Energy transduction in the F1 motor of ATP synthase

@article{Wang1998EnergyTI,
  title={Energy transduction in the F1 motor of ATP synthase},
  author={Hongyun Wang and George F. Oster},
  journal={Nature},
  year={1998},
  volume={396},
  pages={279-282}
}
ATP synthase is the universal enzyme that manufactures ATP from ADP and phosphate by using the energy derived from a transmembrane protonmotive gradient. It can also reverse itself and hydrolyse ATP to pump protons against an electrochemical gradient. ATP synthase carries out both its synthetic and hydrolytic cycles by a rotary mechanism. This has been confirmed in the direction of hydrolysis, after isolation of the soluble F1 portion of the protein and visualization of the actual rotation of… 
Mechanically driven ATP synthesis by F1-ATPase
TLDR
Direct evidence for the chemical synthesis of ATP driven by mechanical energy is presented and shows that a vectorial force working at one particular point on a protein machine can influence a chemical reaction occurring in physically remote catalytic sites, driving the reaction far from equilibrium.
Energy Transduction by the Two Molecular Motors of the F1Fo ATP Synthase
TLDR
The F1Fo ATP synthase has nearly universal importance as the major source of ATP among all life forms and uses the non-equilibrium transmembrane electrochemical proton gradient derived from the oxidation of metabolites or light during photosynthesis to drive the reaction ADP + Pi + H2O away from equilibrium, and thereby maintains high cellular concentrations of ATP.
ATP Synthase : Two rotary molecular motors working together
TLDR
ATP synthase is the universal protein that terminates oxidative phosphorylation by synthesizing ATP from ADP and phosphate, and can be reversed in certain circumstances: ATP hydrolysis can drive the engine in reverse so that FATPase functions as a proton pump.
Thermodynamic efficiency and mechanochemical coupling of F1-ATPase
TLDR
It is found that the maximum work performed by F1-ATPase per 120° step is nearly equal to the thermodynamical maximum work that can be extracted from a single ATP hydrolysis under a broad range of conditions.
Mechanochemical Energy Transduction during the Main Rotary Step in the Synthesis Cycle of F1-ATPase.
TLDR
Extensive molecular dynamics simulations are used to reconcile recent single-molecule experiments with structural data and provide a consistent thermodynamic, kinetic and mechanistic description of the main rotary substep in the synthetic cycle of mammalian ATP synthase.
Structure of a bacterial ATP synthase
TLDR
The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex, and reveals the path of transmembrane proton translocation.
Structure of a bacterial ATP synthase
TLDR
The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex, and reveals the path of transmembrane proton translocation.
Reverse engineering a protein: the mechanochemistry of ATP synthase.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 40 REFERENCES
Energy transduction in ATP synthase
TLDR
It is shown that biased diffusion, augmented by electrostatic forces, does indeed generate sufficient torque to account for ATP production and the motor's reversibility — supplying torque from ATP hydrolysis in F1 converts the motor into an efficient proton pump — can be explained by the model.
Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine.
TLDR
Structural information has provided important hints as to how these enzymes couple H+ transport to the chemical work of ATP synthesis, and the torque of such movement is proposed to cause the rotation of gamma within the alpha 3 beta 3 complex.
Direct observation of the rotation of F1-ATPase
TLDR
It is shown that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion by attaching a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly.
Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1
TLDR
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.
Proton slip of the chloroplast ATPase: its nucleotide dependence, energetic threshold, and relation to an alternating site mechanism of catalysis.
TLDR
The ADP-induced transition between different conduction states of the ATPase is interpreted as a consequence of the alternating site mechanism of catalysis, which clutches proton flow to some (conformational) change that can be executed after the binding of another ADP/P(i) couple to a second site.
Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis.
TLDR
It is found that the gammaM23K mutation prevents the proper utilization of binding energy to drive catalysis and blocks the enzyme in a Pi release mode, consistent with the use of energy from DeltamuH+ for increasing the affinity for Pi so that the substrate binds in a catalytically competent manner for synthesis of ATP.
Rotation of the γ Subunit in F1-ATPase; Evidence That ATP Synthase Is a Rotary Motor Enzyme
ATP-dependent, azide-sensitive rotation of the γ subunit relative to the α3β3 hexagonal ring of ATP synthase was observed with a single molecule imaging system. Thus, ATP synthase is a rotary motor
Rotation of the gamma subunit in F1-ATPase; evidence that ATP synthase is a rotary motor enzyme.
ATP-dependent, azide-sensitive rotation of the gamma subunit relative to the alpha3beta3 hexagonal ring of ATP synthase was observed with a single molecule imaging system. Thus, ATP synthase is a
...
1
2
3
4
...