Cytochrome c and SDS: A Molten Globule Protein with Altered Axial Ligation

Journal of Molecular Biology

Volumn 336, Issue 2, 2004, Pages 489-496

  Bertini, Ivano ^a   Turano, Paola ^a   Vasos, Paul R ^a   Bondon, Arnaud ^b   Chevance, Soizic ^b   Simonneaux, Gérard ^b  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UMR 6509 Organometalliques et Catalyse Chimie et Electrochimie Moleculaires   (France)

Author keywords

Cytochrome c; Metal coordination; NMR spectroscopy; Protein unfolding; SDS

Indexed keywords

AMIDE; CYTOCHROME C; DODECYL SULFATE SODIUM; FUNGAL ENZYME; GLOBULAR PROTEIN; METHIONINE; WATER;

ARTICLE; DATA ANALYSIS; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVATION; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; SACCHAROMYCES CEREVISIAE; VISCOSITY;

EQUUS CABALLUS;

EID: 0742272140     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.12.045     Document Type: Article

References (37)

1. Cortese J.D., Voglino A.L., Hackenbrock C.R. Persistence of cytochrome c binding to membranes at physiological mitochondrial intermembrane space ionic strength. Biochim. Biophys. Acta. 1228:1995;216-228.
2. Döpner S., Hildebrandt P., Rosell F.I., Mauk A.G., Soulimane T., Bouse G. The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase. Eur. J. Biochem. 261:1999;379-391.
3. Jemmerson R., Liu J., Hausauer D., Lam K.-P., Mondino A., Nelson R.D. A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles. Biochemistry. 38:1999;3599-3609.
4. Sedlak E., Antalik M. Molten globule-like state of cytochrome c induced by polyanion poly(vinylsulfate) in slightly acidic pH. Biochim. Biophys. Acta. 1434:1999;347-355.
5. Pinheiro T.J.T. The interaction of horse heart cytochrome c with phospholipid bilayers. Structural and dynamic effects. Biochimie. 76:1994;489-500.
6. Murgida D.H., Hildebrand D.P. Electrostatic-field dependent activation energies modulate electron transfer of cytochrome c. J. Phys. Chem. B. 106:2002;12814-12819.
7. Oellerich S., Wackerbarth H., Hildebrandt P. Spectroscopic characterisation of nonnative conformational states of cytochrome c. J. Phys. Chem. B. 106:2002;6566-6580.
8. Muga A., Mantsch H.H., Surewicz W.K. Membrane binding induces destabilisation of cytochrome c structure. Biochemistry. 30:1991;7219-7224.
9. Das T.K., Mazumdar S., Mitra S. Characterization of a partially unfolded structure of cytochrome c induced by sodium dodecyl sulphate and the kinetics of its refolding. Eur. J. Biochem. 254:1998;662-670.
10. Chottard G., Michelon M., Hervé M., Hervé G. Modification of the structural and redox properties of cytochrome c by heteropolytungstate binding. Biochim. Biophys. Acta. 916:1987;402-410.
11. Hildebrandt P., Stockburger M. Cytochrome c at charged interfaces: 1. Conformational and redox equilibria at the electrode/electrolyte interface probed by surface enhanced resonance Raman spectroscopy. Biochemistry. 28:1989;6710-6721.
12. Elove G.A., Bhuyan A.K., Roder H. Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry. 33:1994;6925-6935.
13. Assfalg M., Bertini I., Dolfi A., Turano P., Mauk A.G., Rosell F.I., Gray H.B. Structural model for an alkaline form of ferricytochrome c. J. Am. Chem. Soc. 125:2003;2913-2922.
14. 1H NMR structural characterization of the cytochrome c modifications in micellar environment. Biochemistry. 42:2003;15342-15351.
15. Russell B.S., Melenkivitz R., Bren K.L. NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state. Proc. Natl Acad. Sci. USA. 97:2000;8312-8317.
