Interaction of horse heart and Thermus thermophilus type c cytochromes with phospholipid vesicles and hydrophobic surfaces

Biophysical Journal

Volumn 86, Issue 6, 2004, Pages 3863-3872

  Bernad, Sophie ^a   Oellerich, Silke ^b,e   Soulimane, Tewfik ^c   Noinville, Sylvie ^a   Baron, Marie Hélène ^a   Paternostre, Maité ^d   Lecomte, Sophie ^a  

^a CNRS   (France)

^b MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

^d CEA SACLAY   (France)

^e LEIDEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME C; CYTOCHROME C552; DIOLEOYLPHOSPHATIDYLGLYCEROL; LIPOSOME; OCTADECYLTRICHLOROSILANE; PHOSPHATIDYLGLYCEROL; SILANE DERIVATIVE; UNCLASSIFIED DRUG;

ADSORPTION; ARTICLE; ATTENUATION TOTAL REFLECTION SPECTROSCOPY; BETA SHEET; ELECTRICITY; FLOCCULATION; HEART; HORSE; HYDROPHOBICITY; INFRARED SPECTROSCOPY; NONHUMAN; PHOSPHOLIPID VESICLE; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; REFLECTOMETRY; THERMUS THERMOPHILUS; TURBIDITY;

BACTERIA (MICROORGANISMS); EQUUS CABALLUS; THERMUS; THERMUS THERMOPHILUS;

EID: 2942662207     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.025114     Document Type: Article

References (41)

