Protein relaxation in the photodissociation of myoglobin-CO complexes

Photochemical and Photobiological Sciences

Volumn 2, Issue 7, 2003, Pages 730-740

  Angeloni, Leonardo ^a   Feis, Alessandro ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; IRON; MYOGLOBIN;

ACIDITY; ARTICLE; DISSOCIATION; ENTHALPY; PRIORITY JOURNAL; TIME;

EQUUS CABALLUS; PHYSETER CATODON;

EID: 3042690149     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b301756g     Document Type: Article

References (59)

1. Q. H. Gibson, An apparatus for flash photolysis and its application to the reactions of myoglobin with gases, J. Physiol., 1956, 134, 112-122.
2. R. H. Austin, K. W. Beeson, L. Eisenstein, H. Frauenfelder and I. C. Gunsalus, Dynamics of ligand binding to myoglobin, Biochemistry, 1975, 14, 5355-5373.
3. E. R. Henry, J. J. Sommer and J. Hofrichter, Geminate recombination of carbon monoxide to myoglobin, J. Mol. Biol., 1983, 166, 443-451.
4. G. Dadusc, J. P. Ogilvie, P. Schulenberg, U. Marvel and R. J. D. Miller, Diffractive optics-based heterodyne-detected four-wave mixing signals of protein motion: from "protein quakes" to ligand escape for myoglobin, Proc. Natl. Acad. Sci. U. S. A., 2001, 98, 6110-6115.
5. M. Sakakura, M. Morishima and M. J. Terazima, The structural dynamics and ligand releasing process after the photodissociation of sperm whale carboxymyoglobin, J. Phys. Chem. B, 2001, 105, 10424-10434.
6. V. Šrajer, Z. Ren, T. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff and K. Moffat, Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction, Biochemistry, 2001, 40, 13802-13815.
7. W. Cao, J. F. Christian, P. M. Champion, F. Rosca and J. T. Sage, Water penetration and binding to ferric myoglobin, Biochemistry, 2001, 40, 5728-5737.
8. J. D. Müller, B. H. McMahon, E. J. T. Chien, S. G. Sligar and G. U. Nienhaus, Connection between the taxonomic substates and protonation of histidines 64 and 97 in carbonmonoxy myoglobin, Biophys. J., 1999, 77, 1036-1051.
9. F. Yang and G. N. Jr. Phillips, Crystal structures of CO-, deoxy-, and met-myoalobins at various pH values, J. Mol. Biol., 1996, 256, 762-774.
10. T. Sugimoto, M. Unno, Y. Shiro, V. Dou and M. Ikeda-Saito, Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain, Biophys. J. 1998, 75, 2188-2194.
11. W. D. Tian, J. T. Sage, P. M. Champion, E. Chien and S. G. Sligar, Probing heme protein conformational equilibration rates with kinetic selection, Biochemistry, 1996, 35, 3487-3502.
12. H. Frauenfelder, N. A. Alberding, A. Ansari, D. Braunstein, B. R. Cowen, M. K. Hong, I. E. T. Iben, J. B. Johnson, S. Luck, M. C. Marden, J. R. Mourant, P. Ormos, L. Reinisch, R. Scholl, A. Schulte, E. Shyamsunder, L. B. Sorensen, P. J. Steibach, A. Xie, R. D. Young and K. T. Yue, Proteins and pressure, J. Phys. Chem., 1990, 94, 1024-1037.
13. A. Ansari, J. Berendzen, D. Braunstein, B. R. Cowen, H. Frauenfelder, M. K. Hong, I. E. T. Iben, J. B. Johnson, P. Ormos, T. B. Sauke, R. Scholl, A. Schulte, P. J. Steinbach, J. Vittitow and R. D. Young, Rebinding and relaxation in the myoglobin pocket, Biophys. Chem., 1987, 26, 337-355.
14. S. E. Braslavsky and G. E. Heibel, Time-resolved photothermal and photoacoustic methods applied to photoinduced processes in solution, Chem. Rev., 1992, 92, 1381-1410.
15. J. A. Westrick, J. L. Goodman and K. S. Peters, A time-resolved photoacoustic calorimetry study of the dynamics of enthalpy and volume changes produced in the photodissociation of carbon monoxide from sperm whale carboxymyoglobin, Biochemistry, 1987, 26, 8313-8318.
