Kinetics of the initial steps of rabbit psoas myofibrillar ATPases studied by tryptophan and pyrene fluorescence stopped-flow and rapid flow- quench. Evidence that cross-bridge detachment is slower than ATP binding

Biochemistry

Volumn 39, Issue 25, 2000, Pages 7508-7520

  Stehle, Robert ^b   Lionne, Corinne ^a   Travers, Franck ^a   Barman, Tom ^a  

^a INSERM   (France)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MYOSIN; PYRENE; TRYPTOPHAN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME BINDING; ENZYME KINETICS; FLUORESCENCE; MUSCLE FIBRIL; NONHUMAN; PRIORITY JOURNAL; PSOAS MUSCLE; RABBIT; REACTION ANALYSIS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANIMALS; BUFFERS; ETHYLENE GLYCOL; KINETICS; METHANOL; MYOFIBRILS; PROTEIN BINDING; PSOAS MUSCLES; PYRENES; RABBITS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0034720730     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0004753     Document Type: Article

References (54)

1. Huxley, H. E. (1969) Science 164, 1356-1365.
2. Lymn, R. W., and Taylor, E. W. (1971) Biochemistry 10, 4617-4624.
3. Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C., and Milligan, R. A. (1993) Science 261, 58-65.
4. Friedman, A. L., and Goldman, Y. E. (1996) Biophys. J. 71, 2774-2785.
5. Colomo, F., Piroddi, N., Poggesi, C., te Kronnie, G., and Tesi, C. (1997) J. Physiol. (London) 500, 535-548.
6. Sleep, J. A. (1981) Biochemistry 20, 5043-5051.
7. White, H. D. (1985) J. Biol. Chem. 260, 982-986.
8. Ma, Y. Z., and Taylor, E. W. (1994) Biophys. J. 66, 1542-1553.
9. Lionne, C., Stehle, R., Travers, F., and Barman, T. (1999) Biochemistry 38, 8512-8520.
10. Stehle, R., Lionne, C., Travers, F., and Barman, T. (1998) J. Muscle Res. Cell Motil. 19, 381-392.
11. Geeves, M. A. (1991) Biochem. J. 274, 1-14.
12. Trentham, D. R., Eccleston, J. F., and Bagshaw, C. R. (1976) Q. Rev. Biophys. 9, 217-281.
13. Chock, S. P., Chock, P. B., and Eisenberg, E. (1976) Biochemistry 15, 3244-3253.
14. Chock, S. P., Chock, P. B., and Eisenberg, E. (1979) J. Biol. Chem. 254, 3236-3243.
15. Johnson, K. A., and Taylor, E. W. (1978) Biochemistry 17, 3432-3442.
16. Rosenfeld, S. S., and Taylor, E. W. (1984) J. Biol. Chem. 259, 11908-11919.
17. Millar, N. C., and Geeves, M. A. (1988) Biochem. J. 249, 735-743.
18. Stehle, R., Lionne, C., Travers, F., and Barman, T. (1999) J. Muscle Res. Cell Motil. 20, 71-72.
19. Biosca, J. A., Barman, T. E., and Travers, F. (1984) Biochemistry 23, 2428-2436.
20. Herrmann, C., Sleep, J., Chaussepied, P., Travers, F., and Barman, T. (1993) Biochemistry 32, 7255-7263.
21. Knight, P. J., and Trinick, J. A. (1982) Methods Enzymol. 85, 9-12.
22. Herrmann, C., Lionne, C., Travers, F., and Barman, T. (1994) Biochemistry 33, 4148-4154.
23. Lionne, C., Travers, F., and Barman, T. (1996) Biophys. J. 70, 887-895.
24. Barman, T. E., and Travers, F. (1985) Methods Biochem. Anal. 31, 1-59.
25. Reimann, E. M., and Umfleet, R. A. (1978) Biochim. Biophys. Acta 523, 516-521.
26. Houadjeto, M., Travers, F., and Barman, T. (1992) Biochemistry 31, 1564-1569.
27. Bagshaw, C. R., and Trentham, D. R. (1974) Biochem. J. 141, 331-349.
28. Herrmann, C., Houadjeto, M., Travers, F., and Barman, T. (1992) Biochemistry 31, 8036-8042.
29. Biosca, J. A., Travers, F., Barman, T. E., Bertrand, R., Audemard, E., and Kassab, R. (1985) Biochemistry 24, 3814-3820.
30. Geerlof, A., Schmidt, P. P., Travers, F., and Barman, T. (1997) Biochemistry 36, 5538-5545.
31. Criddle, A. H., Geeves, M. A., and Jeffries, T. (1985) Biochem. J. 232, 343-349.
32. Trybus, K. M., and Taylor, E. W. (1982) Biochemistry 21, 1284-1294.
33. Geeves, M. A., Jeffries, T. E., and Millar, N. C. (1986) Biochemistry 25, 8454-8458.
34. Schoenberg, M. (1988) Biophys. J. 54, 135-148.
35. Kraft, T., Yu, L. C., Kuhn, H. J., and Brenner, B. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 11362-11366.
36. Lionne, C., Brune, M., Webb, M. R., Travers, F., and Barman, T. (1995) FEBS Lett. 364, 59-62.
37. Barman, T., Brune, M., Lionne, C., Piroddi, N., Poggesi, C., Stehle, R., Tesi, C., Travers, F., and Webb, M. R. (1998) Biophys. J. 74, 3120-3130.
38. Chalovich, J. M., Chock, P. B., and Eisenberg, E. (1981) J. Biol. Chem. 256, 575-578.
39. Wagner, P. D., and Giniger, E. (1981) J. Biol. Chem. 256, 12647-12650.
40. Frisbie, S. M., Chalovich, J. M., Brenner, B., and Yu, L. C. (1997) Biophys. J. 72, 2255-2261.
41. Goldman, Y. E., Hibberd, M. G., and Trentham, D. R. (1984) J. Physiol. (London) 354, 577-604.
42. Horiuti, K., Sakoda, T., and Yamada, K. (1992) J. Muscle Res. Cell Motil. 13, 685-691.
43. Tanner, J. W., Thomas, D. D., and Goldman, Y. E. (1992) J. Mol. Biol. 223, 185-203.
44. Poole, K. J., Rapp, G., Maeda, Y., and Goody, R. S. (1988) Adv. Exp. Med. Biol. 226, 391-404.
45. Tesi, C., Travers, F., and Barman, T. (1990) Biochemistry 29, 1846-1852.
46. Tesi, C., Barman, T., and Travers, F. (1990) FEBS Lett. 260, 229-232.
47. White, H. D., Belknap, B., and Webb, M. R. (1997) Biochemistry 36, 11828-11836.
48. Batra, R., and Manstein, D. J. (1999) J. Biol. Chem. 380, 1017-1023.
49. Peyser, Y. M., Muhlrad, A., and Werber, M. M. (1990) FEBS Lett. 259, 346-348.
50. Werber, M. M., Peyser, Y. M., and Muhlrad, A. (1987) Biochemistry 26, 2903-2909.
51. Hiratsuka, T. (1992) J. Biol. Chem. 267, 14949-14954.
52. Park, S., and Burghardt, T. P. (2000) Biophys. J. 78, 680a.
53. Eccleston, J. F., and Trentham, D. R. (1979) Biochemistry 18, 2896-2904.
54. Woledge, R. C., Curtin, N. A., and Homsher, E. (1985) Monogr. Physiol. Soc. 41, 1-357.