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Figure 7.
FIGURE 7. Proposed critical events in the formation of ATP
catalyzed by the F[1] moiety of mitochondrial ATP synthase based
on structural work reported here, our earlier collaborative
structural studies (10), and our earlier biochemical studies
(15, 16). In the top, ADP and P[i] are both able to bind to the
catalytic F[1] moiety of rat liver ATP synthase in the absence
of Mg^2+ (10). In the middle, when Mg^2+ enters it binds to the
bound P[i], facilitating the formation of the transition state
(16). ADP and MgP[i] are then brought closer together, whereas
the methyl group of P-loop alanine 158 is brought into the
active site. The lower dielectric environment facilitates the
release of water as the ADP and MgP[i] are dehydrated to form
ATPMg (bottom).
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