16. J. A. Westrick, K. S. Peters, J. D. Ropp and S. G. Sligar, Role of the arginine-45 salt bridge in ligand dissociation from sperm whale carboxymyoglobin as probed by photoacoustic calorimetry, Biochemistry, 1990, 29, 6741-6746.
17. J. A. Westrick and K. S. Peters, A photoacoustic calorimetric study of horse myoglobin, Biophys. Chem., 1990, 37, 73-79.
18. C. L. Norris and K. S. Peters, A photoacoustic calorimetry study of horse carboxymyoglobin on the 10-nanosecond time scale, Biophys. J., 1993, 65, 1660-1665.
19. K. S. Peters, T. Watson and T. J. Logan, Photoacoustic calorimetry study of human carboxyhemoglobin, J. Am. Chem. Soc., 1992, 114, 4276-1278.
20. A. Feis and L. Angeloni, Photodissociation of the CO complex of horseradish peroxidase studied by laser-induced optoacoustic spectroscopy, J. Phys. Chem. B, 2001, 105, 2638-2643.
21. J. T. Sage, D. Morikis and P. M. Champion, Spectroscopic studies of myoglobin at low pH: heme structure and ligation, Biochemistry, 1991, 30, 1227-1237.
22. 2 in myoclobin, Eur. Biophys. J., 1997, 26, 209-214.
23. T. Gensch, C. Viappiani and S. E. Braslavsky, Laser induced optoacoustic spectroscopy, Encyclopedia of Spectroscopy and Spectrometry, ed. J. C. Lindon, G. E. Tranter and J. L. Holmes, Academic Press, London, 1999, p. 1124.
24. W. D. Tian, J. T. Sage, V. Šrajer and P. M. Champion, Relaxation dynamics of myoglobin in solution, Phys. Rev. Lett., 1992, 68, 408-411.
25. W. D. Tian, J. T. Sage and P. M. Champion, Investigation of ligand association and dissociation rates in the "open" and "closed" states of myoglobin, J. Mol. Biol., 1993, 233, 155-166.
26. cam: role of the Arg186-Asp251-Lys178 bifurcated salt bridge, Biochemistry, 1997, 36, 112-118.
27. K. A. Walters and K. S. Schanze, Determination of triplet energies in rhenium polypyridine complexes with laser-induced optoacoustic spectroscopy, The Spectrum, 1998, 11, 2-8.
28. M. Sakakura, S. Tamaguchi, N. Hirota and M. Terazima, Dynamics of structure and energy of horse carboxymyoglobin after photodissociation of carbon monoxide, J. Am. Chem Soc., 2001, 123, 4286-4294.
29. S. A. Rudolph, S. O. Boyle, C. F. Dresden and S. J. Gill, Calorimetric study of the binding of carbon monoxide to myoglobin, Biochemistry, 1972, 11, 1098-1101.
30. J. C. Kendrew, G. Bodo, H. N. Dintzis, R. G. Parrish, H. Wycoff and D. C. Phillips, A three-dimensional model of the myoglobin molecule obtained by X-ray analysis, Nature (London), 1958, 181, 662-666.
31. J. Vojtechovský, K. Chu, J. Berendzen, R. M. Sweet and I. Schlichting, Crystal structure of myoglobin-ligand complexes at near-atomic resolution, Biophys. J., 1999, 77, 2153-2174.
32. M. Lim, T. A. Jackson and P. A. Anfinrud, Mid-infrared vibrational spectrum of CO after photodissociation from heme: evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin, J. Chem. Phys., 1995, 102, 4355-4366.
33. V. Šrajer, T.-Y. Teng, Th. Ursby, C. Pradervand, Z. Ren, S.-i. Adachi, W. Schildkamp, D. Bourgeois, M. Wulff and K. Moffat, Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography, Science, 1996, 274, 1726-1729.
34. V. Šrajer, Z. Ren, T.-Y. Teng, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff and K. Moffat, Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction, Biochemistry, 2001, 40, 13802-13815.
35. D. C. Lamb, K. Nienhaus, A. Arcovito, F. Draghi, A. E. Miele, M. Brunori and G. U. Nienhaus, Structural dynamics of myoglobin, J. Biol. Chem., 2002, 277, 11636-11644.
36. A. Ansari, C. M. Jones, E. R. Henry, J. Hofrichter and W. Eaton, Conformational relaxation and ligand binding in myoglobin, Biochemistry, 1994, 33, 5128-5145.