16. Muthukrishnan K., Nall B.T. Effective concentrations of amino acid side chains in an unfolded protein. Biochemistry. 30:1991;4706-4710.
17. Smith L.J., Bolin K.A., Schwalbe H., MacArthur M.W., Thornton J.M., Dobson C.M. Analysis of main chain torsion angles in proteins. Prediction of NMR coupling constants for native and denatured conformations. J. Mol. Biol. 255:1996;494-506.
18. Dubins D.N., Filfil R., Macgregor R.B. Jr, Chalikian T.V. Volume and compressibility changes accompanying thermally-induced native-to-unfolded and molten globule-to-unfoled transitions of cytochrome c: a high pressure study. Biochemistry. 42:2003;8671-8678.
19. Bartalesi I., Bertini I., Ghosh K., Rosato A., Turano P. The unfolding of oxidized c-type cytochromes: the instructive case of B. pasteurii. J. Mol. Biol. 321:2002;693-701.
20. 1H residual dipolar coupling analysis of native and alkaline-K79A S. cerevisiae cytochrome c. Biophys. J. 84:2003;3917-3923.
21. Assfalg M., Banci L., Bertini I., Turano P., Vasos P. Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical features. J. Mol. Biol. 330:2003;145-158.
22. 15N relaxation measurements for oxidized and reduced iso-1-cytochrome c. Biochemistry. 38:1999;4480-4492.
23. Aswal V.K., Goyal P.S. Counterions in the growth of ionic micelles in aqueous electrolyte solutions: a small-angle neutron scattering study. Phys. Rev. E. 61:2000;2947-2953.
24. Caetano W., Barbosa L.R.S., Itri R., Tabak M. Trifluoroperazine effects on anionic and zwitterionic micelles: a study by small angle X-ray scattering. J. Colloid Interface Sci. 260:2003;414-422.
25. Viles J.H., Donne D., Kroon G., Prusiner S.B., Cohen F.E., Dyson H.J., Wright P.E. Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. Biochemistry. 40:2001;2743-2753.
26. Wilson A.J., Groves K., Jain R.K., Soon Park H., Hamilton A.D. Direct denaturation: room temperature and stoichiometric unfolding of cytochrome c by a metalloporphyrin dimer. J. Am. Chem. Soc. 125:2003;4420-4421.
27. Bai Y.W., Sosnick T.R., Mayne L., Englander S.W. Protein folding intermediates: native-state hydrogen exchange. Science. 269:1995;192-197.
28. Hoang L., Maity H., Krishna M.M.G., Lin Y., Englander S.W. Folding units govern the cytochrome c alkaline transition. J. Mol. Biol. 331:2003;37-43.
29. Mines G.A., Pascher T., Lee S.C., Winkler J.R., Gray H.B. Cytochrome c folding triggered by electron transfer. Chem. Biol. 3:1996;491-497.
30. Winkler J.R., Wittung-Stafshede P., Leckner J., Malmström B.G., Gray H.B. Effect of folding on metalloprotein active sites. Proc. Natl Acad. Sci. USA. 94:1997;4246-4249.
31. Pollock W.B.R., Rosell F.I., Twitchett M.B., Dumont M.E., Mauk A.G. Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry. 37:1998;6124-6131.
32. Barker P.B., Bertini I., Del Conte R., Ferguson S.J., Hajieva P., Tomlinson E.J., et al. A further clue to understanding the mobility of mitochondrial yeast cytochrome c: a 15N T1p investigation of the oxidized and reduced species. Eur. J. Biochem. 268:2001;4468-4476.
33. Vuister G.W., Bax A. Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNH.alpha.) coupling constants in 15N-enriched proteins. J. Am. Chem. Soc. 115:1993;7772-7777.
34. 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry. 28:1989;8972-8979.
35. Palmer A.G. III, Skelton N.J., Chazin W.J., Wright P.E., Rance M. Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates. Mol. Phys. 75:1992;699-711.
36. 15N relaxation using inverse detected two-dimensional NMR spectroscopy; the central helix is flexible. Biochemistry. 31:1992;5269-5278.
37. 2 values in proteins. J. Magn. Reson. 97:1992;359-375.