The ATP synthase--a splendid molecular machine.

@article{Boyer1997TheAS,
  title={The ATP synthase--a splendid molecular machine.},
  author={Paul D. Boyer},
  journal={Annual review of biochemistry},
  year={1997},
  volume={66},
  pages={
          717-49
        }
}
  • P. Boyer
  • Published 1997
  • Chemistry
  • Annual review of biochemistry
An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanism with an internal rotation of the gamma subunit. Other structural and mutational probes of the F1 and F0 portions of the ATP synthase are reviewed, together with kinetic and other evaluations of catalytic site occupancy and behavior during hydrolysis or synthesis of ATP. Subunit function as related to… 
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TLDR
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TLDR
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TLDR
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ROTATIONAL COUPLING IN THE F 0 F 1 ATP SYNTHASE
The F0F1 ATP synthase is a large multisubunit complex that couples translocation of protons down an electrochemical gradient to the synthesis of ATP. Recent advances in structural analyses have led
Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation
TLDR
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The rotary mechanism of ATP synthase.
TLDR
Significant progress has been made towards establishing the complete structure of ATP synthase and revealing its mechanism, and direct microscopic observation of rotation has been extended to F(1)-ATPase and F( 1)F(o)-atPase complexes.
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.
TLDR
In the structure of the rat liver F1-ATPase, determined to 2.8-A resolution in the presence of physiological concentrations of nucleotides, all three beta subunits contain bound nucleotide and adopt similar conformations, which suggests a mechanism of ATP synthesis/hydrolysis in which configurations of the enzyme with three bound nucleotide play an essential role.
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References

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TLDR
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