Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin

Nature

Volumn 403, Issue 6772, 2000, Pages 921-923

  Chu, Kelvin ^a,b   Vojtchovský, Jaroslav ^c   McMahon, Benjamin H ^d   Sweet, Robert M ^e   Berendzen, Joel ^b   Schlichting, Ilme ^c  

^a LOS ALAMOS NATIONAL LABORATORY   (United States)

^b University of Vermont   (United States)

^c MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^d CENTER FOR NONLINEAR STUDIES   (United States)

^e BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CARBOXYMYOGLOBIN; HEMOPROTEIN; HYDROGEN; METALLOPROTEIN; NITRIC OXIDE; OXYGEN;

ARTICLE; BINDING SITE; CATALYSIS; CELL RESPIRATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; LIGAND BINDING; MOLECULAR DYNAMICS; OXYGEN DIFFUSION; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN STRUCTURE; REACTION ANALYSIS; SIGNAL TRANSDUCTION; SPECTROSCOPY;

ANIMALS; BINDING SITES; CARBON MONOXIDE; CRYSTALLOGRAPHY, X-RAY; HORSES; LIGANDS; MYOGLOBIN; OXYGEN; PROTEIN CONFORMATION;

EID: 0034708201     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35002641     Document Type: Article

References (30)

1. Antonini, E. and Brunori, M. Hemoglobin and Myoglobin in their Reactions with Ligands (North-Holland Pub. Co., Amsterdam, 1971).
2. Vojtchovský J. et al. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77, 2153-2174 (1999).
3. Elber R. and Karplus M. Multiple-conformational states of proteins: a molecular dynamics analysis of myoglobin. Science, 235, 318-321 (1987).
4. Carlson, M. L., Regan, R. M & Gibson, Q. H. Distal cavity fluctuations in myoglobin: protein motion and ligand diffusion. Biochem. 35, 1125-1136 (1996).
5. Tilton, R. J. Jr et al. Computational studies of the interaction of myoglobin and xenon. J Mol. Biol, 192, 443-456 (1986).
6. Huang X. & Boxer S. G. Discovery of new ligand-binding pathways in myoglobin by random mutagenesis. Nature Struct. Biol. 1, 226-229 (1994).
7. Austin R. H. et al. Dynamics of ligand-binding to myoglobin. Biochem. 14, 5355-5373 (1975).
8. Scott, E. E. & Gibson Q. H. Ligand migration in sperm whale myoglobin. Biochemistry 36, 11909-11917 (1997).
9. McMahon, B. H. Energetics of protein fluctuations: Ligand binding to myoglobin and electron transfer in reaction center. Thesis, Univ. of Illinois at Urbana-Champaign, (1997).
10. Chu, K. et al. Light-induced and thermal relaxation in a protein. Phys. Rev. Lett. 74, 2607-2610 (1995).
11. 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).
12. Alben, J. O. et al. Infrared spectroscopy of photodissociated myoglobin. Proc. Natl Acad. Sci. USA 79, 3744-3748 (1982).
13. Powers, L. et al. Kinetic, structural and spectroscopic identification of geminate states of myoglobin: a ligand-binding site on the reaction pathway. Biochemistry 26, 4785-4796 (1987).
14. Tilton, R. F. Jr., Kuntz, I. D. Jr. & Petsko, G. A. Cavities in proteins; structure of a metmyoglobin-xenon complex solved to 1.9 Å. Biochemistry 23, 2819-2857 (1984).
15. Frauenfelder, H. Sligar, S. G. & Wolynes, P. G. The energy landscapes and motions of proteins. Science 254, 1598-1603 (1991).
16. Schlichting, I., Berendzen, J., Phillips, G. N. Jr. & Sweet, R. M. Crystal structure of photolysed myoglobin. Nature, 371, 808-812 (1994).
17. Hartmann, H. et al. X-ray structure determination of a metastable state of carbonmonoxymyoglobin after photodissociation. Proc. Natl Acad. Sci. USA, 93, 7013-7016 (1996).
18. Teng, T. V., Srajer, V. & Moffat, K. Photolysis-induced structural changes in single crystals of carbonmonoxymyoglobin at 40 K. Nature Struct. Biol., 1, 701-705 (1994).
19. Anfinrud, P., deVivie-Riedle, R. & Engel, V., Ultrafast control and detection of molecular dynamics. Proc. Natl Acad. Sci. USA 96, 8328-8329 (1999).
20. Gibson, Q. H., Regan, R., Elber, R., Olson, J. S. & Carver, T. E. Distal pocket residues affect picosecond ligand recombination in myoglobin: an experimental and molecular dynamics study of position 29 mutants. J. Biol. Chem. 267, 22022-22034 (1992).
21. Quillin, M. L. et al. Structural and functional effects of the distal valine in myoglobin. J. Mol. Biol. 245, 416-436 (1995).
22. Kachalova, G. S., Popov, A. N. & Bartunik, H. D. A steric mechanism for inhibition of CO binding to haem proteins. Science 284, 473-476 (1999).
23. Abadan, Y. et al. Ligand binding to haem proteins V: light-induced relaxation in proximal mutants L89I and H97F of carbonmonoxymyoglobin. Biophys. J. 68, 2497-2504 (1995).
24. Ahmed, A. M. et al. Evidence for proximal control of ligand specificity in haemproteins: absorption and Raman studies of cryogenically trapped photoproducts of ligand bound myoglobins. Chem. Phys. 158, 329-352 (1991).
25. Brunori, M. et al. Does picosecond protein dynamics have survival value? Trends Biochem. Sci. 24, 253-255 (1999).
26. Montet, Y. et al. Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics. Nature Struct. Biol. 4, 523-526 (1997).
27. Kahsch, W. Automatic processing of rotation diffraction data from crystals of originally unknown symmetry and cell constants. J. App. Crystallogr. 24, 795-800 (1993).
28. Brünger, A. T. X-PLOR: A System for Crystallography and NMR, Version 3.1 (Yale Univ. Press, New Haven, 1992).
29. Jones, T. A. et al. Improved methods for building protein models in electron density maps and the location of errors in these models. Actn Crystallogr. A 47, 110-119 (1991).
30. Esnouf, R. A. An extensively modified version of MolStript that includes greatly enhanced coloring capabilities. J. Mol. Graphics 15, 132-134 (1997)