Effect of zinc and cadmium ions on structure and function of myoglobin

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 1, 2009, Pages 103-109

  Lepeshkevich, Sergei V ^a   Dzhagarov, Boris M ^a  

^a B I STEPANOV INSTITUTE OF PHYSICS   (Belarus)

Author keywords

Conformational change; Docking site; Laser spectroscopy; Photodissociation; Quantum yield

Indexed keywords

CADMIUM; METAL ION; MYOGLOBIN; OXYGEN; ZINC ION;

ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; GENETIC RECOMBINATION; LASER; METAL BINDING; MODULATION; MOLECULAR BIOLOGY; MOLECULAR DOCKING; MOLECULAR MODEL; OXYGEN AFFINITY; PERMEABILITY BARRIER; PHOTOLYSIS; PHOTOMETRY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; TIME;

ALGORITHMS; ANIMALS; BINDING SITES; CADMIUM; CATIONS; HORSES; KINETICS; LASERS; MYOGLOBIN; OXYGEN; PHOTOLYSIS; PROTEIN CONFORMATION; TEMPERATURE; XENON; ZINC;

EQUIDAE;

EID: 56449105547     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.09.024     Document Type: Article

References (40)

1. In: Eichhorn G.L. (Ed). Inorganic Biochemistry Vol. 1 (1973), Elsevier Scientific Publishing Company, New York
2. Cann J.R. Kinetics of the reversible reaction of sperm whale myoglobin with zinc. Biochemistry 3 (1964) 714-722
3. Blum O., Haiek A., Cwikel D., Dori Z., Meade T.J., and Gray H.B. Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6659-6662
4. Hemdan E.S., Zhao Y.-J., Sulkowski E., and Porath J. Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 1811-1815
5. Kirchner C., Liedl T., Kudera S., Pellegrino T., Javier A.M., Gaub H.E., Stölzle S., Fertig N., and Parak W.J. Cytotoxicity of colloidal CdSe and CdSe/ZnS nanoparticles. Nano Lett. 5 (2005) 331-338
6. Antonini E., and Brunori M. Hemoglobin and Myoglobin in their Reaction with Ligands (1971), North-Holland Publishers Co, Amsterdam
7. Breslow E., and Gurd F.R.N. Interaction of cupric and zinc ions with sperm whale metmyoglobin. J. Biol. Chem. 238 (1963) 1332-1342
8. Makinen M.W., Houtchens R.A., and Caughey W.S. Structure of carboxymyoglobin in crystals and in solution. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 6042-6046
9. Rifkind J.M., Keyes M.H., and Lumry R. Linkage between the binding sites for zinc and oxygen on sperm whale myoglobin. Biochemistry 16 (1977) 5564-5568
10. Hunter C.L., Maurus R., Mauk M.R., Lee H., Raver E.L., Tong H., Nguyen N., Smith M., Brayer G.D., and Mauk A.G. Introduction and characterization of a functionally linked metal ion binding site at the exposed heme edge of myoglobin. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 3647-3652
11. Banaszak L.J., Watson H.C., and Kendrew J.C. The binding of cupric and zinc ions to crystalline sperm whale myoglobin. J. Mol. Biol. 12 (1965) 130-137
12. Sillen L.G., and Martell A.E. Stability Constants of Metal Ion Complexes (1964), The Chemical Society, London
13. Puett D., Friebele E., and Wasserman B.K. The equilibrium unfolding parameters of horse and sperm whale myoglobin. J. Biol. Chem. 248 (1973) 4623-4634
14. Tetreau C., Novikov E., Tourbez M., and Lavalette D. Kinetic evidence for three photolyzable taxonomic conformational substates in oxymyoglobin. Biophys. J. 82 (2002) 2148-2155
15. Lepeshkevich S.V., Karpiuk J., Sazanovich I.V., and Dzhagarov B.M. A kinetic description of dioxygen motion within alpha-and beta-subunits of human hemoglobin in the R-state: geminate and bimolecular stages of the oxygenation reaction. Biochemistry 43 (2004) 1675-1684
16. Lepeshkevich S.V., Konovalova N.V., and Dzhagarov B.M. Laser kinetic studies of bimolecular oxygenation reaction of α and β subunits within the R state of human hemoglobin. Biochemistry (Russian) 68 (2003) 676-685
17. Dzhagarov B.M., and Lepeshkevich S.V. Kinetic studies of differences between α-and β-chains of human hemoglobin: an approach for determination of the chain affinity to oxygen. Chem. Phys. Lett. 390 (2004) 59-64
18. 2 and the vibrational relaxation of the six-coordinate heme species. J. Am. Chem. Soc. 124 (2002) 5914-5924
