ATP Hydrolysis in the B^sub TP^ and B^sub DP^ Catalytic Sites of F^sub 1^-ATPase

ABSTRACT

The enzyme F^sub 1^-adenosine triphosphatase (ATPase) is a molecular motor that converts the chemical energy stored in the molecule adenosine triphosphate (ATP) into mechanical rotation of its γ-subunit. During steady-state catalysis, the three catalytic sites of F^sub 1^ operate in a cooperative fashion such that at every instant each site is in a different conformation corresponding to a different stage along the catalytic cycle. Notwithstanding a large amount of biochemical and, recently, structural data, we still lack an understanding of how ATP hydrolysis in F^sub 1^ is coupled to mechanical motion and how the catalytic sites achieve cooperativity during rotatory …