Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 2001 Jan;80(1):379–397. doi: 10.1016/S0006-3495(01)76022-5

Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.

I Amitani 1, T Sakamoto 1, T Ando 1
PMCID: PMC1301241  PMID: 11159410

Abstract

We have attempted to link the solution actomyosin ATPase with the mechanical properties of in vitro actin filament sliding over heavy meromyosin. To accomplish this we perturbed the system by altering the substrate with various NTPs and divalent cations, and by altering ionic strength. A wide variety of enzymatic and mechanical measurements were made under very similar solution conditions. Excellent correlations between the mechanical and enzymatic quantities were revealed. Analysis of these correlations based on a force-balance model led us to two fundamental equations, which can be described approximately as follows: the maximum sliding velocity is proportional to square root of V(max)K(m)(A), where K(m)(A) is the actin concentration at which the substrate turnover rate is half of its maximum (V(max)). The active force generated by a cross-bridge under no external load or under a small external load is proportional to square root of V(max)/K(m)(A). The equations successfully accounted for the correlations observed in the present study and observations in other laboratories.

Full Text

The Full Text of this article is available as a PDF (186.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ando T. Fluorescence of fluorescein attached to myosin SH1 distinguishes the rigor state from the actin-myosin-nucleotide state. Biochemistry. 1984 Jan 17;23(2):375–381. doi: 10.1021/bi00297a029. [DOI] [PubMed] [Google Scholar]
  2. Arheden H., Arner A., Hellstrand P. Cross-bridge behaviour in skinned smooth muscle of the guinea-pig taenia coli at altered ionic strength. J Physiol. 1988 Sep;403:539–558. doi: 10.1113/jphysiol.1988.sp017263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Barman T., Brune M., Lionne C., Piroddi N., Poggesi C., Stehle R., Tesi C., Travers F., Webb M. R. ATPase and shortening rates in frog fast skeletal myofibrils by time-resolved measurements of protein-bound and free Pi. Biophys J. 1998 Jun;74(6):3120–3130. doi: 10.1016/S0006-3495(98)78018-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bell G. I. Models for the specific adhesion of cells to cells. Science. 1978 May 12;200(4342):618–627. doi: 10.1126/science.347575. [DOI] [PubMed] [Google Scholar]
  5. Bobkov A. A., Bobkova E. A., Lin S. H., Reisler E. The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head. Proc Natl Acad Sci U S A. 1996 Mar 19;93(6):2285–2289. doi: 10.1073/pnas.93.6.2285. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Borejdo J., Ando T., Burghardt T. P. The rate of MgADP binding to and dissociation from acto-S1. Biochim Biophys Acta. 1985 Apr 5;828(2):172–176. doi: 10.1016/0167-4838(85)90054-8. [DOI] [PubMed] [Google Scholar]
  7. Brune M., Hunter J. L., Corrie J. E., Webb M. R. Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry. 1994 Jul 12;33(27):8262–8271. doi: 10.1021/bi00193a013. [DOI] [PubMed] [Google Scholar]
  8. Bárány M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol. 1967 Jul;50(6 Suppl):197–218. doi: 10.1085/jgp.50.6.197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cook R. K., Root D., Miller C., Reisler E., Rubenstein P. A. Enhanced stimulation of myosin subfragment 1 ATPase activity by addition of negatively charged residues to the yeast actin NH2 terminus. J Biol Chem. 1993 Feb 5;268(4):2410–2415. [PubMed] [Google Scholar]
