Muscle contraction and free energy transduction in biological systems.

Muscle contraction occurs when the actin and myosin filaments in muscle are driven past each other by a cyclic interaction of adenosine triphosphate (ATP) and actin with cross-bridges that extend from myosin. Current biochemical studies suggest that, during each adenosine triphosphatase cycle, the myosin cross-bridge alternates between two main conformations, which differ markedly in their strength of binding to actin and in their overall structure. Binding of ATP to the cross-bridge induces the weak-binding conformation, whereas inorganic phosphate release returns the cross-bridge to the strong-binding conformation. This cross-bridge cycle is similar to the kinetic cycle that drives active transport and illustrates the general principles of free energy transduction by adenosine triphosphatase systems.

[1]  S. Lowey,et al.  Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. , 1969, Journal of molecular biology.

[2]  S. Ebashi,et al.  Calcium ion and muscle contraction. , 1968, Progress in biophysics and molecular biology.

[3]  R. Goody,et al.  Synthesis of ATP from ADP and inorganic phosphate at the myosin-subfragment 1 active site. , 1974, European journal of biochemistry.

[4]  E. Taylor,et al.  Transient state phosphate production in the hydrolysis of nucleoside triphosphates by myosin. , 1970, Biochemistry.

[5]  E. Eisenberg,et al.  Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[6]  E. Eisenberg,et al.  Mechanism of action of troponin . tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin. , 1981, The Journal of biological chemistry.

[7]  A. L. Vianna,et al.  Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum. , 1979, Annual review of biochemistry.

[8]  P. Wagner,et al.  Calcium-sensitive binding of heavy meromyosin to regulated actin requires light chain 2 and the head-tail junction. , 1983, Biochemistry.

[9]  E. Eisenberg,et al.  The relation of muscle biochemistry to muscle physiology. , 1980, Annual review of physiology.

[10]  T. L. Hill,et al.  Cross-bridge model of muscle contraction. Quantitative analysis. , 1980, Biophysical journal.

[11]  E. Eisenberg,et al.  Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[12]  E. Eisenberg,et al.  Mechanism of the actomyosin ATPase: effect of actin on the ATP hydrolysis step. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[13]  P. B. Chock,et al.  Interconvertible enzyme cascades in metabolic regulation. , 1978, Current topics in cellular regulation.

[14]  E. Eisenberg,et al.  Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[15]  A. Huxley,et al.  Proposed Mechanism of Force Generation in Striated Muscle , 1971, Nature.

[16]  P. Boyer,et al.  A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[17]  T. L. Hill.  A proposed common allosteric mechanism for active transport, muscle contraction, and ribosomal translocation. , 1969, Proceedings of the National Academy of Sciences of the United States of America.

[18]  D. Mornet,et al.  Structure of the actin–myosin interface , 1981, Nature.

[19]  Clive R. Bagshaw,et al.  The reversibility of adenosine triphosphate cleavage by myosin. , 1973, The Biochemical journal.

[20]  T. L. Hill,et al.  Reaction free energy surfaces in myosin-actin-ATP systems. , 1976, Biochemistry.

[21]  S. Rosenfeld,et al.  The ATPase mechanism of skeletal and smooth muscle acto-subfragment 1. , 1984, The Journal of biological chemistry.

[22]  W F Harrington,et al.  On the origin of the contractile force in skeletal muscle. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[23]  D. Parry,et al.  Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles. , 1973, Journal of molecular biology.

[24]  L. Franco,et al.  Purification of the histone H1 from the fruit fly Ceratitis capitata , 1977, FEBS letters.

[25]  Steven B Marston,et al.  Coupling between the enzymatic site of myosin and the mechanical output of muscle. , 1979, Journal of molecular biology.

[26]  E. Eisenberg,et al.  The rate-limiting step in the actomyosin adenosinetriphosphatase cycle. , 1984, Biochemistry.

