Conformational substates and dynamic properties of carbonmonoxy hemoglobin

Biophysical Chemistry

Volumn 104, Issue 1, 2003, Pages 335-344

  Cupane, Antonio ^a   Leone, Maurizio ^a   Militello, Valeria ^a  

^a UNIVERSITY OF PALERMO   (Italy)

Author keywords

Amide II band; Amide I band; CO stretching band; FTIR spectroscopy; Protein dynamics; Protein solvent coupling

Indexed keywords

AMIDE; CARBOXYHEMOGLOBIN; SOLVENT; WATER;

ARTICLE; CONFIDENCE INTERVAL; CONFORMATION; CONTROLLED STUDY; GLASS TRANSITION TEMPERATURE; HUMAN; HUMAN EXPERIMENT; INFRARED SPECTROSCOPY; MOLECULAR DYNAMICS; NORMAL HUMAN; PH; PRIORITY JOURNAL; STATISTICAL ANALYSIS; TAXONOMY; TEMPERATURE DEPENDENCE; THERMAL ANALYSIS;

EID: 0038016446     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(03)00002-4     Document Type: Article

References (40)

1. Frauenfelder H., Wolynes P.G. Biomolecules: where the physics of complexity and simplicity meet. Phys. Today. 47:1994;58-64.
2. Frauenfelder H., Parak F., Young R.D. Conformational substates in proteins. Annu. Rev. Biophys. Biophys. Chem. 17:1988;451-479.
3. Nienhaus G.U., Young R.D. Trigg G.L. Encyclopedia of Applied Physics, Protein Dynamics, vol. 15. 1996;163 VCH Publishers, New York.
4. Alben J.O., Caughey W.S. An infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin and heme carbonyls. Biochemistry. 7:1968;175-183.
5. Alben J.O., Beece D., Bowne S.F., et al. Infrared spectroscopy of photodissociated carboxy-myoglobin at low temperatures. Proc. Natl. Acad. Sci. USA. 79:1982;3744-3748.
6. Ansari A., Berendzen J., Braunstein D., et al. Rebinding and relaxation in the myoglobin pocket. Biophys. Chem. 26:1987;337-355.
7. Ormos P., Braunstein D., Frauenfelder H., Hong M.K., Lin S.L., Sauke T.B. Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin. Proc. Natl. Acad. Sci. USA. 85:1988;8492-8496.
8. Lim M., Jackson T.A., Anfinrud P.A. Binding of CO to myoglobin from a heme pocket docking site to form a nearly linear Fe-C-O. Science. 269:1995;962-966.
9. Li X.Y., Spiro T.G. Is bound CO linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data. J. Am. Chem. Soc. 110:1988;6024-6033.
10. Li T.S., Quillin M.L., Phillips G.N. Jr., Olson J.S. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry. 33:1994;1433-1446.
11. Karavitis M., Fronticelli C., Brinigar W.S., et al. Properties of human hemoglobins with increased polarity in the α- or β-heme pocket. Carbonmonoxy derivatives. J. Biol. Chem. 273:1998;23740-23749.
12. Morikis D., Champion P.M., Springer B.A., Sligar S.G. Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry. 28:1989;4791-4800.
13. Braunstein D.P., Chu K., Egeberg D., et al. Ligand binding to heme proteins. III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin. Biophys. J. 65:1993;2447-2454.
14. Balasubramanian S., Lambright D.G., Marden M.C., Boxer S.G. Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kinetics. Proc. Natl. Acad. Sci. USA. 90:1993;4718-4722.
15. Muller J.D., McMahon B.H., Chien E.Y.T., Sligar S.G., Nienhaus G.U. Connection between the taxonomic substates and protonation of histidines 64 and 97 in carbonmonoxy myoglobin. Biophys. J. 77:1999;1036-1051.
16. 17O isotopic chemical shifts and nuclear quadrupole coupling constants. Biophys. J. 72:1997;899-912.
17. Vojtechovsky J., Chu K., Berendzen J., Sweet R.M., Schlichting I. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77:1999;2153-2174.
18. Johnson J.B., Lamb D.C., Frauenfelder H., et al. Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxy-myoglobin. Biophys. J. 71:1996;1563-1573.
19. Ansari A., Berendzen J., Bowne S.F., et al. Protein states and proteinquakes. Proc. Natl. Acad. Sci. USA. 82:1985;5000-5004.
