Determination of the pK for the Acid-Induced Denaturation of Ferrocytochrome c

Biochemistry

Volumn 43, Issue 12, 2004, Pages 3564-3569

  Varhač, Rastislav ^a   Antalík, Marián ^a,b  

^a INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^b P J AFÁRIK UNIVERSITY   (Slovakia)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; ACIDITY; CONFORMATIONS; EXTRAPOLATION; OPTICAL PROPERTIES;

ACIDIC CONDITIONS; ZERO DENATURANT CONCENTRATION;

IRON COMPOUNDS;

CYTOCHROME C; IRON SULFUR PROTEIN; UREA;

ABSORPTION SPECTROSCOPY; ACIDITY; ANIMAL CELL; ARTICLE; CHEMICAL BINDING; CHEMICAL MODEL; CHEMICAL STRUCTURE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DENATURATION; ENZYME DENATURATION; HEART; HORSE; LINEAR EXTRAPOLATION; LINEAR SYSTEM; MATHEMATICAL ANALYSIS; MATHEMATICAL COMPUTING; NONHUMAN; PKA; PRIORITY JOURNAL;

ANIMALS; CYTOCHROME C GROUP; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HORSES; HYDROCHLORIC ACID; HYDROGEN-ION CONCENTRATION; MYOCARDIUM; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROPHOTOMETRY, ULTRAVIOLET; UREA;

ANIMALIA; EQUUS CABALLUS;

EID: 1642294585     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036011x     Document Type: Article

References (54)