19. Dzhagarov B.M., Galievsky V.A., Kruk N.N., and Yakutovich M.D. Photodissociation of oxygenated forms of the native hemoglobin HbA and its isolated α-and β-subunits and kinetics of molecular oxygen rebinding. Dokl. Biophys. (Doklady Akademii Nauk) 366 (1999) 38-41
20. Chatfield M.D., Walda K.N., and Magde D. Activation parameters for ligand escape from myoglobin proteins at room temperature. J. Am. Chem. Soc. 112 (1990) 4680-4687
21. Scott E.E., and Gibson Q.H. Ligand migration in sperm whale myoglobin. Biochemistry 36 (1997) 11909-11917
22. 2 entry into and exit from myoglobin. J. Biol. Chem. 276 (2001) 5177-5188
23. Dantsker D., Roche C., Samuni U., Blouin G., Olson J.S., and Friedman J.M. The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities. J. Biol. Chem. 280 (2005) 38740-38755
24. Nienhaus K., Deng P., Olson J.S., Warren J.J., and Nienhaus G.U. Structural dynamics of myoglobin. Ligand migration and binding in valine 68 mutants. J. Biol. Chem. 278 (2003) 42532-42544
25. Lamb D.S., Nienhaus K., Arcovito A., Draghi F., Miele A.E., Brunori M., and Nienhaus G.U. Structural dynamics of myoglobin. Ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy. J. Biol. Chem. 277 (2002) 11636-11644
26. Elber R., and 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
27. Bossa C., Anselmi M., Roccatano D., Amadei A., Vallone B., Brunori M., and Di Nola A. Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin. Biophys. J. 86 (2004) 3855-3862
28. Ostermann A., Waschipky R., Parak F.G., and Nienhaus G.U. Ligand binding and conformational motions in myoglobin. Nature 404 (2000) 205-208
29. Chu K., Vojtchovský J., McMahon B.H., Sweet R.M., Berendzen J., and Schlichting I. Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin. Nature 403 (2000) 921-923
30. Schotte F., Lim M., Jackson T.A., Smirnov A.V., Soman J., Olson J.S., Phillips Jr. G.N., Wulff M., and Anfinrud P.A. Watching a protein as it functions with 150-ps time-resolved X-ray crystallography. Science 300 (2003) 1944-1947
31. Bourgeois D., Vallone B., Schotte F., Arcovito A., Miele A.E., Sciara G., Wulff M., Anfinrud P., and Brunori M. Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 8704-8709
32. Tilton Jr. R.F., Kuntz Jr. I.D., and Petsko G.A. Cavities in proteins: structure of a metmyoglobin - xenon complex solved to 1.9 Å. Biochemistry 23 (1984) 2849-2857
33. Steinbach P.J., Ansari A., Berendzen J., Braunstein D., Chu K., Cowen B.R., Ehrenstein D., Frauenfelder H., Johnson J.B., Lamb D.C., Luck S., Mourant J.R., Nienhaus G.U., Ormos P., Philipp R., Xie A., and Young R.D. Ligand binding to heme proteins: connection between dynamics and function. Biochemistry 30 (1991) 3988-4001
34. Matsukawa S., Mawataii K., Yoneyama Y., and Kitagawa T. Correlation between the iron-histidine stretching frequencies and oxygen affinity of hemoglobin. A continuous strain model. J. Am. Chem. Soc. 107 (1985) 1108-1113
35. Friedman J.M. Structure, dynamics, and reactivity in hemoglobin. Science 228 (1985) 1273-1280
36. Morikis D., Champion P.M., Springer B.A., and Sligar S.G. Resonance Raman investigation of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry 28 (1989) 4791-4800
37. Ansari A., Berendzen J., Bowne S.F., Frauenfelder H., Iben I.E.T., Sauke T.B., Shyamsunder E., and Young R.D. Protein states and proteinquakes. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 5000-5004
38. Merchant K.A., Thompson D.E., Xu Q.-H., Williams R.B., Loring R.F., and Fayer M.D. Myoglobin-CO conformational substate dynamics: 2D vibrational echoes and MD simulations. Biophys. J. 82 (2002) 3277-3288
39. Franzen S., Bohr B., Poyart C., and Martin J.L. Evidence for the sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species. Biochemistry 34 (1995) 1224-1237
40. Kholodenko Y., Volk M., Gooding E., and Hochstrasser R.M. Energy dissipation and relaxation processes in deoxy myoglobin after photoexcitation in the Soret region. Chem. Phys. 259 (2000) 71-87