ATPase activity.