  10. Cooke R. Actomyosin interaction in striated muscle. Physiol Rev. 1997 Jul;77(3):671–697. doi: 10.1152/physrev.1997.77.3.671. [DOI] [PubMed] [Google Scholar]
  11. Cooke R., Bialek W. Contraction of glycerinated muscle fibers as a function of the ATP concentration. Biophys J. 1979 Nov;28(2):241–258. doi: 10.1016/S0006-3495(79)85174-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Cooke R. The actomyosin engine. FASEB J. 1995 May;9(8):636–642. doi: 10.1096/fasebj.9.8.7768355. [DOI] [PubMed] [Google Scholar]
  13. Crosbie R. H., Miller C., Cheung P., Goodnight T., Muhlrad A., Reisler E. Structural connectivity in actin: effect of C-terminal modifications on the properties of actin. Biophys J. 1994 Nov;67(5):1957–1964. doi: 10.1016/S0006-3495(94)80678-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Cuda G., Pate E., Cooke R., Sellers J. R. In vitro actin filament sliding velocities produced by mixtures of different types of myosin. Biophys J. 1997 Apr;72(4):1767–1779. doi: 10.1016/S0006-3495(97)78823-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Dantzig J. A., Goldman Y. E., Millar N. C., Lacktis J., Homsher E. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol. 1992;451:247–278. doi: 10.1113/jphysiol.1992.sp019163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. DiSanto M. E., Cox R. H., Wang Z., Chacko S. NH2-terminal-inserted myosin II heavy chain is expressed in smooth muscle of small muscular arteries. Am J Physiol. 1997 May;272(5 Pt 1):C1532–C1542. doi: 10.1152/ajpcell.1997.272.5.C1532. [DOI] [PubMed] [Google Scholar]
  17. Eccleston J. F., Trentham D. R. Magnesium ion dependent rabbit skeletal muscle myosin guanosine and thioguanosine triphosphatase mechanism and a novel guanosine diphosphatase reaction. Biochemistry. 1979 Jun 26;18(13):2896–2904. doi: 10.1021/bi00580a034. [DOI] [PubMed] [Google Scholar]
  18. Edman K. A., Reggiani C., Schiaffino S., te Kronnie G. Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres. J Physiol. 1988 Jan;395:679–694. doi: 10.1113/jphysiol.1988.sp016941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ferenczi M. A., Goldman Y. E., Simmons R. M. The dependence of force and shortening velocity on substrate concentration in skinned muscle fibres from Rana temporaria. J Physiol. 1984 May;350:519–543. doi: 10.1113/jphysiol.1984.sp015216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Galler S., Rathmayer W. Shortening velocity and force/pCa relationship in skinned crab muscle fibres of different types. Pflugers Arch. 1992 Feb;420(2):187–193. doi: 10.1007/BF00374989. [DOI] [PubMed] [Google Scholar]
  21. Goody R. S., Hofmann W. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides. J Muscle Res Cell Motil. 1980 Mar;1(1):101–115. doi: 10.1007/BF00711928. [DOI] [PubMed] [Google Scholar]
  22. Gulati J., Podolsky R. J. Isotonic contraction of skinned muscle fibers on a slow time base: effects of ionic strength and calcium. J Gen Physiol. 1981 Sep;78(3):233–257. doi: 10.1085/jgp.78.3.233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. HASSELBACH W. Die Wechselwirkung verschiedener Nukleosidtriphosphate mit Aktomyosin in Gelzustand. Biochim Biophys Acta. 1956 May;20(2):355–368. doi: 10.1016/0006-3002(56)90297-9. [DOI] [PubMed] [Google Scholar]
  24. HUXLEY A. F. Muscle structure and theories of contraction. Prog Biophys Biophys Chem. 1957;7:255–318. [PubMed] [Google Scholar]
  25. Haeberle J. R. Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in an in vitro motility assay. J Biol Chem. 1994 Apr 29;269(17):12424–12431. [PubMed] [Google Scholar]