[27]  K. Holmes,et al.  Induced Changes in Orientation of the Cross-Bridges of Glycerinated Insect Flight Muscle , 1965, Nature.

[28]  S. Lowey,et al.  Substructure of the myosin molecule. IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actin. , 1973, Journal of molecular biology.

[29]  E. Eisenberg,et al.  The binding of heavy meromyosin to F-actin. , 1980, The Journal of biological chemistry.

[30]  E. Eisenberg,et al.  Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5'-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. , 1979, Biochemistry.

[31]  J. Eccleston,et al.  Elementary processes of the magnesium ion-dependent adenosine triphosphatase activity of heavy meromyosin. A transient kinetic approach to the study of kinases and adenosine triphosphatases and a colorimetric inorganic phosphate assay in situ. , 1972, The Biochemical journal.

[32]  E. Taylor,et al.  Mechanism of adenosine triphosphate hydrolysis by actomyosin. , 1971, Biochemistry.

[33]  J. Lowy,et al.  The structure of F-actin and of actin filaments isolated from muscle , 1963 .

[34]  B. Brenner,et al.  X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. , 1984, Biophysical journal.

[35]  P. B. Chock,et al.  Interconvertible enzyme cascades in cellular regulation. , 1980, Annual review of biochemistry.

[36]  G. Hammes.  Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[37]  E. Taylor,et al.  Studies on the kinetics of formation and dissociation of the actomyosin complex. , 1969, Biochemistry.

[38]  S Ebashi,et al.  Control of muscle contraction , 1969, Quarterly Reviews of Biophysics.

[39]  H E Huxley,et al.  The Mechanism of Muscular Contraction , 1965, Scientific American.

[40]  W. Jencks.  The utilization of binding energy in coupled vectorial processes. , 2006, Advances in enzymology and related areas of molecular biology.

[41]  Steven B Marston,et al.  The rates of formation and dissociation of actin-myosin complexes. Effects of solvent, temperature, nucleotide binding and head-head interactions. , 1982, The Biochemical journal.

[42]  P. Boyer,et al.  The reversal of the myosin and actomyosin ATPase reactions and the free energy of ATP binding to myosin. , 1974, Biochemical and biophysical research communications.

[43]  E. Eisenberg,et al.  Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. , 1982, The Journal of biological chemistry.

[44]  Y. Tonomura,et al.  The pre-steady state of the myosin-adenosine triphosphate system. II. Initial rapid absorption and liberation of hydrogen ion followed by a stopped-flow method. , 1965, Journal of biochemistry.

[45]  R. Goody,et al.  The binding constant of ATP to myosin S1 fragment. , 1977, European journal of biochemistry.

[46]  W. Stoeckenius,et al.  The purple membrane of salt-loving bacteria. , 1976, Scientific American.

[47]  Steven B Marston,et al.  Changes in muscle crossbridges when beta, gamma-imido-ATP binds to myosin. , 1976, Journal of molecular biology.

[48]  T. L. Hill,et al.  Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I. , 1974, Progress in biophysics and molecular biology.

[49]  Steven B Marston,et al.  The dissociation constant of the actin-heavy meromyosin subfragment-1 complex. , 1975, Biochemistry.

[50]  T. L. Hill,et al.  A cross-bridge model of muscle contraction. , 1978, Progress in biophysics and molecular biology.

[51]  H. Huxley,et al.  ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE. , 1963, Journal of molecular biology.

[52]  J. Sleep,et al.  Exchange between inorganic phosphate and adenosine 5'-triphosphate in the medium by actomyosin subfragment 1. , 1980, Biochemistry.

[53]  E. Eisenberg,et al.  The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation. , 1968, Biochemistry.

[54]  D. DeRosier,et al.  Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. , 1970, Journal of molecular biology.

[55]  B. Sykes,et al.  Energetics of the equilibrium between two nucleotide-free myosin subfragment 1 states using fluorine-19 nuclear magnetic resonance. , 1982, Biochemistry.