1. Butt, W. D., and Keilin D. (1962) Absorption spectra and some other properties of cytochrome c and of its compounds with ligands. Proc. R. Soc. London Ser. B 156, 429-458.
2. George, P., and Schejter, A. (1964) The reactivity of ferrocytochrome c with iron-binding ligands. J. Biol. Chem. 239, 1504-1508.
3. Moore, T. A., Greenwood, C., and Wilson, M. T. (1975) Ligand binding to ferrocytochrome c at high pH. Biochem. J. 147, 335-341.
4. Moore, G. R., and Williams, R. J. (1980) Nuclear-magnetic-resonance studies of ferrocytochrome c. pH and temperature dependence. Eur. J. Biochem. 103, 513-521.
5. 1 and of their interactions with phospholipids. Biochim. Biophys. Acta 736, 226-234.
6. Hilgen-Willis, S., Bowden, E. F., and Pielak, G. J. (1993) Dramatic stabilization of ferricytochrome c upon reduction. J. Inorg. Biochem. 51, 649-653.
7. Pascher, T., Chesick, J. P., Winkler, J. R., and Gray, H. B. (1996) Protein folding triggered by electron transfer. Science 271, 1558-1560.
8. Bágel'ová, J., Antalík, M., and Tomori, Z. (1997) Effect of polyglutamate on the thermal stability of ferricytochrome c. Biochem. Mol. Biol. Int. 43, 891-900.
9. Santucci, R., Giartosio, A., and Ascoli, F. (1989) Structural transitions of carboxymethylated cytochrome c: calorimetric and circular dichroic studies. Arch. Biochem. Biophys. 275, 496-504.
10. Myer, Y. P. (1968) Conformation of cytochromes. III. Effect of urea, temperature, extrinsic ligands, and pH variation on the conformation of horse heart ferricytochrome c. Biochemistry 7, 765-776.
11. Myer, Y. P., MacDonald, L. H., Verma, B. C., and Pande, A. (1980) Urea denaturation of horse heart ferricytochrome c. Equilibrium studies and characterization of intermediate forms. Biochemistry 19, 199-207.
12. Hagihara, Y., Tan, Y., and Goto, Y. (1994) Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride. J. Mol. Biol. 237, 336-348.
13. Varhač, R., Antalík, M., and Bánó, M. (2004) Effect of temperature and guanidine hydrochloride on ferrocytochrome c at neutral pH. J. Biol. Inorg. Chem. 9, 12-22.
14. Bixler, J., Bakker, G., and McLendon, G. (1992) Electrochemical probes of protein folding. J. Am. Chem. Soc. 114, 6938-6939.
15. Thomas, Y. G., Goldbeck, R. A., and Kliger, D. S. (2000) Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies. Biopolymers 57, 29-36.
16. Bhuyan, A. K., and Udgaonkar, J. B. (2001) Folding of horse cytochrome c in the reduced state. J. Mol. Biol. 312, 1135-1160.
17. Hamada, D., Kuroda, Y., Kataoka, M., Aimoto, S., Yoshimura, T., and Goto, Y. (1996) Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J. Mol. Biol. 256, 172-186.
18. Brumer, P., Levine, W. G., and Peisach, J. (1966) Some properties of denatured horse heart cytochrome c. Arch. Biochem. Biophys. 117, 232-238.
19. Kurihara, M., and Sano, S. (1970) Reduction of cytochrome c by ferrous ions and ethylenediaminetetraacetic acid in acid solution. J. Biol. Chem. 245, 4804-4806.
20. Lambeth, D. O., Campbell, K. L., Zand, R., and Palmer, G. (1973) The appearance of transient species of cytochrome c upon rapid oxidation or reduction at alkaline pH. J. Biol. Chem. 248, 8130-8136.
21. Yoshimura, T. (1988) A change in the heme stereochemistry of cytochrome c upon addition of sodium dodecyl sulfate: electron paramagnetic resonance and electronic absorption spectral study. Arch. Biochem. Biophys. 264, 450-461.
22. Churg, A. K., and Warshel, A. (1986) Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins. Biochemistry 25, 1675-1681.
23. Cohen, D. S., and Pielak, G. J. (1995) Entropic stabilization of cytochrome c upon reduction. J. Am. Chem. Soc. 117, 1675-1677.
24. Schejter, A., and Plotkin, B. (1988) The binding characteristics of the cytochrome c iron. Biochem. J. 255, 353-356.
25. Cheng, M.-C., Rich, A. M., Armstrong, R. S., Ellis, P. J., and Lay, P. A. (1999) Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple-scattering analyses of XAFS data. Inorg. Chem. 38, 5703-5708.
26. Viola, F., Aime, S., Coletta, M., Desideri, A., Fasano, M., Paoletti, S., Tarricone, C., and Ascenzi, P. (1996) Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a comparative study. J. Inorg. Biochem. 62, 213-222.
27. Theorell, H., and Åkesson, Å. (1941) Studies on cytochrome c. II. The optical properties of pure cytochrome c and some of its derivatives. J. Am. Chem. Soc. 63, 1812-1818.
