Structural investigation of pig metmyoglobin by 129Xe NMR spectroscopy

Biochimica et Biophysica Acta - General Subjects

Volumn 1674, Issue 2, 2004, Pages 182-192

  Corda, Marcella ^a   Era, Benedetta ^a   Fais, Antonella ^a   Casu, Mariano ^b  

^a Cittadella Univ di Monserrato   (Italy)

^b UNIVERSITY OF CAGLIARI   (Italy)

Author keywords

129Xe NMR; Hydrophobic cavity; Metmyoglobin; Xenon binding

Indexed keywords

METMYOGLOBIN; XENON; CARBOXYMYOGLOBIN; MYOGLOBIN;

AMINO ACID COMPOSITION; AQUEOUS SOLUTION; ARTICLE; BINDING SITE; CONCENTRATION (PARAMETERS); EQUILIBRIUM CONSTANT; MATHEMATICAL MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE ANALYSIS; SENSITIVITY AND SPECIFICITY; STRUCTURE ANALYSIS; SWINE; ANIMAL; CHEMISTRY; GENETICS; HORSE; MAGNETISM; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION;

EQUUS CABALLUS; SUS SCROFA;

ANIMALS; BINDING SITES; HORSES; MAGNETICS; METMYOGLOBIN; MYOGLOBIN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; SWINE; XENON ISOTOPES;

EID: 7044220470     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.06.011     Document Type: Article

References (57)

