Structural changes of horse heart ferricytochrome c induced by changes of ionic strength and anion binding

Biochemistry

Volumn 47, Issue 18, 2008, Pages 5250-5257

  Shah, Ronak ^a,b   Schweitzer Stenner, Reinhard ^a,b  

^a DREXEL UNIVERSITY   (United States)

^b Department of Chemistry ^*

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHARGE TRANSFER; FUNCTIONAL GROUPS; IONIC STRENGTH; MOLECULAR STRUCTURE;

ANION BINDING; FERRICYTOCHROME; SODIUM ACETATE;

PROTEINS;

ACETIC ACID; ANION; CYTOCHROME C; HEME; IRON; OXYGEN DERIVATIVE; SODIUM DIHYDROGEN PHOSPHATE; SOLVENT;

ABSORPTION; ARTICLE; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); HYDROGEN BOND; IONIC STRENGTH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; ANIONS; CIRCULAR DICHROISM; CYTOCHROMES C; HORSES; MYOCARDIUM; OSMOLAR CONCENTRATION; PROTEIN BINDING; SPECTROPHOTOMETRY;

EQUIDAE;

EID: 42949105053     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702492n     Document Type: Article

References (36)

1. Moore, G. W., and Pettigrew, G. W. (1990) Cytochrome c's Evolutionary, Structural and Physicochemical Aspects, Springer, Berlin, Germany.
2. Lyubovitsky, J. G., Gray, H. B., and Winkler, J. R. (2002) Mapping the cytochrome c folding landscape. J. Am. Chem. Soc. 124, 5481-5485.
3. Pletneva, E. V., Gray, H. B., and Winkler, J. R. (2005) Snapshots of cytochrome c folding. Proc. Natl. Acad. Sci. U.S.A. 102, 18397-18402.
4. Latypov, R. F., Cheng, H., Roder, N., Zhang, A., and Roder, H. (2006) Structural characterization of an equilibrium unfolding intermediate in cytochrome c. J. Mol. Biol. 357, 1009-1025.
5. Battistuzzi, G., Loschi, L., Borsari, M., and Sola, M. (1999) Effects of nonspecific ion-protein interactions of the redox chemistry of cytochrome c. J. Biol. Inorg. Chem. 4, 601-607.
6. Battistuzzi, G., Borsari, M., Dallari, D., Lancellotti, I., and Sola, M. (1996) Anion binding to mitochondrial cytochromes c studied through electrochemistry. Effects of the neutralization of surface charges on the redox potential. Eur. J. Biochem. 241, 208-214.
7. Sanishvili, R., Volz, K. W., Westbrook, E. M., and Margoliash, E. (1995) The low ionic strength crystal structure of horsed cytochrome c at 2.1 Å resolution and comparison with its high ionic strength counterpart. Structure 3, 707-716.
8. Feng, Y., and Englander, S. W. (1990) Salt-dependent structure change and ion binding in cytochrome c studied by two-dimensional proton NMR. Biochemistry 29, 3505-3509.
9. Moench, S. J., Shi, T., and Satterlee, J. D. (1991) Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c. Eur. J. Biochem. 197, 631-641.
10. Trewhella, J., Carlson, V., Curtis, E. H., and Heidorn, D. B. (1988) Differences in the solution structures of oxidized and reduced cytochrome c measured by small-angle X-ray scattering. Biochemistry 27, 1121-1125.
11. Liu, G., Grygon, C. A., and Spiro, T. G. (1989) Ionic strength dependence of cytochrome c structure and Trp-59 H/D exchange from ultraviolet resonance Raman spectroscopy. Biochemistry 28, 5046-5050.
12. Battistuzzi, G., Borsari, M., Ranieri, A., and Sola, M. (2001) Effects of specific anion-protein binding on the alkaline transition of cytochrome c. Arch. Biochem. Biophys. 386, 117-122.
13. Silkstone, G. G., Cooper, C. E., Svistunenko, D., and Wilson, M. T. (2005) EPR and optical spectroscopic studies of Met80X mutants of yeast Ferricytochrome c. Models for intermediates in the alkaline transition. J. Am. Chem. Soc. 127, 92-99.
14. Tezcan, F. A., Winkler, J. R., and Gray, H. B. (1998) Effects of ligation and folding on reduction potentials of heme proteins. J. Am. Chem. Soc. 120, 13383-13388.
15. Eaton, W., and Hochstrasser, R. M. (1968) Single crystal spectra of ferricytochrome c. J. Chem. Phys. 49, 985-995.
16. Makinen, M. V., and Churg, A. K. (1983) Structural and analytical aspects of the electronic spectra of hemeproteins, in Iron Porphyrins, Vol. 1, pp 141-235 (Lever, A. B. P., and Gray, H., Eds.) Addison and Wesley, Reading, U.K.
