Influence of NaCl and sorbitol on the stability of conformations of cytochrome c

Biophysical Chemistry

Volumn 135, Issue 1-3, 2008, Pages 110-115

  Bagelova J ^a   Fedunova D ^a   Gazova Z ^a   Fabian, M ^c   Antalik M ^a,b  

^a INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^b P J AFÁRIK UNIVERSITY   (Slovakia)

^c RICE UNIVERSITY   (United States)

Author keywords

Cytochrome c; Heme ligands; Molten globule; Protein conformation; Protein stability

Indexed keywords

CYTOCHROME C; SODIUM CHLORIDE; SORBITOL;

ACIDIFICATION; ARTICLE; CIRCULAR DICHROISM; ELECTRON SPIN RESONANCE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; TEMPERATURE;

ANIMALS; CIRCULAR DICHROISM; CYTOCHROMES C; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME STABILITY; HORSES; HUMANS; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; SODIUM CHLORIDE; SORBITOL; SPECTROPHOTOMETRY; TEMPERATURE;

EID: 43049090774     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.03.010     Document Type: Article

References (37)

1. Pascher T., Chesick J.P., Winkler J.P., and Gray H.B. Protein folding triggered by electron transfer. Science 271 (1996) 1558-1560
2. Marmorino J.L., and Pielak G.J. A native tertiary interaction stabilizes the A-state of cytochrome c. Biochemistry 34 (1995) 3140-3143
3. Bushnell G.W., Louie G.V., and Brayer G.D. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214 (1990) 585-595
4. Winkler J.R. Cytochrome c folding dynamics. Curr. Opin. Chem. Biol. 8 (2004) 169-174
5. 2O. Biochemistry 32 (1993) 11878-11885
6. Damaschun G., Damaschun H., Gast K., Zirwer D., and Bychkova V.E. Solvent dependence of dimensions of unfolded protein chains. Int. J. Biol. Macromol. 13 (1991) 217-221
7. Ohgushi M., and Wada A. 'Molten-globule state': a compact form of globular proteins with mobile side-chains. FEBS Lett. 164 (1983) 21-24
8. Goto Y., Calciano L.J., and Fink A.L. Acid-induced folding of proteins. Proc. Natl. Acad. Sci. U S A. 87 (1990) 573-577
9. Kataoka M., Hagihara Y., Mihara K., and Goto Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229 (1993) 591-596
10. Hamada D., Kidokoro S., Fukada H., Takahashi K., and Goto Y. Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl. Acad. Sci. U S A. 91 (1994) 10325-10329
11. Davis-Searles P.R., Morar A.S., Saunders A.J., Erie D.A., and Pielak G.J. Sugar-induced molten-globule model. Biochemistry. 37 (1998) 17048-17053
12. Kamiyama T., Sadahide Y., Nogusa Y., and Gekko K. Polyol-induced molten globule of cytochrome c: an evidence for stabilization by hydrophobic interaction. Biochim. Biophys. Acta. 1434 (1999) 44-57
13. Sedlák E. Characterization of the polyanion-induced molten globule-like state of cytochrome c. Biopolymers 86 (2007) 119-126
14. Hamada D., Kuroda Y., Kataoka M., Aimoto S., Yoshimura T., and Goto Y. Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J.Mol.Biol. 256 (1996) 172-186
15. Hagihara Y., Tan Y., and Goto Y. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effect of acetylation, heat, urea and guanidine-hydrochloride. J. Mol. Biol. 237 (1994) 336-348
16. Margoliash E., and Frohwirt N. Appendix-spectrum of horse-heart cytochrome c. Biochem. J. 71 (1959) 570-572
17. Sreenathan B.R., and Taylor C.P.S. The insensitivity of the 695 nm band of horse heart ferricytochrome c to protein conformation. Biochem. Biophys. Res. Commun. 42 (1971) 1122-1126
18. Shechter E., and Saludjian P. Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformation. Biopolymers 5 (1967) 788-790
19. Palmer G. The electron paramagnetic resonance of metalloproteins. Biochem. Soc. Trans. 13 (1985) 548-560
20. Blumberg W.E., and Peisach J. Low-spin compounds of heme proteins. In: Dessy R., Willard J., and Taylor L. (Eds). Bioinorganic Chemistry. Advances in Chemistry Series Vol. 100 (1971) 271
21. Ikeda-Saito M., Hori H., Andersson L.A., Prince R.C., Pickering I.J., George G.N., Sanders Jr. C.R., Lutz R.S., McKelvey E.J., and Mattera R. Coordination structure of the ferric heme iron in the engineered distal histidine myoglobin mutants. J. Biol. Chem. 267 (1992) 22843-22852
22. Goto Y., Takahashi N., and Fink A.L. Mechanism of acid-induced folding of proteins. Biochemistry 29 (1990) 3480-3488
23. Chen Y.H., Yang J.T., and Chau K.H. Determination of the helix and β form of protein in aqueous solution by circular dichroism. Biochemistry 13 (1974) 3350-3359
24. Polverino de Laureto P., Frare E., Gottardo R., van Dael H., and Fontana A. Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Sci. 11 (2002) 2932-2946
25. Chen Y.H., Yang J.T., and Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry. 11 (1972) 4120-4131
26. Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51 (1998) 355-432
27. Kuroda Y., Kidokoro S., and Wada A. Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process. J. Mol. Biol. 223 (1992) 1139-1153
28. Saunders A.J., Davis-Searles P.R., Allen D.L., Pielak G.J., and Erie D.A. Osmolyte-induced changes in protein conformational equilibria. Biopolymers 53 (2000) 293-307
29. Santucci R., Polizio F., and Desideri A. Formation of a molten-globule-like state of cytochrome c induced by high concentrations of glycerol. Biochimie. 81 (1999) 745-751
30. Qureshi S.H., Moza B., Yadav S., and Ahmad F. Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes c by weak salt denaturants. Biochemistry 42 (2003) 1684-1695
31. Nakamura S., and Kidokoro S. Direct observation of the enthalpy change accompanying the native to molten globule transition of cytochrome c by using isothermal acid-titration calorimetry. Biophys. Chemist. 113 (2005) 161-168
32. Myer Y.P., and Saturno A.F. Horse heart ferricytochrome c: conformation and heme configuration of low ionic strength acidic forms. J. Protein Chem. 9 (1990) 379-387
33. Yoshimura T., Suzuki S., Nakahara A., Iwasaki H., Masuko M., and Matsubara T. Identification of heme axial ligands of cytochrome c ́ from Alcaligenes sp. N.C.I.B. 11015. Biochim. Biophys. Acta 831 (1985) 267-274
34. Stupák M., Bágeľová J., Fedunová D., and Antalík M. Conformational transitions of ferricytochrome c in strong inorganic acids. Coll. Czechoslov. Chem. Commun. 71 (2006) 1627-1641
35. Bren K.L., and Gray H.B. Structurally engineered cytochromes with novel ligand-binding sites: oxy and carbon monoxy derivates of semisynthetic horse heart Ala80 cytochrome c. J. Am. Chem. Soc. 115 (1993) 10382-10383
36. Quillin M.L., Li T., Olson J.S., Phillips Jr. G.N., Dou Y., Ikeda-Saito M., Regan R., Carlson M., Gibson Q.H., Li H., and Elber R. Structural and functional effects of apolar mutations of the distal valine in myoglobin. J. Mol. Biol. 245 (1995) 416-436
37. Goto Y., and Nishikori S. Role of electrostatic repulsion in the acidic molten globule of cytochrome c. J. Mol. Biol. 222 (1991) 679-686