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Molecular dynamics trajectories for the bovine mitochondrial F 1 -ATPase are used to demonstrate the motions and interactions that take place during the elementary (120 o rotation) step of the γ subunit. The results show how rotation of the γ subunit induces the observed structural changes in the catalytic β subunits. Both steric and electrostatic interactions contribute. An ''ionic track'' of Arg and Lys residues on the protruding portion of the γ subunit plays a role in guiding the motions of the β subunits. Experimental data for mutants of the DELSEED motif and the hinge region are interpreted on the basis of the molecular dynamics results. The trajectory provides a unified dynamic description of the coupled subunit motions involved in the 120 o rotation cycles of F 1 -ATPase.