Ligand binding and conformational motions in myoglobin

Nature

Volumn 404, Issue 6774, 2000, Pages 205-208

  Ostermann, Andreas ^a   Waschipky, Robert ^b   Parak, Fritz G ^a   Nienhaus, G Ulrich ^b,c  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSITY OF ULM   (Germany)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MYOGLOBIN;

ARTICLE; BINDING KINETICS; BINDING SITE; CONFORMATIONAL TRANSITION; DISSOCIATION; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; TEMPERATURE SENSITIVITY;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HEME; KINETICS; LIGANDS; MYOGLOBIN; PHOTOLYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, INFRARED; WHALES; XENON;

EID: 0034624691     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35004622     Document Type: Article

References (31)

1. Austin, R. H., Beeson, K. W., Eisenstein, L., Frauenfelder, H. & Gunsalus, I. C. Dynamics of ligand binding to myoglobin. Biochemistry 14, 5355-5373 (1975).
2. Steinbach, P. J. et al. Ligand binding to heme proteins: connection between dynamics and function. Biochemistry 30, 3988-4001 (1991).
3. Olson, I. S. & Phillips, G. N. Jr. Kinetic pathways and barriers for ligand binding to myoglobin. J Biol. Chem. 271, 17593-17596 (1996).
4. Henry, E. R., Sommer, J. H., Hofrichter, J. & Eaton, W. A. Geminate recombination of carbon-monoxide to myoglobin. J. Mol. Biol. 166, 443-451 (1983).
5. Huang, X. & Boxer, S. G. Discovery of new ligand binding pathways in myoglobin by random mutagenesis. Nature Struct. Biol. 1, 226-229 (1994).
6. Quillin, M. L. et al. Structural and functional effects of apolar mutations of the distal valine in myoglobin. J. Mol. Biol. 245, 416-436 (1995).
7. Scott, E. E. & Gibson, Q. H. Ligand migration in sperm whale myoglobin. Biochemistry 36, 11909-11917 (1997).
8. Parak, F., Knapp, E. W. & Kucheida, D. Protein dynamics: Mössbauer-spectroscopy on deoxymyoglobin crystals. J. Mol. Biol. 161, 177-194 (1982).
9. Doster, W., Cusack, S. & Petry, W. Dynamical transition of myoglobin revealed by inelastic neutron-scattering. Nature 337, 754-756 (1939).
10. Nienhaus, G. U., Heinzl, J., Huenges, E. & Parak, F. Protein crystal dynamics studied by time-resolved analysis of X-ray diffuse scattering. Nature 338, 665-666 (1989).
11. Rasmussen, B. F., Stock, A. M., Ringe, D. & Petsko, G. A. Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 357, 423-424 (1992).
12. Schlichting, I., Berendzen, J., Phillips, G. N. Jr & Sweet, R. M. Crystal structure of photolysed carbonmonoxy-myoglobin. Nature 371, 808-812 (1494).
13. Teng, T. Y., Srajer, V. & Moffat, K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nature Struct. Biol. 1, 701-705 (1994).
14. Hartmann, H. et al. X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation. Proc. Natl Acad. Sci. USA 93, 7013-7016 (1996).
15. Lim, M., Jackson, T. A. & Anfinrud, P. A. Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin. Nature Struct. Biol. 4, 209-214 (1997).
16. Srajer, V. et al. Photolysis of the carbon-monoxide complex of myoglobin: nanosecond time-resolved crystallography. Science 274, 1726-1729 (1996).
17. Vitkup, D., Petsko, G. A. & Karplus, M. A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobin. Nature Struct. Biol. 4, 202-208 (1997).
18. Nienhaus, G. U., Mourant, I. R. & Frauenfelder, H. Spectroscopic evidence for conformational relaxation in myoglobin. Proc. Natl Acad. Sci. USA 89, 2902-2906 (1992).
19. Springer, B. A., Sligar S. G., Olson J. S. & Phillips, G. N. Jr. Mechanisms of ligand recognition in myoglobin. Chem. Rev. 94, 699-714 (1994).
20. Tilton, R. F., Kuntz, I. D. & Petsko, G. A. Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9-Å. Biochemistry 23, 2849-2857 (1984).
21. O2 Raman bands for oxymyoglobin mutants. J. Am. Chem. Soc. 118, 7845-7846 (1996).
22. Schoenborn, B. P., Watson, H. C. & Kendrew, J. C. Binding of xenon to sperm whale myoglobin, Nature 207, 28-30 (1965).
23. Elber, R. & Karplus, M. Enhanced sampling in molecular-dynamics: use of the time-dependent Hartree approximation for a simulation of carbon-monoxide diffusion through myoglobin. J. Am. Chem. Soc. 112, 9161-9175 (1990).
24. Frauenfelder, H., Parak, F. & Young, R. D. Conformational substates in proteins. Annu. Rev. Biophys. Biophys. Chem. 17, 451-479 (1988).
25. Nienhaus, G. U. & Young, R. D. Protein dynamics. Encyclopedia Appl. Phys. 15, 163-184 (1996).
26. Alben, J. O. et al. Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures. Prot. Natl Acad. Sci. USA 79, 3744-3748 (1982).
27. Nienhaus, G. U., Mourant, J. R., Chu, K. & Frauenfelder, H. Ligand binding to heme proteins: the effect of light on ligand binding in myoglobin. Biochemistry 33, 13413-13430 (1994).
28. Springer, B. A. & Sligar, S. G. High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Natl Acad. Sci. USA 84, 8961-8965 (1987).
29. Bailey, S. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
30. Brünger, A. T. X-PLOR Version 3.1. (Yale Univ. Press, New Haven, CT, 1992).
31. Read, R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149 (1986).