  26. Harada Y., Noguchi A., Kishino A., Yanagida T. Sliding movement of single actin filaments on one-headed myosin filaments. Nature. 1987 Apr 23;326(6115):805–808. doi: 10.1038/326805a0. [DOI] [PubMed] [Google Scholar]
  27. He Z. H., Chillingworth R. K., Brune M., Corrie J. E., Trentham D. R., Webb M. R., Ferenczi M. A. ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay. J Physiol. 1997 May 15;501(Pt 1):125–148. doi: 10.1111/j.1469-7793.1997.125bo.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. He Z., Stienen G. J., Barends J. P., Ferenczi M. A. Rate of phosphate release after photoliberation of adenosine 5'-triphosphate in slow and fast skeletal muscle fibers. Biophys J. 1998 Nov;75(5):2389–2401. doi: 10.1016/s0006-3495(98)77683-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Helper D. J., Lash J. A., Hathaway D. R. Distribution of isoelectric variants of the 17,000-dalton myosin light chain in mammalian smooth muscle. J Biol Chem. 1988 Oct 25;263(30):15748–15753. [PubMed] [Google Scholar]
  30. Hibberd M. G., Trentham D. R. Relationships between chemical and mechanical events during muscular contraction. Annu Rev Biophys Biophys Chem. 1986;15:119–161. doi: 10.1146/annurev.bb.15.060186.001003. [DOI] [PubMed] [Google Scholar]
  31. Higashi-Fujime S., Hozumi T. The mechanism for mechanochemical energy transduction in actin-myosin interaction revealed by in vitro motility assay with ATP analogues. Biochem Biophys Res Commun. 1996 Apr 25;221(3):773–778. doi: 10.1006/bbrc.1996.0672. [DOI] [PubMed] [Google Scholar]
  32. Higashi-Fujime S. Reconstitution of active movement in vitro based on the actin-myosin interaction. Int Rev Cytol. 1991;125:95–138. doi: 10.1016/s0074-7696(08)61217-6. [DOI] [PubMed] [Google Scholar]
  33. Homsher E., Wang F., Sellers J. R. Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am J Physiol. 1992 Mar;262(3 Pt 1):C714–C723. doi: 10.1152/ajpcell.1992.262.3.C714. [DOI] [PubMed] [Google Scholar]
  34. Hozumi T., Miki M., Higashi-Fujime S. Maleimidobenzoyl actin: its biochemical properties and in vitro motility. J Biochem. 1996 Jan;119(1):151–156. doi: 10.1093/oxfordjournals.jbchem.a021200. [DOI] [PubMed] [Google Scholar]
  35. Ikebe M., Tonomura Y., Onishi H., Watanabe S. Elementary steps in the F-actin activated Mg2+-ATPase reaction of gizzard H-meromysin: effects of phosphorylation of the light-chain subunit. J Biochem. 1981 Jul;90(1):61–77. doi: 10.1093/oxfordjournals.jbchem.a133470. [DOI] [PubMed] [Google Scholar]
  36. Ishijima A., Doi T., Sakurada K., Yanagida T. Sub-piconewton force fluctuations of actomyosin in vitro. Nature. 1991 Jul 25;352(6333):301–306. doi: 10.1038/352301a0. [DOI] [PubMed] [Google Scholar]
  37. Ishijima A., Kojima H., Higuchi H., Harada Y., Funatsu T., Yanagida T. Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: unitary steps and forces. Biophys J. 1996 Jan;70(1):383–400. doi: 10.1016/S0006-3495(96)79582-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Johara M., Toyoshima Y. Y., Ishijima A., Kojima H., Yanagida T., Sutoh K. Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2127–2131. doi: 10.1073/pnas.90.6.2127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Kim E., Miller C. J., Reisler E. Polymerization and in vitro motility properties of yeast actin: a comparison with rabbit skeletal alpha-actin. Biochemistry. 1996 Dec 24;35(51):16566–16572. doi: 10.1021/bi9623892. [DOI] [PubMed] [Google Scholar]
