F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps

A single molecule of F1-ATPase, a portion of ATP synthase, is by itself a rotary motor in which a central gamma subunit rotates against a surrounding cylinder made of alpha3beta3 subunits. Driven by three catalytic betas, each fueled with ATP, gamma makes discrete 120 degree steps, occasionally stepping backward. The work done in each step is constant over a broad range of imposed load and is close to the free energy of hydrolysis of one ATP molecule.

[1]  I. Sase,et al.  Real time imaging of single fluorophores on moving actin with an epifluorescence microscope. , 1995, Biophysical journal.

[2]  J. Gelles,et al.  Coupling of kinesin steps to ATP hydrolysis , 1997, Nature.

[3]  P. Mitchell.  Coupling of Phosphorylation to Electron and Hydrogen Transfer by a Chemi-Osmotic type of Mechanism , 1961, Nature.

[4]  V. V. Bulygin,et al.  Rotation of subunits during catalysis by Escherichia coli F1-ATPase. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[5]  P. Boyer.  The ATP synthase--a splendid molecular machine. , 1997, Annual review of biochemistry.

[6]  F. Oosawa,et al.  The loose coupling mechanism in molecular machines of living cells. , 1986, Advances in biophysics.

[7]  Jan Pieter Abrahams,et al.  Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria , 1994, Nature.

[8]  Masasuke Yoshida,et al.  A single mutation at the catalytic site of TF1‐α3β3γ complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity , 1997 .

[9]  T. Yanagida,et al.  Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[10]  E. Muneyuki,et al.  Steady state kinetics of proton translocation catalyzed by thermophilic F0F1-ATPase reconstituted in planar bilayer membranes. , 1989, The Journal of biological chemistry.

[11]  P. Boyer,et al.  Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase. , 1998, The Biochemical journal.

[12]  Analysis of time-dependent change of Escherichia coli F1-ATPase activity and its relationship with apparent negative cooperativity. , 1995, Biochimica et biophysica acta.

[13]  T. Hamamoto,et al.  Intramolecular rotation in ATP synthase: dynamic and crystallographic studies on thermophilic F1. , 1997, Biochemical and biophysical research communications.

[14]  R. Vale,et al.  The load dependence of kinesin's mechanical cycle. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[15]  J. Howard,et al.  The force exerted by a single kinesin molecule against a viscous load. , 1994, Biophysical journal.

[16]  Masasuke Yoshida,et al.  Catalytic Activity of the α3β3γ Complex of F1-ATPase without Noncatalytic Nucleotide Binding Site* , 1997, The Journal of Biological Chemistry.

[17]  V. V. Bulygin,et al.  ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits. , 1996, Biochimica et biophysica acta.

[18]  C. Grubmeyer,et al.  Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site. , 1982, The Journal of biological chemistry.

[19]  P. Boyer,et al.  Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model. , 1982, The Journal of biological chemistry.

[20]  R. Aggeler,et al.  Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex. , 1997, The Journal of biological chemistry.

[21]  E. Muneyuki,et al.  Kinetic analysis of proton translocation catalyzed by F0F1 ATPase , 1988, FEBS letters.

[22]  A. Huxley.  Muscle structure and theories of contraction. , 1957, Progress in biophysics and biophysical chemistry.

[23]  The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites. , 1995, Biochemistry.

[24]  W. Junge,et al.  ATP synthase: an electrochemical transducer with rotatory mechanics. , 1997, Trends in biochemical sciences.

[25]  Kazuhiko Kinosita,et al.  Rotation of the γ Subunit in F1-ATPase; Evidence That ATP Synthase Is a Rotary Motor Enzyme , 1997 .

[26]  R. L. Cross,et al.  Catalytic site occupancy during ATP hydrolysis by MF1-ATPase. Evidence for alternating high affinity sites during steady-state turnover. , 1988, The Journal of biological chemistry.

[27]  Kazuhiko Kinosita,et al.  Direct observation of the rotation of F1-ATPase , 1997, Nature.

[28]  H. Penefsky,et al.  Energetics of ATP Dissociation from the Mitochondrial ATPase during Oxidative Phosphorylation (*) , 1995, The Journal of Biological Chemistry.

[29]  W. Junge,et al.  Intersubunit rotation in active F-ATPase , 1996, Nature.

[30]  Kiwamu Saito,et al.  Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution , 1995, Nature.

[31]  I. Sase,et al.  Axial rotation of sliding actin filaments revealed by single-fluorophore imaging. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[32]  Howard C. Berg,et al.  The proton flux through the bacterial flagellar motor , 1987, Cell.

[33]  William D. McElroy,et al.  [1] Purification and properties of firefly luciferase , 1978 .

[34]  Kazuhiko Kinosita,et al.  F1-ATPase: A Rotary Motor Made of a Single Molecule , 1998, Cell.