20. Potter W.T., Hazzard J.H., Choc M.G., Tucker M.P., Caughey W.S. Infrared spectra of carbonyl hemoglobins: characterization of dynamic heme pocket conformers. Biochemistry. 29:1990;6283-6295.
21. Schneebeck M.C., Vigil L.E., Friedman J.M., Chavez M.D., Ondrias M.R. Heme-CO religation in photolyzed hemoglobin: a time resolved Raman study of the Fe-CO stretching mode. Biochemistry. 32:1993;1318-1323.
22. Rebane K.K. Impurity Spectra of Solids. Elementary Theory of Vibrational Structure. 1970;Plenum Press, New York.
23. Shelby R.M., Harris C.B., Cornelius P.A. The origin of vibrational dephasing of polyatomic molecules in condensed phases. J. Chem. Phys. 70:1979;34-41.
24. Marks S., Cornelius P.A., Harris C.B. A critical test of vibrational dephasing theories in solids using spontaneous Raman scattering in isotopically mixed crystals. J. Chem. Phys. 73:1980;3069-3081.
25. Bitler A., Stavrov S.S. Iron-histidine resonance Raman band of deoxyheme proteins: effects of anharmonic coupling and glass-liquid phase transition. Biophys. J. 77:1999;2764-2776.
26. Ondrias M.R., Rousseau D.L., Simon S.R. Resonance Raman detection of structural dynamic at the active site in hemoglobin. Proc. Natl. Acad. Sci. USA. 79:1982;1511-1514.
27. Kaposi A.D., Vanderkooi J.M., Wright W.W., Fidy J., Stavrov S.S. Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase. Biophys. J. 81:2001;3472-3482.
28. Cordone L., Cupane A., San Biagio P.L., Vitrano E. Effect of some monohydric alcohols on the oxygen affinity of hemoglobin: relevance of solvent dielectric constant and hydrophobicity. Biopolymers. 18:1979;1975-1988.
29. Cupane A., Vitrano E., Cordone L. Effect of organic cosolvents on the dimer/tetramer equilibrium of human haemoglobin. J. Mol. Biol. 189:1986;343-351.
30. Potter W.T., Hazzard J.H., Kawanishi S., Caughey W.S. Direct measurement of carbon monoxide bound to different subunits of hemoglobin A in solution and in red cells by infrared spectroscopy. Biochem. Biophys. Res. Commun. 116:1983;719-725.
31. Bangcharoenpaurpong O., Schomacker K.T., Champion P.M. A resonance Raman investigation of myoglobin and hemoglobin. J. Am. Chem. Soc. 106:1984;5688-5689.
32. Schweitzer-Stenner R., Bobinger U., Dreybrodt W. Multimode analysis of depolarization ratio dispersion and excitation profiles of seven Raman fundamentals from the heme group in ferrocytochrome c. J. Raman Spectr. 22:1991;65-78.
33. Iben I.E.T., Braunstein D., Doster W., et al. Glassy behavior of a protein. Phys. Rev. Lett. 62:1989;1916-1919.
34. Ray G.B., Li X.-Y., Ibers J.A., Sessler J.L., Spiro T.G. How far can proteins bend the FeCO unit? Distal polar effects in heme proteins and models. J. Am. Chem. Soc. 116:1994;162-176.
35. Demmel F., Doster W., Petry W., Schulte A. Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents. Eur. Biophys. J. 26:1997;327-335.
36. Manas E.S., Getahun Z., Wright W.W., De Grado W.F., Vanderkooi J.M. Infrared spectra of amide groups in alpha-helical proteins: evidence for hydrogen bonding between helices and water. J. Am. Chem. Soc. 122:2000;9883-9890.
37. Gilmanshin R., Williams S., Callender R.H., Woodruff W.H., Dyer R.B. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA. 94:1997;3709-3713.
38. Meersmann F., Smeller L., Heremans K. Comparative Fourier transform infrared spectroscopy study of cold-, pressure- and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82:2002;2635-2644.
39. Caronna C., Cupane A. Dynamics and protein-solvent interactions of hemoglobin in T and R quaternary conformations. Spectr. Int. J. 16:2002;227-233.
40. Cordone L., Cupane A., Leone M., Vitrano E., Bulone D. Interaction between external medium and heme pocket in myoglobin probed by low-temperature optical spectroscopy. J. Mol. Biol. 199:1988;213-218.