  40. Kron S. J., Spudich J. A. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6272–6276. doi: 10.1073/pnas.83.17.6272. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Lowey S., Waller G. S., Trybus K. M. Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay. J Biol Chem. 1993 Sep 25;268(27):20414–20418. [PubMed] [Google Scholar]
  42. Lund J., Webb M. R., White D. C. Changes in the ATPase activity of insect fibrillar flight muscle during calcium and strain activation probed by phosphate-water oxygen exchange. J Biol Chem. 1987 Jun 25;262(18):8584–8590. [PubMed] [Google Scholar]
  43. Malmqvist U., Arner A. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Pflugers Arch. 1991 Jul;418(6):523–530. doi: 10.1007/BF00370566. [DOI] [PubMed] [Google Scholar]
  44. Mehta A. D., Finer J. T., Spudich J. A. Detection of single-molecule interactions using correlated thermal diffusion. Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7927–7931. doi: 10.1073/pnas.94.15.7927. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Miller C. J., Wong W. W., Bobkova E., Rubenstein P. A., Reisler E. Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry. 1996 Dec 24;35(51):16557–16565. doi: 10.1021/bi962388+. [DOI] [PubMed] [Google Scholar]
  46. Murphy C. T., Spudich J. A. Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates. Biochemistry. 1998 May 12;37(19):6738–6744. doi: 10.1021/bi972903j. [DOI] [PubMed] [Google Scholar]
  47. Nakajima H., Kunioka Y., Nakano K., Shimizu K., Seto M., Ando T. Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin. Biochem Biophys Res Commun. 1997 May 8;234(1):178–182. doi: 10.1006/bbrc.1997.6612. [DOI] [PubMed] [Google Scholar]
  48. Nishizaka T., Miyata H., Yoshikawa H., Ishiwata S., Kinosita K., Jr Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature. 1995 Sep 21;377(6546):251–254. doi: 10.1038/377251a0. [DOI] [PubMed] [Google Scholar]
  49. Okagaki T., Higashi-Fujime S., Ishikawa R., Takano-Ohmuro H., Kohama K. In vitro movement of actin filaments on gizzard smooth muscle myosin: requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon. J Biochem. 1991 Jun;109(6):858–866. doi: 10.1093/oxfordjournals.jbchem.a123471. [DOI] [PubMed] [Google Scholar]
  50. Pate E., Franks-Skiba K., White H., Cooke R. The use of differing nucleotides to investigate cross-bridge kinetics. J Biol Chem. 1993 May 15;268(14):10046–10053. [PubMed] [Google Scholar]
  51. Regnier M., Lee D. M., Homsher E. ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis. Biophys J. 1998 Jun;74(6):3044–3058. doi: 10.1016/S0006-3495(98)78012-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Rosenfeld S. S., Taylor E. W. The ATPase mechanism of skeletal and smooth muscle acto-subfragment 1. J Biol Chem. 1984 Oct 10;259(19):11908–11919. [PubMed] [Google Scholar]
  53. Rovner A. S., Freyzon Y., Trybus K. M. Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J Biol Chem. 1995 Dec 22;270(51):30260–30263. doi: 10.1074/jbc.270.51.30260. [DOI] [PubMed] [Google Scholar]
  54. Saito K., Aoki T., Aoki T., Yanagida T. Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. Biophys J. 1994 Mar;66(3 Pt 1):769–777. doi: 10.1016/s0006-3495(94)80853-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Schwyter D. H., Kron S. J., Toyoshima Y. Y., Spudich J. A., Reisler E. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J Cell Biol. 1990 Aug;111(2):465–470. doi: 10.1083/jcb.111.2.465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Sellers J. R., Eisenberg E., Adelstein R. S. The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation. J Biol Chem. 1982 Dec 10;257(23):13880–13883. [PubMed] [Google Scholar]
