Protein dynamics in an intermediate state of myoglobin: Optical absorption, resonance Raman spectroscopy, and x-ray structure analysis

Biophysical Journal

Volumn 78, Issue 4, 2000, Pages 2081-2092

  Engler, Niklas ^a   Ostermann, Andreas ^a   Gassmann, Alexandra ^a   Lamb, Don C ^a   Prusakov, Valeri E ^b   Schott, Joachim ^c   Schweitzer Stenner, Reinhard ^c   Parak, Fritz G ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b SEMENOV INSTITUTE OF CHEMICAL PHYSICS   (Russian Federation)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

METMYOGLOBIN; MYOGLOBIN;

ABSORPTION SPECTROSCOPY; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTRON TRANSPORT; MOLECULAR DYNAMICS; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; REDUCTION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; X IRRADIATION; X RAY CRYSTALLOGRAPHY;

EID: 0034028925     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76755-5     Document Type: Article

References (54)

1. 15N substituted derivatives. II. A normal coordinate analysis. J. Chem. Phys. 69: 4526-4534.
2. Agmon, N., and J. J. Hopfield. 1983. CO binding to heme proteins: A model for barrier height distributions and slow conformational changes. J. Chem. Phys. 79:2042-2053.
3. Austin, R. H., K. W. Beeson, L. Eisenstein, H. Frauenfelder, and I. C. Gunsalus. 1975. Dynamics of ligand binding to myoglobin. Biochemistry: 14:5355-5373.
4. Balasubramanian, S., D. G. Lambright, M. C. Marden, and S. G. Boxer. 1993. CO recombination to human myoglobin mutants in glycerol-water solutions. Biochemistry. 32:2202-2212.
5. Bersuker, I. B., and S. S. Stavrov. 1988. Structure and properties of metalloporphyrins an hemoproteins: the vibronic approach. Coord. Chem. Rev. 88:1-68.
6. Brünger, A. T. 1992. X-PLOR, version 3.1. A System for X-Ray Crystallography and NMR. Yale University Press, New Haven. CT.
7. 1994. Collaborative computational project, number 4. Acta Crystallogr. D. 50:760-763.
8. Chan, C. K., and J. B. Page. 1983. Temperature effects in the time correlator theory of resonance Raman scattering. J. Chem. Phys. 79: 5234-5250.
9. Chan, C. K., and J. B. Page. 1984. T ≠ 0 K multimode modeling of optical absorption spectra and resonance Raman profiles. Chem. Phys. Lett. 104:609-614.
10. Choi, S., J. J. Lee, Y. H. Wie, and T. G. Spiro. 1983. Resonance Raman and electronic spectra of heme a complexes and cytochrome oxidase. J. Am. Chem. Soc. 105:3692-3707.
11. Cupane, A., M. Leone, L. Cordone, H. Gilch, W. Dreybrodt, E. Unger, and R. Schweitzer-Stenner. 1996a. Conformational properties of Ni(II)octaethylporphyrin in solution. 2. A low-temperature optical absorption spectroscopy study. J. Phys. Chem. 100:14192-14197.
12. Cupane, A., M. Leone, E. Vitrano, and L. Cordone. 1995. Low temperature optical absorption spectroscopy: an approach to the study of stereodynamic properties of hemeproteins. Eur. Biophys. J. 23:385-398.
13. Cupane, A., E. Vitrano, P. Ormos, and G. U. Nienhaus. 1996b. Heme geometry in the 10 K photoproduct from sperm whale carbonmonoxymyoglobin. Biophys. Chem. 60:111-117.
14. DiPace, A., A. Cupane, M. Leone, E. Vitrano, and L. Cordone. 1992. Protein dynamics vibrational coupling, spectral broadening mechanisms, and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band line shape. Biophys. J. 63:475-484.
15. Esquerra, R. M., R. A. Goldbeck, D. B. Kim-Shapiro, and D. S. Kliger. 1998. Spectroscopic evidence tor nanosecond protein relaxation after photodissociation of myoglobin-CO. Biochemistry. 37:17527-17536.