1. Baron, M. H., C. De Loze, C. Toniolo, and C. D. Fasman. 1978. Structure in solution of protected homo-oligopeptides of L-valine, L-isoleucine, and L-phenylalanine: an infrared adsorption study. Biopolymers. 17:2225-2239.
2. 552 from Thermus thermophilus adsorbed on chemically modified silver electrode probed by surface enhanced resonance Raman spectroscopy. J. Raman Spectr. 35:47-54.
3. 6. Appl. Spectr. 49:1737-1746.
4. Boulkanz, L., C. Vidal-Madjar, N. Balcar, and M. H. Baron. 1997. Adsorption mechanism of human serum albumin on a reversed-phase support by kinetic, chromatographic, and FTIR method. J. Coll. Interf. Sci. 188:58-67.
5. Buschnell, G. W., G. V. Louie, and G. D. Brayer. 1990. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214:585-595.
6. Byler, D. M., and H. Susi. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 25:469-487.
7. Chirgadze, Y. N., O. V. Fedorov, and N. P. Trushina. 1975. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers. 14:679-694.
8. Choi, S., and J. M. Swanson. 1995. Interaction of cytochrome c with cardiolipin: an infrared spectroscopic study. Biophys. Chem. 54:271-278.
9. Cortese, J. D., A. L. Voglino, and C. R. Hackenbrock. 1998. Multiple conformations of physiological membrane-bound cytochrome c. Biochemistry. 37:6402-6409.
10. De Meulenaer, B., P. Van der Meeren, M. De Cuyper, J. Vanderdeelen, and L. Baert. 1997. Electrophoretic and dynamic light scattering study of the interaction of cytochrome c with dimyristoylphosphatidylglycerol, dimyristoylphosphatidylcholine, and intramembranously mixed liposomes. J. Coll. Interf. Sci. 189:254-258.
11. Dong, A., P. Huang, and W. S. Caughed. 1992. Redox-dependent changes in β-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra. Biochemistry. 31:182-189.
12. Goormaghtigh, E., V. Cabiaux, and J. M. Ruysschaert. 1990. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 193:409-420.
13. Heimburg, T., and D. Marsh. 1993. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. Biophys. J. 65:2408-2417.
14. Hellwig, P., T. Soulimane, G. Buse, and W. Mantele. 1999. Electrochemical, FTIR, and UV/VIS spectroscopic properties of the ba3 oxidase from Thermus thermophilus. Biochemistry. 38:9648-9658.
15. Kleinschmidt, J. H., G. L. Powell, and D. Marsh. 1998. Cytochrome c-induced increase of motionally restricted lipid in reconstituted cytochrome c oxidase membranes, revealed by spin-label ESR spectroscopy. Biochemistry. 37:11579-11585.
16. Kostrzewa, A., T. Pali, W. Froncisz, and D. Marsh. 2000. Membrane location of spin-labeled cytochrome c determined by paramagnetic relaxation agents. Biochemistry. 39:6066-6074.
17. 552 from Thermus thermophilus. A time-resolved surface-enhanced resonance Raman spectroscopic study. J. Phys. Chem. B. 103:10053-10064.
18. 552 from Thermus thermophilus adsorbed on anionic and hydrophobic surfaces probed by FTIR and 2D-FTIR spectroscopy. Chem. Biochem. 2:180-189.
19. Lecomte, S., H. Wackerbarth, T. Soulimane, G. Buse, and P. Hildebrandt. 1998. Time-resolved surface-enhanced resonance Raman spectroscopy for studying electron-transfer dynamics of heme proteins. J. Am. Chem. Soc. 120:7381-7382.
20. Lo, Y. L., and Y. E. Rahman. 1998. Effect of lipids on the thermal stability and conformational changes of proteins: ribonuclease A and cytochrome c. Int. J. Pharm. 161:137-148.
21. Morse, P. D., and D. W. Deamer. 1973. Interaction of cytochrome c with lipid monolayers. Biochim. Biophys. Acta. 298:769-782.
22. Muga, A., H. H. Mantsch, and W. K. Surewicz. 1991. Membrane binding induces destabilization of cytochrome c structure. Biochemistry. 30:7219-7224.
23. Noinville, S., M. Revault, M. H. Baron, A. Tiss, S. Yapoudjian, M. Ivanova, and M. R. Verger. 2002. Conformational changes and orientation of humicola lanuginosa lipase on a solid hydrophobic surface: an in situ interface FTIR-ATR study. Biophys. J. 82:2709-2719.
24. Nuzzo, R. G., L. H. Dubois, and D. L. Allara. 1990. Fundamental studies of microscopic wetting on organic surfaces. 1. Formation and structural characterization of a self-consistent series of polyfunctional organic monolayers. J. Am. Chem. Soc. 112:558-569.
25. Oellerich, S., S. Lecomte, M. Paternostre, T. Heimburg, and P. Hildebrandt. 2004. Peripheral and integral binding of cytochrome c to phospholipid vesicles. J. Phys. Chem. B. 108:3871-3878.
26. Paquet, M.-J., M. Laviolette, M. Pezolet, and M. Auger. 2001. Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol. Biophys. J. 81:305-312.
27. Pinheiro, T. J. T. 1994. The interaction of horse heart cytochrome c with phospholipid bilayers. Structural and dynamic effects. Biochimie. 76:489-500.
28. 31P NMR. Biochemistry. 33:2451-2458.
29. Pott, T., M. Paternostre, and E. J. Dufourc. 1998. A comparative study of the action of melittin on sphingomyelin and phosphatidylcholine bilayers. Eur. Biophys. J. 27:237-245.
30. Quinn, P. J., and R. M. C. Dawson. 1969. The interaction of cytochrome c with monolayers of phosphatidylethanolamine. Biochem. J. 113:791-803.
31. Rivas, L., D. H. Murgida, and P. Hildebrandt. 2002. Conformational and redox equilibria and dynamics of cytochrome c immobilized on electrodes via hydrophobic interactions. J. Phys. Chem. B. 106:4823-4830.
32. Salamon, Z., and G. Tollin. 1996a. Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase. Biophys. J. 71:848-857.
33. Salamon, Z., and G. Tollin. 1996b. Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. II. Binding cytochrome c to oxidase-containing cardiolipin/phosphatidylcholine membranes. Biophys. J. 71:858-867.
34. 3- cytochrome c oxidase from Thermus thermophilus. EMBO. J. 19:1766-1776.
35. 552 from Thermus thermophilus: a functional and crystallographic investigation. Biochim. Biophys. Res. Com. 237:572-576.
36. Subramanian, M., A. Jutila, and K. J. Kinnunen. 1998. Binding and dissociation of cytochrome c to and from membranes containing acidic phospholipids. Biochemistry. 37:1394-1402.
37. Sukhishvili, S. A., and S. Granick. 1999. Adsorption of human serum albumin: dependence on molecular architecture of the oppositely charged surface. J. Chem. Phys. 110:10153-10161.
38. Surewicz, W. K., and H. H. Mantsch. 1988. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta. 952:115-130.
39. 552: a new highly thermostable cytochrome c structure obtained by MAD phasing. J. Mol. Biol. 271:629-644.
40. Wasserman, S. R., Y.-T. Tao, and G. M. Whitesides. 1989. Structure and reactivity of alkylsiloxane monolayers formed by reaction of alkyltrichlorosilanes on silicon substrates. J. Am. Chem. Soc. 5:1074-1087.
41. Zuckermann, M. J., and T. Heimburg. 2001. Insertion and pore formation driven by adsorption of proteins onto lipid bilayer membrane-water interfaces. Biophys. J. 81:2458-2472.