17. McKnight, J., Cheesman, M. R., Thomson, A. J., Miles, J. S., and Munro, A. W. (1993) Identification of the charge transfer transitions in the optical spectrum of low-spin ferri-cytochrome P-450 Bacillus megaterium. Eur. J. Biochem 213, 683-687.
18. Schejter, A., and George, P. (1964) The 695 μm band of ferricytochrome c and its relationship to protein conformation. Biochemistry 3, 1045-1049.
19. Kaminsky, L. S., Miller, V. L., and Davison, A. J. (1973) Thermodynamic studies of the heme crevice of ferrocytochrome c. Biochemistry 12, 2215-2221.
20. Schweitzer-Stenner, R., Shah, R., Hagarman, A., and Dragomir, I. (2007) Conformational substates of horse heart cytochrome c exhibit different thermal unfolding of the heme cavity. J. Phys. Chem. B 111, 9603-9607.
21. Dragomir, I., Hagarman, A., Wallace, C., and Schweitzer-Stenner, R. (2007) Optical band splitting and electronic perturbations of the heme chromophore in cytochrome c at room temperature probed by visible electronic circular dichroism spectroscopy. Biophys. J. 92, 989-998.
22. Manas, E. S., Vanderkooi, J. M., and Sharp, K. A. (1999) The effects of protein environment on the low temperature electronic spectroscopy of cytochrome c and microperoxidase-11. J. Phys. Chem. 103, 6344-6348.
23. Schweitzer-Stenner, R, Gorden, J. P., and Hagarman, A. (2007) The asymmetric band profile of the Soret band of deoxymyoglobin is caused by electronic and vibronic perturbations of the heme group rather than by a doming deformation. J. Chem. Phys. 127, 135103.
24. Salmeen, I., and Palmerand, G. (1968) Electron paramagnetic resonance of beef-heart ferricytochrome c. J. Chem. Phys. 48, 2049-2052.
25. Droghetti, E., Oellerich, S., Hildebrandt, P., and Smulevich, G. (2006) Heme coordination states of unfolded ferrous cytochrome c. Biophys. J. 91, 3022-3031.
26. Marti, M. A., Scherlis, D. A., Doctorovich, F. A., Ordejon, P., and and Estrin, D. A. (2003) Modulation of the NO trans effect in heme proteins: Implications for the activation of soluble guanylate cyclase. J. Biol. Inorg. Chem. 8, 595-600.
27. Hsu, M., and Woody, R. W. (1971) The origin of the heme cotton effects in myoglobin and hemoglobin. J. Am. Chem. Soc. 93, 3515-3525.
28. Blauer, G., Sreeama, N., and Woody, R. W. (1993) Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution. Biochemistry 32, 66774-6679.
29. Berghuis, A. M., and Brayer, G. D. (1992) Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223, 959-976.
30. Osherhoff, N., Borden, D., Koppenol, W. H., and Margoliash, E. (1980) Electrostatic interactions in cytochrome c. The role of interactions between residues 13 and 90 and residues 79 and 47 in stabilizing the heme crevice structure. J. Biol. Chem. 255, 1689-1697.
31. Berghuis, A. M., Guillemette, J. G., McLendon, G., Sherman, F., Smith, M., and Brayer, G. D. (1994) Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment. J. Mol. Biol. 236, 786-799.
32. Margoliash, E., and Schejter, A. (1966) Cytochrome c. Adv. Protein Chem. 21, 113-286.
33. Englander, S. W., Sosnick, T. R., Mayne, L. C., Shtilerman, M., Phoebe, X. Q., and Bai, Y. (1998) Fast and slow folding in cytochrome c. Acc. Chem. Res. 31, 737-744.
34. Krishna, M. M. G., Maity, H., Rumbley, J. N., Lin, Y., and Englander, S. W. (2006) Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. J. Mol. Biol. 359, 1410-1419.
35. Belikova, N. A., Vladimirov, Y. A., Osipov, A. N., Kapralov, A. A., Tyurin, V. A., Potapovich, M. V., Basova, L. V., Peterson, J., Kumikov, I. V., and Kagan, V. E. (2006) Peroxidase activity and structural transitions of cytochrome c bound to cardiolipin-containing membranes. Biochemistry 45, 4998-5009.
36. Battistuzzi, G., Borsari, M., and Sola, M. (2001) Medium and temperature effects on the redox chemistry of cytochrome c. Eur. J. Inorg. Chem. 2889-3004.