16. Franzen, S., and S. G. Boxer. 1997. On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis. J. Biol. Chem. 272:9655-9660.
17. Gouterman, M. 1959. Study of the effects of substitution on the absorption spectra of porphyrin. 7. Chem. Phys. 30:1139-1161.
18. Hartmann, H., S. Zinser, P. Komninos, R. T. Schneider, G. U. Nienhaus, and F. Parak. 1996. X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation. Proc. Natl. Acad. Sci. USA. 93:7013-7016.
19. Hodel, A., S.-H. Kim, and A. T. Brünger. 1992. Model bias in macromolecular crystal structures. Acta Crystallogr. A. 48:851-859.
20. Hu, S., K. M. Smith, and T. G. Spiro. 1996. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118:12638-12646.
21. Jentzen, W., E. Unger, G. Karvounis, J. A. Shelnutt, W. Dreybrodt, and R. Schweitzer-Stenner. 1995. Conformational properties of nickel(II)octaethylporphyrin in solution. 1. Resonance excitation profiles and temperature dependence of structure sensitive Raman lines. J. Phys. Chem. 100:14184-14191.
22. Johnson, J. B., D. C. Lamb, H. Frauenfelder, J. D. Müller, B. McMahon, G. U. Nienhaus, and R. D. Young. 1996. Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin. Biophys. J. 71:1563-1573.
23. Kitagawa, T., Y. Ozaki, and Y. Kyogoku. 1978. Resonance Raman studies on the ligand-iron interactions in hemoproteins and metallo-porphyrins. Adv. Biophys. 11:153-196.
24. Kleinert, T., W. Doster, H. Leyser, W. Petry, V. Schwarz, and M. Settles 1998. Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin. Biochemistry. 37:717-733.
25. Kushkuley, B., and S. Stavrov. 1996. Theoretical study of the distal-side steric and electrostatic effects on the vibrational characteristics of the FeCO unit of the carbonylheme proteins and their models Biophys. J. 70:1214-12229.
26. Lamb, D. C., A. Ostermann, V. E. Prusakov, and F. G. Parak. 1998a. From metmyoglobin to deoxy myoglobin: relaxations of an intermediate state. Eur. Biophys. J. 27:113-125.
27. 2O to ferrous sperm whale myoglobin. J. Am. Chem. Soc. 120:2981-2982.
28. Lambright, D. G., S. Balasubramanian, and S. G. Boxer. 1991. Protein relaxation dynamics in human myoglobin. Chem. Phys. 158:249-260.
29. Lemke, C., W. Dreybrodt, J. A. Shelnutt, J. M. E. Quirke, and R. Schweitzer-Stenner. 1998. Polarized Raman dispersion spectroscopy probes planar and non-planar distortions of Ni(II)porphyrins with different peripheral substituents. J. Raman Spectrosc. 29:945-953.
30. Leone, M., A. Cupane, and L. Cordone. 1996. Low temperature optical spectroscopy of low-spin ferric hemeproteins. Eur. Biophys. J. 24: 117-124.
31. 16 Raman and infrared isotope shifts. J. Phys. Chem. 94:47-61.
32. Lim, M., T. A. Jackson, and P. A. Anfinrud. 1993. Nonexponential protein relaxation: dynamics of conformational change in myoglobin. Proc. Natl. Acad. Sci. USA. 90:5801-5804.
33. Makinen, M. W., and A. K. Churg. 1983. Structural and analytical aspects of the electronic spectra of hemeproteins. In Iron Porphyrins, Part I. A. B. P. Lever and H. B. Gray, editors. Addison-Wesley, Reading, PA. 141-235.
34. Melchers, B., E. W. Knapp, F. Parak, L. Cordone, A. Cupane, and M. Leone. 1996. Structural Fluctuations of Myoglobin from Normal-Modes, Mossbauer, Raman and Absorption Spectroscopy. Biophys. J. 70:2092-2099.
35. Nienhaus, G. U., J. R. Mourant, and H. Frauenfelder. 1992. Spectroscopic evidence for conformational relaxation in myoglobin. Proc. Natl. Acad Sci. USA. 89:2902-2906.
36. Ormos, P., S. Szaraz, A. Cupane, and G. U. Nienhaus. 1998. Structural factors controlling ligand binding to myoglobin: a kinetic hole burning study. Proc. Natl. Acad. Sci. USA. 95:6762-6767.
