ATP synthase — a marvellous rotary engine of the cell

  title={ATP synthase — a marvellous rotary engine of the cell},
  author={Masasuke Yoshida and Eiro Muneyuki and Toru Hisabori},
  journal={Nature Reviews Molecular Cell Biology},
ATP synthase can be thought of as a complex of two motors — the ATP-driven F1 motor and the proton-driven Fo motor — that rotate in opposite directions. The mechanisms by which rotation and catalysis are coupled in the working enzyme are now being unravelled on a molecular scale. 

The rotary mechanism of the ATP synthase.

Chemo-Mechanical Coupling in the Rotary Molecular Motor F1-ATPase

F1-ATPase is a molecular motor in which the central γ subunit rotates inside the cylinder made of α3β3 subunits that is coupled to the chemical reactions in the three catalytic sites: binding/release of ATP, ADP, and phosphate, and hydrolysis/synthesis of ATP.

ATP synthesis in an ancient ATP synthase at low driving forces.

  • Dennis LittyV. Müller
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2022
By purification and reconstitution of an ATP synthase with a V-type c subunit, it is unequivocally demonstrated, against expectations, the capability of such an enzyme to synthesize ATP at physiological relevant driving forces of 90 to 150 mV.

Rotary catalysis of FoF1-ATP synthase

The novel experimental setup to reproduce the proton motive force in vitro is developed and succeeded in directly observing theProton-driven rotation of FoF1 is observed.

A New Type of Na+-Driven ATP Synthase Membrane Rotor with a Two-Carboxylate Ion-Coupling Motif

Multi-disciplinary methods reveal a novel type of ion binding in the rotor ring of the F1Fo-ATP synthase from the opportunistic pathogen Fusobacterium nucleatum.

F(1)-ATPase: a prototypical rotary molecular motor.

  • K. Kinosita
  • Chemistry, Biology
    Advances in experimental medicine and biology
  • 2012
F(1)-ATPase, the soluble portion of ATP synthase, has been shown to be a rotary molecular motor in which the central γ subunit rotates inside the cylinder made of α(3)β(3) subunits. The rotation is

Rotation of F1-ATPase: how an ATP-driven molecular machine may work.

A toy model of F1-ATPase is introduced and its free-energy diagrams discussed to possibly answer two related questions, How is free energy obtained by ATP hydrolysis converted to the mechanical work of rotation, and how is mechanical work done on F1 converted to free energy to produce ATP.

Inhibitors of the catalytic domain of mitochondrial ATP synthase.

The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states and four independent inhibitory sites have been identified by high-resolution structural studies.



ATP synthase: an electrochemical transducer with rotatory mechanics.

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.

Structural biology: Proton-powered turbine of a plant motor

This work has imaged the ATP synthase from leaf chloroplasts by using atomic force microscopy and, surprisingly, finds that its turbine has 14 subunits, arranged in a cylindrical ring.

The ATP synthase--a splendid molecular machine.

  • P. Boyer
  • Chemistry
    Annual review of biochemistry
  • 1997
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

Bacterial Na+‐ATP synthase has an undecameric rotor

The rotor stoichiometry of Ilyobacter tartaricus ATP synthase is determined by atomic force microscopy and cryo‐electron microscopy, and shows the cylindrical sodium‐driven rotor to comprise 11 c‐subunits.

Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation.

C coupled rotation may be essential for energy coupling between proton transport through F0 and ATP hydrolysis or synthesis in F1, found in mitochondria or bacterial membranes.

Structure of the γ–ɛ complex of ATP synthase

ATP synthases (F1Fo-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency.

Why Is the Mechanical Efficiency of F1-ATPase So High?

The experimentally measured mechanical efficiency of the F1-ATPase under viscous loading is nearly 100%, far higher than any other hydrolysis-driven molecular motor (Yasuda et al., 1998). Here we

Direct observation of the rotation of F1-ATPase

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.