  57. Sheetz M. P., Chasan R., Spudich J. A. ATP-dependent movement of myosin in vitro: characterization of a quantitative assay. J Cell Biol. 1984 Nov;99(5):1867–1871. doi: 10.1083/jcb.99.5.1867. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Sheetz M. P., Spudich J. A. Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature. 1983 May 5;303(5912):31–35. doi: 10.1038/303031a0. [DOI] [PubMed] [Google Scholar]
  59. Shimizu T., Furusawa K., Ohashi S., Toyoshima Y. Y., Okuno M., Malik F., Vale R. D. Nucleotide specificity of the enzymatic and motile activities of dynein, kinesin, and heavy meromyosin. J Cell Biol. 1991 Mar;112(6):1189–1197. doi: 10.1083/jcb.112.6.1189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Siemankowski R. F., Wiseman M. O., White H. D. ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci U S A. 1985 Feb;82(3):658–662. doi: 10.1073/pnas.82.3.658. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Sleep J. A., Hutton R. L. Exchange between inorganic phosphate and adenosine 5'-triphosphate in the medium by actomyosin subfragment 1. Biochemistry. 1980 Apr 1;19(7):1276–1283. doi: 10.1021/bi00548a002. [DOI] [PubMed] [Google Scholar]
  62. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  63. Stein L. A., Chock P. B., Eisenberg E. The rate-limiting step in the actomyosin adenosinetriphosphatase cycle. Biochemistry. 1984 Mar 27;23(7):1555–1563. doi: 10.1021/bi00302a033. [DOI] [PubMed] [Google Scholar]
  64. Stein L. A., Schwarz R. P., Jr, Chock P. B., Eisenberg E. Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5'-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry. 1979 Sep 4;18(18):3895–3909. doi: 10.1021/bi00585a009. [DOI] [PubMed] [Google Scholar]
  65. Stone D. B., Prevost S. C. Characterization of modified myosin at low ionic strength. Enzymatic and spin-label studies. Biochemistry. 1973 Oct 9;12(21):4206–4211. doi: 10.1021/bi00745a026. [DOI] [PubMed] [Google Scholar]
  66. Sugiura S., Yamashita H., Serizawa T., Iizuka M., Shimmen T., Sugimoto T. Active movement of cardiac myosin on Characeae actin cables. Pflugers Arch. 1992 May;421(1):32–36. doi: 10.1007/BF00374730. [DOI] [PubMed] [Google Scholar]
  67. Sutoh K., Ando M., Sutoh K., Toyoshima Y. Y. Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N terminus. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7711–7714. doi: 10.1073/pnas.88.17.7711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Takiguchi K., Hayashi H., Kurimoto E., Higashi-Fujime S. In vitro motility of skeletal muscle myosin and its proteolytic fragments. J Biochem. 1990 May;107(5):671–679. doi: 10.1093/oxfordjournals.jbchem.a123106. [DOI] [PubMed] [Google Scholar]
  69. Tawada K., Sekimoto K. A physical model of ATP-induced actin-myosin movement in vitro. Biophys J. 1991 Feb;59(2):343–356. doi: 10.1016/S0006-3495(91)82228-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Tonomura Y., Appel P., Morales M. On the molecular weight of myosin. II. Biochemistry. 1966 Feb;5(2):515–521. doi: 10.1021/bi00866a017. [DOI] [PubMed] [Google Scholar]
  71. Toyoshima Y. Y., Kron S. J., McNally E. M., Niebling K. R., Toyoshima C., Spudich J. A. Myosin subfragment-1 is sufficient to move actin filaments in vitro. Nature. 1987 Aug 6;328(6130):536–539. doi: 10.1038/328536a0. [DOI] [PubMed] [Google Scholar]
  72. Umemoto S., Bengur A. R., Sellers J. R. Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay. J Biol Chem. 1989 Jan 25;264(3):1431–1436. [PubMed] [Google Scholar]
  73. Umemoto S., Sellers J. R. Characterization of in vitro motility assays using smooth muscle and cytoplasmic myosins. J Biol Chem. 1990 Sep 5;265(25):14864–14869. [PubMed] [Google Scholar]