37. Parak, F., H. Hartmann, K. D. Aumann, H. Reuscher, G. Rennekamp, H. Bartunik, and W. Steigemann. 1987. Low temperature x-ray investigation of structural distributions in myoglobin. Eur. Biophys. J. 15: 237-249.
38. Parak, F., and V. E. Prusakov. 1994. Relaxation of non-equilibrium states of myoglobin studied by Mössbauer spectroscopy. Hyperfine Interact. 91:885-890.
39. Perutz, M. F., A. J. Wilkinson, M. Paoli, and G. G. Dodson. 1998. The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu. Rev. Biophys. Biomol. Struct. 27:1-34.
40. Prusakov, V. E., J. Steyer, and F. Parak. 1995. Mossbauer spectroscopy on nonequilibrium states of myoglobin: a study of r-t relaxation. Biophys. J. 68:2524-2530.
41. Read, R. J. 1986. Improved Fourier coefficients for maps using phases from partial structure with errors. Acta Crystallogr. A. 42:140-149.
42. Schlichting, I., J. Berendzen, G. N. Phillips, Jr., and R. M. Sweet. 1994. Crystal structure of photolysed carbonmonoxy-myoglobin. Nature. 371: 808-812.
43. Schweitzer-Stenner, R. 1989. Allosteric linkage-induced distortions of the prosthetic group in haem proteins as derived by the theoretical interpretation of the depolarization ratio in resonance Raman scattering. Q. Rev. Biophys. 22:381-479.
44. Schweitzer-Stenner, R., A. Stichternath, W. Dreybrodt, W., Jentzen, X.-Z. Song, J. A. Shelnutt, O. Faurskov-Nielsen, C. J. Medforth. and K. M. Smith. 1997. Raman dispersion spectroscopy on the highly saddled nickel(II)-octaethyltetraphenylporphyrin reveals the symmetry of non-planar distortions and the vibronic coupling strength of normal modes. J. Chem. Phys. 107:1794-1814.
45. Smulevich, G., S. Hu, K. R. Rodgers, D. B. Goodin, K. M. Smith, and T. G. Spiro. 1996. Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labelled hemes. Biospectroscopy. 2:365-376.
46. Spiro, T. G. 1983. The resonance Raman spectroscopy of metallo porphyrins and heme proteins. In Iron Porphyrins, Part II. A. B. P. Lever and H. B. Gray, editors. Addison-Wesley, Reading, PA. 90-159.
47. Šrajer, V., K. T. Schomacker, and P. M. Champion. 1986. Spectral broadening in biomolecules. Phys. Rev. Lett. 57:1267-1270.
48. Šrajer, V., and P. M. Champion. 1991. Investigations of optical line shapes and kinetic hole burning in myoglobin. Biochemistry. 30:7390-7402.
49. Šrajer, V., T.-Y. Teng, T. Ursby, C. Pradervand, Z. Ren, S.-I. Adachi, W. Schildkamp, D. Bourgeois, M. Wulff, and K. Moffat. 1996. Photolysis of the carbon monoxide complex of myoglobin: Nanosecond time-resolved crystallography. Science. 274:1726-1729.
50. Steinbach, P. J., A. Ansari, J. Berendzen, D. Braunstein, K. Chu, B. R. Cowen, D. Ehrenstein, H. Frauenfelder, B. Johnson, D. C. Lamb, S. Luck, J. R. Mourant, G. U. Nienhaus, P. Ormos, R. Phillip, A. Xie, and R. D. Young. 1991. Ligand binding to heme proteins: connection between dynamics and function. Biochemistry. 30:3988-4001.
51. Teng, T.-Y., V. Srajer, and K. Moffat. 1994. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nature Struct. Biol. 1:701-705.
52. Vitkup, D., G. A. Petsko, and M. Karplus. 1997. A comparison between molecular dynamics and x-ray results for dissociated CO in myoglobin. Nature Struct. Biol. 4:202-208.
53. Vojtechovsky, J., K. Chu, J. Berendzen, R. M. Sweet, and I. Schlichting. 1999. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77:2153-2174.
54. Zgierski, M. Z., and M. Pawlikowski. 1982. Depolarization dispersion curves of resonance Raman fundamentals of metalloporphyrins and metallophtalocyanines. Subject to asymmetric perturbations. Chem. Phys. 65:335-367.