ATP Synthase: The machine that makes ATP

@article{Pedersen1994ATPST,
  title={ATP Synthase: The machine that makes ATP},
  author={Peter L. Pedersen},
  journal={Current Biology},
  year={1994},
  volume={4},
  pages={1138-1141}
}
  • P. Pedersen
  • Published 1 December 1994
  • Chemistry
  • Current Biology
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References

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Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
TLDR
The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
Crystallization of F1-ATPase from bovine heart mitochondria.
Crystals of the F1-ATPase sector of the ATP synthase complex from bovine heart mitochondria have been grown from solutions containing polyethylene glycol 6000. The crystals diffract to 2.9 A
H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function
TLDR
A unique class of suppressor mutations identify a transmembrane helix of subunita that is proposed to interact with the bihelical unit of subunitc during proton transport and the role of multiple units of sub unitc in coupling proton translocation to ATP synthesis is considered.
Escherichia coli ATP synthase (F-ATPase): catalytic site and regulation of H+ translocation.
TLDR
Recent results on the Escherichia coli F-ATPase, in particular its catalytic site in the beta subunit and regulation of H+ transport by the gamma subunit are discussed, which suggests that this subunit has an essential role in coupling catalysis with proton translocation.
Functional sites in F1-ATPases: Location and interactions
TLDR
This review focuses on the location and interaction of three functional sites in F1-ATPases, which are catalytic sites, noncatalytic nucleotide-binding sites, and a site that binds inhibitory amphipathic cations which is at an interface of α and β subunits.
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