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Enzyme (Fi)

synthase (derived from PDB ID 1 BMF). The a subunit is shown in green, 3 in gray. The positively charged residues 3-Arg182 and a-Arg376 coordinate two oxygens of the pentavalent phosphate intermediate; 3-Lys155 interacts with a third oxygen, and the Mg2+ ion (green sphere) further stabilizes the intermediate. The blue sphere represents the leaving group (H2O). These interactions result in the ready equilibration of ATP and ADP + p, in the active site.

FIGURE 19-21 Catalytic mechanism of F1. (a) 18O-exchange experiment. Fi solubilized from mitochondrial membranes is incubated with ATP in the presence of 18O-labeled water. At intervals, a sample of the solution is withdrawn and analyzed for the incorporation of 18O into the P| produced from ATP hydrolysis. In minutes, the P| contains three or four 18O atoms, indicating that both ATP hydrolysis and ATP synthesis have occurred several times during the incubation. (b) The likely transition state complex for ATP hydrolysis and synthesis in ATP

synthase (derived from PDB ID 1 BMF). The a subunit is shown in green, 3 in gray. The positively charged residues 3-Arg182 and a-Arg376 coordinate two oxygens of the pentavalent phosphate intermediate; 3-Lys155 interacts with a third oxygen, and the Mg2+ ion (green sphere) further stabilizes the intermediate. The blue sphere represents the leaving group (H2O). These interactions result in the ready equilibration of ATP and ADP + p, in the active site.

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