37. R. F. Tilton Jr., I. D. Kuntz Jr. and G. A. Petsko, Cavities in proteins: structure of metmyoglobin-xenon complex solved to 1.9 Å, Biochemistry, 1984, 23, 2849-2857.
38. 45 rSer), Biochemistry, 1992, 31, 8732-8739.
39. S. R. Hubbard, W. A. Hendrickson, D. G. Lambright and S. G. Boxer, X-ray structure of a mutant recombinant human myoglobin at 2.8 Å resolution, J. Mol. Biol., 1990, 213, 215-218.
40. R. Maurus, C. M. Overall, R. Bogumil, Y. Luo, A. G. Mauk, M. Smith and G. D. Brayer, A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket, Biochim. Biophys. Acta, 1997, 1341, 1-13.
41. G. N. Phillips Jr., M. L. Teodoro, T. Li, B. Smith and J. S. Olson, Bound CO is the molecular probe of electrostatic potential in the distal pocket of myoglobin, J. Phys. Chem. B, 1999, 103, 8817-8829.
42. P. A. Anfinrud, R. de Vivie-Riedle and V. Engel, Ultrafast detection and control of molecular dynamics, Proc. Natl. Acad. Sci. U. S. A., 1999, 96, 8328-8329.
43. M. Lim, T. A. Jackson and P. A. Anfinrud, Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O, Science, 1995, 269, 962-966.
44. M. Lim, T. A. Jackson and P. A. Anfinrud, Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin, Nat. Struct. Biol., 1997, 4, 209-214.
45. T.-Y. Teng, V. Šrajer and K. Moffat, Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures, Biochemistry, 1997, 36, 12087-12100.
46. B. A. Springer, S. G. Sligar, J. S. Olson and G. N. Phillips Jr., Mechanism of ligand recognition in myoglobin, Chem. Rev., 1994, 94, 699-714.
47. J. S. Olson and G. N. Phillips Jr., Kinetic pathways and barriers for licand binding to myoglobin, J. Biol. Chem., 1996, 271, 17593-17596.
48. J. B. Johnson, D. C. Lamb, H. Frauenfelder, J. D. Müller, B. McMahon, G. U. Nienhaus and R. D. Young, Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin, Biophys. J., 1996, 71, 1563-1573.
49. T. Kleinert, W. Doster, H. Leyser, W. Petry, V. Schwarz and M. Settles, Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin, Biochemistry, 1998, 37, 717-733.
50. D. D. Eley, On the solubility of gases. Part II. A comparison of organic solvents with water, Trans. Faraday Soc., 1939, 35, 1421-1432.
51. M. Gajhede, D. J. Schuller, A. Henriksen, A. T. Smith and Th. L. Poulos, Crystal structure of horseradish peroxidase C at 2.15 Å resolution, Nat. Struct. Biol., 1997, 4, 1032-1038.
52. W. J. Le Noble, Kinetics of reactions in solutions under pressure, Prog. Phys. Org. Chem., 1967, 5, 207-330.
53. D. P. Kharakoz, Volumetric properties of proteins and their analogs in diluted water solutions. 1. Partial volumes of amino acids at 15-55 °C, Biophys. Chem., 1989, 34, 115-125.
54. K. Chu, J. Vojtchovský, B. H. McMahon, R. M. Sweet, J. Berendzen and I. Schlichting, Structure and ligand-binding intermediate in wild-type carbonmonoxy myoglobin, Nature, 2000, 403, 921-923.
55. C. Balny and F. Travers, Activation thermodynamics of the binding of carbon monoxide to horseradish peroxidase. Role of pressure, temperature and solvent, Biophys. Chem., 1989, 33, 237-244.
56. T. Uchida, K. Ishimori and I. Morishima, Unusual pressure effects on ligand rebinding to the human myoglobin leucine 29 mutants, J. Biol. Chem., 2000, 275, 30309-30316.
57. G. Kachalova, A. N. Popov and H. D. Bartunik, Steric mechanism for inhibiting of CO binding to heme proteins, Science, 1999, 284, 473-176.
58. E. F. Caldin and B. B. Hasinoff, Diffusion-controlled kinetics in the reaction of ferroprotoporphyrin IX with carbon monoxide, J. Chem. Soc., Faraday Trans, 1, 1975, 515-527.
59. R. W. Larsen, Volume and thermodynamic profiles of CO-binding to Fe(II) protoporphyrin IX in detergent micelles, Inorg. Chim. Acta, 1999, 288, 74-81.