Mechanistic basis for differential inhibition of the F1Fo-ATPase by aurovertin.

@article{Johnson2009MechanisticBF,
  title={Mechanistic basis for differential inhibition of the F1Fo-ATPase by aurovertin.},
  author={Kathryn MS Johnson and Lara B. Swenson and Anthony Opipari and Rolf Reuter and Nawid Zarrabi and Carol A. Fierke and Michael B{\"o}rsch and Gary D Glick},
  journal={Biopolymers},
  year={2009},
  volume={91 10},
  pages={830-40}
}
The mitochondrial F(1)F(o)-ATPase performs the terminal step of oxidative phosphorylation. Small molecules that modulate this enzyme have been invaluable in helping decipher F(1)F(o)-ATPase structure, function, and mechanism. Aurovertin is an antibiotic that binds to the beta subunits in the F(1) domain and inhibits F(1)F(o)-ATPase-catalyzed ATP synthesis in preference to ATP hydrolysis. Despite extensive study and the existence of crystallographic data, the molecular basis of the differential… CONTINUE READING

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