1. Schoenborn B.P., Watson H.C., Kendrew J.C. Binding of xenon to sperm whale myoglobin. Nature. 207:1965;28-30
2. Schoenborn B.P., Nobbs C.L. The binding of xenon to sperm whale. deoxymyoglobin. Mol. Pharmacol. 2:1966;495-498
3. Schoenborn B.P. Structure of alkaline metmyoglonin-xenon complex. J. Mol. Biol. 45:1969;279-303
4. Tilton R.F. Jr., Kuntz I.D. Jr., Petsko G.A. Cavities in proteins: structure of metmyoglobin-xenon complex solved to 1.9 Å Biochemistry. 23:1984;2849-2857
5. Tilton R.F. Jr., Kuntz I.D. Jr. Nuclear magnetic resonance studies of xenon-129 with myoglobin and haemoglobin. Biochemistry. 21:1982;6850-6857
6. McKim S., Hinton J.F. Evidence of xenon transport through the gramicidin channel - a Xe-129 NMR study. Biochim. Biophys. Acta. 1193:1994;186-198
7. Ratcliffe C. Xenon NMR. Annu. Rep. NMR Spectrosc. 36:1998;124-208
8. Miller K.W., Reo N.V., Schoot Uiterkamp A.J., Stengle D.P., Stengle T.R., Williamson K.L. Xenon NMR: chemical shift of a general anesthetic in common solvents, proteins, and membranes. Proc. Natl. Acad. Sci. U. S. A. 78:1981;4946-4949
9. Tilton R.F. Jr., Singh U.C., Weiner S.J., Connelly M.L., Kuntz I.D. Jr., Kollmann P.A. Computational studies of the interaction of myoglobin and xenon. Biochemistry. 23:1984;2849-2857
10. Navon G., Song Y.Q., Room T., Appelt S., Taylor R.E., Pines A. Enhancement of solution NMR and MRI with laser-polarized xenon. Science. 271:1996;1848-1851
11. Wolber J., Cherubini A., Dzik-Jurasz A.S., Leach M.O., Bifone A. Spin-lattice relaxation of laser-polarized xenon in human blood. Proc. Natl. Acad. Sci. U. S. A. 96:1999;3664-3669
12. Bowers C.R., Storhaug V., Webster C.E., Bharatam J., Cottone A. III, Gianna R., Betsey K., Gaffney B.J. Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized Xenon-129 NMR. J. Am. Chem. Soc. 121:1999;9370-9377
13. 1H cross relaxation in aqueous solutions. J. Magn. Reson. 139:1999;225-231
14. Rubin S.M., Spence M.M., Goodson B.M., Wemmer D.E., Pines A. Evidence of non-specific surface interactions between laser-polarized xenon and myoglobin in solution. Proc. Natl. Acad. Sci. 97:2000;3472-9475
15. 129Xe NMR spectroscopy. J. Magn. Reson. 150:2001;167-174
16. 129Xe chemical shifts in aqueous solution: further development of xenon as a biomolecular probe. J. Magn. Reson. 152:2001;79-86
17. Rubin S.M., Spence M.M., Dimitrov I.E., Ruiz E.J., Pines A., Wemmer D.E. Detection of a conformational change in maltose binding protein by Xe-129 NMR spectroscopy. J. Am. Chem. Soc. 123:2001;8616-8617
18. 129Xe NMR relaxation measurements for the study of heme proteins. ChemPhysChem. 3:2002;812-814
19. 129Xe spectroscopy. J. Mol. Biol. 322:2002;425-440
20. Wei B.Q.Q., Baase W.A., Weaver L.H., Matthews B.W., Shoichet B.K. A model binding site for testing scoring functions in molecular docking. J. Mol. Biol. 322:2002;339-355
21. Mulder F.A.A., Hon B., Ranjith Muhandiram D., Dahlquist F.W., Kay L.E. Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry. 39:2000;12614-12622
22. Landon C., Berthault P., Vovelle F., Desvaux H. Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat non-specific lipid transfer protein. Protein Sci. 10:2001;762-770
23. Rousseaux J., Dautrevaux M., Han K. Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobins. Biochim. Biophys. Acta. 439:1976;55-62
24. Wittenberg J.B., Wittenberg B.A. Preparation of myoglobins. Methods Enzymol. 76:1981;29-33
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
26. Smith D.W., Williams J.P. Analysis of the visible spectra of some sperm whale ferrimyoglobin derivatives. Biochem. J. 110:1968;297-301
27. Kleywegt G.J., Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr., D Biol. Crystallogr. 50:1994;178-185
28. Connolly M.L. The molecular surface package. J. Mol. Graph. 11:1993;139-143
29. Eisenhaber F., Argos P. Improved strategy in analytic surface calculation for molecular systems: handling of singularities and computational efficiency. J. Comput. Chem. 14:1993;1272-1280
30. Eisenhaber F., Lijnzaad P., Argos P., Sander C., Scharf M. The double cubic lattice method: efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies. J. Comput. Chem. 16:1995;273-284
31. Ewing G.J., Maestas S. The thermodynamic of absorption of xenon by myoglobin. J. Phys. Chem. 74:1970;2341-2344
32. Kurland R.J., McGarvey B.R. Isotropic NMR shifts in transitions metals complexes: the calculation of the contact and pseudocontact terms. J. Magn. Reson. 2:1970;286-301
33. Ann Walker F., La Mar G.N. Nuclear magnetic resonance studies of ferric porphyrins. Ann. N.Y. Acad. Sci. 206:1973;328-348
34. 45→Ser). Biochemistry. 31:1992;8732-8739
35. 1H nuclear magnetic resonance spectrum of carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques. J. Mol. Biol. 194:1987;313-327
36. James T.L. Nuclear Magnetic Resonance in Biochemistry. 1975;84-86 Academic Press, New York
37. Solomon I. Relaxation processes in a system of two spins. Phys. Rev. 99:1955;559-560
38. Bloembergen N. Proton relaxation times in paramagnetic solutions. J. Chem. Phys. 52:1957;572-573
39. Asakura T., Reed G.H., Leigh J.S. Jr. Solution electron paramagnetic spectra of hemoprotein at room temperature. Biochemistry. 11:1972;334-338
40. Fabry M.E., Eisenstadt M. The mechanism of water proton nuclear magnetic resonance relaxation in the presence of mammalian and Aplysia metmyoglobin fluoride. J. Biol. Chem. 249:1974;2915-2929
41. Gupta R.K., Mildvan A.S. Nuclear relaxation studies on human methemoglobin. J. Biol. Chem. 250:1975;246-253
42. Lanir A. Electron spin relaxation time of Fe(III) in high spin heme proteins. Biochim. Biophys. Acta. 497:1977;29-34
43. Zhou Y., Bowler B.E., Eaton G.R., Eaton S.S. Electron spin-lattice relaxation rates of high-spin Fe(III) complexes in glassy solvents at temperature between 6 and 298 K. J. Magn. Reson. 144:2000;115-122
44. Tilton R.F., Singh U.C., Kuntz I.D., Kollman P.A. Protein-ligand dynamics. A 96 picosecond simulation of a myoglobin-xenon complex. J. Mol. Biol. 199:1988;195-211
45. 1H NMR hyperfine shift pattern as a probe for ligation state in high-spin ferric hemoproteins: water binding in metmyoglobin mutants. J. Am. Chem. Soc. 113:1991;7886-7892
46. La Mar G.N., Budd D.I., Smith K.M., Langry K.C. Nuclear magnetic resonance of high-spin ferric hemoproteins. Assignment of proton resonances in met-aquo myoglobins using deuterium-labeled hemes. J. Am. Chem. Soc. 102:1980;1822-1827
47. Unger S.W., LeComte J.T.J., La Mar G.N. The utility of the nuclear overhauser effect for peak assignment and structure elucidation in paramagnetic proteins. J. Magn. Reson. 64:1985;521-526
48. Shulman R.G., Peisach J., Wyluda B.J. Effect of cyclopropane and xenon upon the high-resolution nuclear magnetic resonance spectrum of ferrimyoglobin cyanide. J. Mol. Biol. 48:1970;517-523
49. Ripmeester J.A., Ratcliffe C.I., Tse J.S. The nuclear magnetic resonance of Xe-129 trapped in clarthrates and some other solids. J. Chem. Soc., Faraday Trans. 84:1988;3731-3745
50. Bonardet J., Fraissard J., Gedeon A., Sprinuel-Huet M. Nuclear magnetic resonance of physisorbed Xe-129 used a probe to investigate porous solids. Catal. Rev., Sci. Eng. 41:1999;115-225
51. Sozzani P., Comotti A., Simonutti R., Meersmann T., Logan J.W., Pines A. A porous crystalline molecular solid explored by hyperpolarized xenon. Angew. Chem., Int. ed. 39:2000;2695-2698
52. Reisse J. Monoatomic xenon: its great interest in chemistry as a probe of intermolecular interactions, and its (easy) study by NMR. N. J. Chem. 10:1986;665-672
53. 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. 112:1990;9161-9175
54. Scott E.E., Gibson Q.H. Ligand migration in sperm whale myoglobin. Biochemistry. 36:1997;11909-11917
55. 2 entry into and exit from myoglobin. J. Biol. Chem. 276:2001;5177-5188
56. Brunori B., Cuttruzzolà F., Savino C., Travaglino-Allocatelli C., Vallone B., Gibson Q.H. Structural dinamics of ligand diffusion in the protein matrix: a study of a new myoglobin mutant Y(B10) Q(E7) R(E10). Biophys. J. 76:1999;1259-1269
57. Brunori B., Gibson Q.H. Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep. 2:2001;674-679