The ATP synthase--a splendid molecular machine.

  title={The ATP synthase--a splendid molecular machine.},
  author={Paul D. Boyer},
  journal={Annual review of biochemistry},
  • 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… 
Rotational coupling in the F0F1 ATP synthase.
Kinetic and biochemical evidence is consistent with the expected equal participation of the three catalytic sites in the alpha 3 beta 3 hexamer, which operate in sequential, cooperative reaction pathways.
The rotary mechanism of the ATP synthase.
Evolutionary modifications of molecular structure of ATP-synthase γ-subunit
  • S. Ponomarenko
  • Biology
    Journal of Evolutionary Biochemistry and Physiology
  • 2007
It is suggested that elongation of the γ-subunit globular part had resulted from the atpC intragene duplication in the process of adaptive evolution and the evolved fragment participates in light regulation of the chloroplast ATP-synthase.
Molecular architecture of the rotary motor in ATP synthase.
An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits whose extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
Studies of the C-terminal Region of the Gamma Subunit of the Chloroplast ATP Synthase
This work has shown that the structure and function of the F1 Enzyme and the structure of the ATP Synthase are determined by the H2O2/O2 mixture, which is a mixture of the following: H2CO3, H3O2, and O2.
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
The crystal structure of the ATP synthase catalytic complex (F1) from Escherichia coli described here reveals the structural basis for autoinhibition by one of its rotary stalk subunits, and adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme.
The rotary mechanism of ATP synthase.
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.
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.


Kinetic studies of ATP synthase: The case for the positional change mechanism
This review summarizes recent isotopic and kinetic evidence in favour of the concept, originally proposed by Boyer and coworkers, that energy from the proton gradient is exerted not directly for the reaction at the catalytic site, but rather to release product from a single catalysttic site.
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
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.
Rotation of subunits during catalysis by Escherichia coli F1-ATPase.
The results demonstrate that gamma subunit rotates relative to the beta subunits during catalysis, and similar reactivities of unlabeled and radiolabeled beta sub units with gamma C87 upon reoxidation.
Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1
It is concluded that the γ subunit of F1 rotates relative to the surrounding catalytic subunits during catalytic turnover by both soluble F1 and membrane-bound F0F1.
Electron microscopy of the F1F0 ATP synthase: From structure to function
  • E. Gogol
  • Biology, Chemistry
    Microscopy research and technique
  • 1994
Electron microscopy has provided most of the available structural information on the F1F0, and recent applications of cryo‐electron microscopeopy have captured different functionally relevant configurations which may finally address longstanding questions about subunit rearrangement during the catalytic cycle.
Intersubunit rotation in active F-ATPase
An intersubunit rotation in real time in the functional enzyme F-ATPase is recorded by applying polarized absorption relaxation after photobleaching to immobilized F1 with eosin-labelled γ in a timespan of 100 ms, compatible with the rate of ATP hydrolysis by immobilization F1.
Conformational transmission in ATP synthase during catalysis: Search for large structural changes
  • M. Futai, H. Omote
  • Biology, Chemistry
    Journal of bioenergetics and biomembranes
  • 1996
The results suggest that the dynamic conformation change and its transmission are essential for ATP synthase.
A mutation altering the kinetic responses of the yeast mitochondrial F1-ATPase.
  • D. Mueller
  • Biology
    The Journal of biological chemistry
  • 1989
A single amino acid replacement of Thr197 to Ser197 resulted in a 3-fold increase in the specific activity of the enzyme, eliminated the stimulatory effects of oxyanions, and modulated the effects of the inhibitor NaN3 while having little effect on the uni-site ATPase.