28. Barker, P. D., and Mauk, A. G. (1992) pH-linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: electrochemical analysis of the alkaline form of cytochrome c. J. Am. Chem. Soc. 114, 3619-3624.
29. Battistuzzi, G., Borsari, M., Loschi, L., Martinelli, A., and Sola, M. (1999) Thermodynamics of the alkaline transition of cytochrome c. Biochemistry 38, 7900-7907.
30. McLendon, G., and Smith, M. (1978) Equilibrium and kinetic studies of unfolding of homologous cytochromes c. J. Biol. Chem. 253, 4004-4008.
31. Goto, Y., Calciano, L. J., and Fink, A. L. (1990) Acid-induced folding of proteins. Proc. Natl. Acad. Sci. U.S.A. 87, 573-577.
32. Tsong, T. Y. (1975) An acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutions. Biochemistry 14, 1542-1547.
33. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
34. Acevedo, O., Guzman-Casado, M., Garcia-Mira, M. M., Ibarra-Molero, B., and Sanchez-Ruiz, J. M. (2002) pH corrections in chemical denaturant solutions. Anal. Biochem. 306, 158-161.
35. Margoliash, E., and Frohwirt, N. (1959) Spectrum of horse-heart cytochrome c. Biochem. J. 71, 570-572.
36. Myer, Y. P., and Saturno, A. F. (1990) Horse heart ferricytochrome c: conformation and heme configuration of low ionic strength acidic forms. J. Protein Chem. 9, 379-387.
37. Stellwagen, E. (1968) The reversible unfolding of horse heart ferricytochrome c. Biochemistry 7, 2893-2898.
38. Telford, J. R., Tezcan, F. A., Gray, H. B., and Winkler, J. R. (1999) Role of ligand substitution in ferrocytochrome c folding. Biochemistry 38, 1944-1949.
39. Dickerson, R. E., Takano, T., Eisenberg, D., Kallai, O. B., Samson, L., Cooper, A., and Margoliash, E. (1971) Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 Å resolution. J. Biol. Chem. 246, 1511-1535.
40. Harbury, H. A., Cronin, J. R., Fanger, M. W., Hettinger, T. P., Murphy, A. J., Myer, Y. P., and Vinogradov, S. N. (1965) Complex formation between methionine and a heme peptide from cytochrome c. Proc. Natl. Acad. Sci. U.S.A. 54, 1658-1664.
41. Babul, J., and Stellwagen, E. (1972) Participation of the protein ligands in the folding of cytochrome c. Biochemistry 11, 1195-1200.
42. Lanir, A., Yu, N. T., and Felton, R. H. (1979) Conformational transitions and vibronic couplings in acid ferricytochrome c: a resonance Raman study. Biochemistry 18, 1656-1660.
43. Dyson, H. J., and Beattie, J. K. (1982) Spin state and unfolding equilibria of ferricytochrome c in acidic solutions. J. Biol. Chem. 257, 2267-2273.
44. Oellerich, S., Wackerbarth, H., and Hildebrandt, P. (2002) Spectroscopic characterization of nonnative conformational states of cytochrome c. J. Phys. Chem. B 106, 6566-6580.
45. Moore, G. R., and Pettigrew, G. W. (1990) Cytochromes c: Evolutionary, Structural and Physicochemical Aspects, Springer-Verlag, Berlin.
46. Corradin, G., and Harbury, H. A. (1971) Reconstitution of horse heart cytochrome c: interaction of the components obtained upon cleavage of the peptide bond following methionine residue 65. Proc. Natl. Acad. Sci. U.S.A. 68, 3036-3039.
47. Yoshimura, T., Fujii, S., Kamada, H., Yamaguchi, K., Suzuki, S., Shidara, S., and Takakuwa, S. (1996) Spectroscopic characterization of nitrosylheme in nitric oxide complexes of ferric and ferrous cytochrome c′ from photosynthetic bacteria, Biochim. Biophys. Acta 1292, 39-46.
48. Ibarra-Molero, B., Loladze, V. V., Makhatadze, G. I., and Sanchez-Ruiz, J. M. (1999) Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 38, 8138-8149.
49. Russell, B. S., Melenkivitz, R., and Bren, K. L. (2000) NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state. Proc. Natl. Acad. Sci. U.S.A. 97, 8312-8317.
50. Muthukrishnan, K., and Nall, B. T. (1991) Effective concentrations of amino acid side chains in an unfolded protein. Biochemistry 30, 4706-4710.
51. Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T., and Palleros, D. R. (1994) Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33, 12504-12511.
52. Myer, Y. P., and Satumo, A. F. (1991) Horse heart ferricytochrome c: conformation and heme configuration of high ionic strength acidic forms. J. Protein Chem. 10, 481-494.
53. Sedlák, E., and Antalík, M. (2002) Effect of polyanion on the acidic conformational transition of native and denatured ferricytochrome c. Circular dichroism study. Gen. Physiol. Biophys. 21, 175-188.
54. Godbole, S., and Bowler, B. E. (1997) A histidine variant of yeast iso-1-cytochrome c that strongly affects the energetics of the denatured state. J. Mol. Biol. 268, 816-821.