  74. Uyeda T. Q., Abramson P. D., Spudich J. A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4459–4464. doi: 10.1073/pnas.93.9.4459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Uyeda T. Q., Kron S. J., Spudich J. A. Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J Mol Biol. 1990 Aug 5;214(3):699–710. doi: 10.1016/0022-2836(90)90287-V. [DOI] [PubMed] [Google Scholar]
  76. Uyeda T. Q., Ruppel K. M., Spudich J. A. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature. 1994 Apr 7;368(6471):567–569. doi: 10.1038/368567a0. [DOI] [PubMed] [Google Scholar]
  77. Uyeda T. Q., Warrick H. M., Kron S. J., Spudich J. A. Quantized velocities at low myosin densities in an in vitro motility assay. Nature. 1991 Jul 25;352(6333):307–311. doi: 10.1038/352307a0. [DOI] [PubMed] [Google Scholar]
  78. Vale R. D., Oosawa F. Protein motors and Maxwell's demons: does mechanochemical transduction involve a thermal ratchet? Adv Biophys. 1990;26:97–134. doi: 10.1016/0065-227x(90)90009-i. [DOI] [PubMed] [Google Scholar]
  79. Vale R. D., Szent-Gyorgyi A. G., Sheetz M. P. Movement of scallop myosin on Nitella actin filaments: regulation by calcium. Proc Natl Acad Sci U S A. 1984 Nov;81(21):6775–6778. doi: 10.1073/pnas.81.21.6775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Wahr P. A., Metzger J. M. Peak power output is maintained in rabbit psoas and rat soleus single muscle fibers when CTP replaces ATP. J Appl Physiol (1985) 1998 Jul;85(1):76–83. doi: 10.1152/jappl.1998.85.1.76. [DOI] [PubMed] [Google Scholar]
  81. Wang F., Martin B. M., Sellers J. R. Regulation of actomyosin interactions in Limulus muscle proteins. J Biol Chem. 1993 Feb 15;268(5):3776–3780. [PubMed] [Google Scholar]
  82. Warshaw D. M., Desrosiers J. M., Work S. S., Trybus K. M. Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J Cell Biol. 1990 Aug;111(2):453–463. doi: 10.1083/jcb.111.2.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Webb M. R., Trentham D. R. The mechanism of ATP hydrolysis catalyzed by myosin and actomyosin, using rapid reaction techniques to study oxygen exchange. J Biol Chem. 1981 Nov 10;256(21):10910–10916. [PubMed] [Google Scholar]
  84. Weeds A. G., Pope B. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J Mol Biol. 1977 Apr;111(2):129–157. doi: 10.1016/s0022-2836(77)80119-8. [DOI] [PubMed] [Google Scholar]
  85. White H. D., Belknap B., Jiang W. Kinetics of binding and hydrolysis of a series of nucleoside triphosphates by actomyosin-S1. Relationship between solution rate constants and properties of muscle fibers. J Biol Chem. 1993 May 15;268(14):10039–10045. [PubMed] [Google Scholar]
  86. White H. D., Belknap B., Webb M. R. Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry. 1997 Sep 30;36(39):11828–11836. doi: 10.1021/bi970540h. [DOI] [PubMed] [Google Scholar]
  87. White H. D., Taylor E. W. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry. 1976 Dec 28;15(26):5818–5826. doi: 10.1021/bi00671a020. [DOI] [PubMed] [Google Scholar]
  88. Wolenski J. S., Cheney R. E., Forscher P., Mooseker M. S. In vitro motilities of the unconventional myosins, brush border myosin-I, and chick brain myosin-V exhibit assay-dependent differences in velocity. J Exp Zool. 1993 Sep 15;267(1):33–39. doi: 10.1002/jez.1402670106. [DOI] [PubMed] [Google Scholar]
  89. Yanagida T., Nakase M., Nishiyama K., Oosawa F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature. 1984 Jan 5;307(5946):58–60. doi: 10.1038/307058a0. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES