Photolysis of the carbon monoxide complex of myoglobin: Nanosecond time- resolved crystallography

Science

Volumn 274, Issue 5293, 1996, Pages 1726-1729

  Šrajer, Vukica ^a   Teng, Tsu Yi ^a   Ursby, Thomas ^b   Pradervand, Claude ^a   Ren, Zhong ^a   Adachi, Shin Ichi ^c   Schildkamp, Wilfried ^a   Bourgeois, Dominique ^b,d   Wulff, Michael ^b   Moffat, Keith ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^c INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^d INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; MYOGLOBIN;

ARTICLE; CRYSTALLOGRAPHY; FOURIER ANALYSIS; MACROMOLECULE; MOLECULAR DYNAMICS; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN STRUCTURE; X RAY DIFFRACTION;

CARBON MONOXIDE; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; FOURIER ANALYSIS; GLOBINS; HEME; HISTIDINE; IRON; LIGANDS; MYOGLOBIN; PHOTOLYSIS; TEMPERATURE; TIME FACTORS;

EID: 10544231457     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5293.1726     Document Type: Article

References (44)

1. J.-L. Martin and M. H. Vos, Annu. Rev. Biophys. Biomol. Struct. 21, 199 (1992).
2. D. W. J. Cruickshank, J. R. Helliwell, L. N. Johnson, Eds., Time-resolved Macromolecular Crystallography (Oxford Science Publications, Oxford, UK, 1992); K. Moffat, Annu. Rev. Biophys. Biophys. Chem. 18, 309 (1989).
3. D. W. J. Cruickshank, J. R. Helliwell, L. N. Johnson, Eds., Time-resolved Macromolecular Crystallography (Oxford Science Publications, Oxford, UK, 1992); K. Moffat, Annu. Rev. Biophys. Biophys. Chem. 18, 309 (1989).
4. J. M. Bolduc et al., Science 268, 1312 (1995).
5. S. Sikora, A. S. Little, T. G. Dewey, Biochemistry 33, 4454 (1994).
6. T.-Y. Teng, V. Šrajer, K. Moffat, Nature Struct. Biol. 1, 701 (1994). Coordinates from related studies by Schlichting et al., Nature 317, 808 (1994) and Hartmann et al., Proc, Natl. Acad. Sci. U.S.A. 93, 7013 (1996) are not yet available. The three studies differ in key experimental conditions.
7. T.-Y. Teng, V. Šrajer, K. Moffat, Nature Struct. Biol. 1, 701 (1994). Coordinates from related studies by Schlichting et al., Nature 317, 808 (1994) and Hartmann et al., Proc, Natl. Acad. Sci. U.S.A. 93, 7013 (1996) are not yet available. The three studies differ in key experimental conditions.
8. T.-Y. Teng, V. Šrajer, K. Moffat, Nature Struct. Biol. 1, 701 (1994). Coordinates from related studies by Schlichting et al., Nature 317, 808 (1994) and Hartmann et al., Proc, Natl. Acad. Sci. U.S.A. 93, 7013 (1996) are not yet available. The three studies differ in key experimental conditions.
9. K. Moffat and R. Henderson, Curr. Opin. Struct. Biol. 5, 656 (1995).
10. K. Moffat, D. Szebenyi, D. Bilderback, Science 223, 1423 (1984).
11. S. Franzen, B. Bohn, C. Poyart, J.-L Martin, Biochemistry 34, 1224 (1995).
12. S. J. Hagen, J. Hofrichter, W. A. Eaton, Science 269, 959 (1995).
13. M. Lim, T. A. Jackson, P. A. Anfinrud, ibid., p. 962; _, J. Chem. Phys. 102, 4355 (1995).
14. M. Lim, T. A. Jackson, P. A. Anfinrud, ibid., p. 962; _, J. Chem. Phys. 102, 4355 (1995).
15. A. Ansari, C. Jones, E. R. Henry, J. Hofrichter, W. A. Eaton, Biochemistry 33, 5128 (1994).
16. M. Lim, T. A. Jackson, P. A. Anfinrud, Proc. Natl. Acad. Sci. U.S.A. 90, 5801 (1993).
17. A. Ansari, C. M. Jones, E. R. Henry, J. Hofrichter, W. A. Eaton, Science 256, 1796 (1992).
18. W. D. Tian, J. T. Sage, V. Srajer, P. M. Champion, Phys. Rev. Lett. 68, 408 (1992); L. Genberg, L. Richard, G. McLendon, R. J. D. Miller, Science 251, 1051 (1991); X. Xie and J. D. Simon, Biochemistry 30, 3682 (1991).
19. W. D. Tian, J. T. Sage, V. Srajer, P. M. Champion, Phys. Rev. Lett. 68, 408 (1992); L. Genberg, L. Richard, G. McLendon, R. J. D. Miller, Science 251, 1051 (1991); X. Xie and J. D. Simon, Biochemistry 30, 3682 (1991).
20. W. D. Tian, J. T. Sage, V. Srajer, P. M. Champion, Phys. Rev. Lett. 68, 408 (1992); L. Genberg, L. Richard, G. McLendon, R. J. D. Miller, Science 251, 1051 (1991); X. Xie and J. D. Simon, Biochemistry 30, 3682 (1991).
21. S. M. Janes, G. A. Dalickas, W. A. Eaton, R. M. Hochstrasser, Biophys. J. 54, 545 (1988).
22. R. H. Austin, K. W. Beeson, L. Eisenstein, H. Frauenfelder, I. C. Gunsalus, Biochemistry 14, 5355 (1975).
23. Q. H. Gibson, J. S. Olson, R. E. McKinnie, R. J. Rohlfs, J. Biol. Chem. 261, 10228 (1986).
24. P. Li, J. T. Sage, P. M. Champion, J. Chem. Phys. 97, 3214 (1992); R. Lingle Jr. et al., J. Am. Chem. Soc. 113, 3992 (1991).
25. P. Li, J. T. Sage, P. M. Champion, J. Chem. Phys. 97, 3214 (1992); R. Lingle Jr. et al., J. Am. Chem. Soc. 113, 3992 (1991).
26. H. Li, R. Elber, J. E. Straub, J. Biol. Chem. 268, 17908 (1993); K. Kuczera, J.-C. Lambry, J.-L. Martin, M. Karplus, Proc. Natl. Acad. Sci. U.S.A. 90, 5805 (1993); O. Schaad, H.-X. Zhou, A. Szabo, W. A. Eaton, E. Henry, ibid., p. 9547.
27. H. Li, R. Elber, J. E. Straub, J. Biol. Chem. 268, 17908 (1993); K. Kuczera, J.-C. Lambry, J.-L. Martin, M. Karplus, Proc. Natl. Acad. Sci. U.S.A. 90, 5805 (1993); O. Schaad, H.-X. Zhou, A. Szabo, W. A. Eaton, E. Henry, ibid., p. 9547.
28. H. Li, R. Elber, J. E. Straub, J. Biol. Chem. 268, 17908 (1993); K. Kuczera, J.-C. Lambry, J.-L. Martin, M. Karplus, Proc. Natl. Acad. Sci. U.S.A. 90, 5805 (1993); O. Schaad, H.-X. Zhou, A. Szabo, W. A. Eaton, E. Henry, ibid., p. 9547.
29. R. Elber and M. Karplus, J. Am. Chem. Soc. 112, 9161 (1990).
30. E. R. Henry, W. A. Eaton, R. M. Hochstrasser, Proc. Natl. Acad. Sci. U.S.A. 83, 8982 (1986).
31. -1, which in turn is equivalent to about five photons absorbed per pulse per molecule. If we assume that half of the absorbed laser pulse energy appears as heat (16), the maximum temperature jump in the crystal does not exceed 10 K.
32. D. Bourgeois et al., J. Synchrotron Rad. 3, 65 (1996).
33. S. E. V. Phillips, Brookhaven Protein Data Bank (1981), Identification Cods 1MBD.
34. J. Kuriyan, S. Wilz, M. Karplus, G. A. Petsko, J. Mol. Biol. 192, 133 (1986).
35. L. Zhu, J. T. Sage, A. A. Rigos, D. Morikis, P. M. Champion, ibid. 224, 207 (1992); I. E. T. Iben, L. Keszthelyi, D. Ringe, G. Váró, Biophys. J. 56, 459 (1989); D. Morikis, T. J. Sage, A. K. Rizos, P. M. Champion, J. Am. Chem. Soc. 110, 6341 (1988).
36. L. Zhu, J. T. Sage, A. A. Rigos, D. Morikis, P. M. Champion, ibid. 224, 207 (1992); I. E. T. Iben, L. Keszthelyi, D. Ringe, G. Váró, Biophys. J. 56, 459 (1989); D. Morikis, T. J. Sage, A. K. Rizos, P. M. Champion, J. Am. Chem. Soc. 110, 6341 (1988).
37. L. Zhu, J. T. Sage, A. A. Rigos, D. Morikis, P. M. Champion, ibid. 224, 207 (1992); I. E. T. Iben, L. Keszthelyi, D. Ringe, G. Váró, Biophys. J. 56, 459 (1989); D. Morikis, T. J. Sage, A. K. Rizos, P. M. Champion, J. Am. Chem. Soc. 110, 6341 (1988).
38. U. Genick et al., in preparation.
39. J. C. Kendrew and R. G. Parrish, Proc. R. Soc. London Ser. A 238, 305 (1956).
40. Y. Chen, V. Srajer, K. Ng, A. LeGrand, K. Moffat, Rev. Scient. Instrum. 65, 1506 (1994).
41. K. Ng, E. D. Getzoff, K. Moffat, Biochemistry 34, 879 (1995).
42. Z. Ren and K. Moffat, J. Appl. Cryst. 28, 461 (1995); ibid., p. 482.
43. Z. Ren and K. Moffat, J. Appl. Cryst. 28, 461 (1995); ibid., p. 482.
44. We thank J.-L. Laclare and the accelerator physics staff of ESRF for assistance; M. Roth for the use of his pulsed laser and for assistance and discussions; S. Labouré, C. Rubin, and A. LeGrand for experimental assistance; and C.-I. Brändén for continued support. Supported by the W. M. Keck Foundation, NIH GM 36452 and RR 07707 (K.M.), and a grantin-aid for Scientific Research on Priority Areas (06235102) from the Ministry of Education, Science, and Culture, Japan (S.-i.A.).