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Abstract:

Time-resolved surface enhanced infrared absorption (SEIRA) spectroscopy is employed to analyse the dynamics of the protein structural changes coupled to the electron transfer process of immobilised cytochrome c (Cyt-c). Upon electrostatic binding of Cyt-c to Au electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated thiols, cyclic voltammetric measurements demonstrate a reversible redox process with a redox potential that is similar to that of Cyt-c in solution, and a non-exponential distance-dependence of the electron transfer rate as observed previously (D. H. Murgida and P. Hildebrandt, Chem. Soc. Rev. 2008, 37, 937). On the basis of characteristic redox-state-sensitive amide I bands, the protein structural changes triggered by the electron transfer are monitored by rapid scan and step scan SEIRA spectroscopy in combination with the potential jump technique. Whereas the temporal evolution of the conjugate bands at 1693 and 1673 cm -1 displays the same rate constants as electron transfer, the time-dependent changes of the 1660-cm-1 band are slower by about a factor of 2. The study demonstrates that time-resolved SEIRA spectroscopy provides further information about the dynamics and mechanism of interfacial processes of redox proteins, thereby complementing the results obtained from other surface-sensitive techniques. In comparison with previous surface enhanced resonance Raman spectroscopic findings, the present results are discussed in terms of the local electric field strengths at the Au/SAM/Cyt-c interface.

Registro:

Documento: Artículo
Título:Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
Autor:Wisitruangsakul, N.; Zebger, I.; Ly, K.H.; Murgida, D.H.; Ekgasit, S.; Hildebrandt, P.
Filiación:Technische Universität Berlin, Institut für Chemie, Sekr. PC 14 Straße des 17. Juni 135, D-10623 Berlin, Germany
Departamento de Química Inorgánica, Analítica Y Química Física/INQUIMAE-CONICET, Ciudad Universitaria, Pab. 2, Buenos Aires C1428EHA, Argentina
Department of Chemistry, Faculty of Science, Chulalongkorn University, Phayathai Road, Patumwan, Bangkok 10330, Thailand
Palabras clave:cytochrome c; cytochrome c''; animal; article; chemistry; horse; infrared spectrophotometry; metabolism; methodology; oxidation reduction reaction; Animals; Cytochrome c Group; Horses; Oxidation-Reduction; Spectrophotometry, Infrared
Año:2008
Volumen:10
Número:34
Página de inicio:5276
Página de fin:5286
DOI: http://dx.doi.org/10.1039/b806528d
Título revista:Physical Chemistry Chemical Physics
Título revista abreviado:Phys. Chem. Chem. Phys.
ISSN:14639076
CODEN:PPCPF
CAS:cytochrome c, 9007-43-6, 9064-84-0; Cytochrome c Group; cytochrome c'', 116110-46-4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v10_n34_p5276_Wisitruangsakul

Referencias:

  • (2005) Bioelectronics-From Theory to Applications, Ed., , I. Willner and E. Katz, Wiley-VCH, Weinheim, 1st edn
  • Siebert, F., Hildebrandt, P., (2008) Vibrational Spectroscopy in Life Science, , Wiley-VCH, Weinheim, 1st edn
  • Murgida, D.H., Hildebrandt, P., (2005) Phys. Chem. Chem. Phys., 7, p. 3773
  • Murgida, D.H., Hildebrandt, P., (2008) Chem. Soc. Rev., 37, p. 937
  • Smulevich, G., Spiro, T.G., (1985) J. Phys. Chem., 89, p. 5168
  • Ataka, K., Heberle, J., (2004) J. Am. Chem. Soc., 126, p. 9445
  • Ataka, K., Giess, F., Knoll, W., Naumann, R., Haber-Pohlmeier, S., Richter, B., Heberle, J., (2004) J. Am. Chem. Soc., 126, p. 16199
  • Ataka, K., Heberle, J., (2007) Anal. Bioanal. Chem., 388, p. 47
  • Miyake, H., Ye, S., Osawa, M., (2002) Electrochem. Commun., 4, p. 973
  • Murgida, D.H., Hildebrandt, P., (2001) J. Phys. Chem. B, 105, p. 1578
  • Murgida, D.H., Hildebrandt, P., (2001) J. Am. Chem. Soc., 123, p. 4062
  • Moss, D., Nabedryk, E., Breton, J., Mantele, W., (1990) Eur. J. Biochem., 187, p. 565
  • Schlereth, D.D., Mantele, W., (1992) Biochemistry, 31, p. 7494
  • Dong, A., Huang, P., Caughey, W.S., (1992) Biochemistry, 31, p. 182
  • Susi, H., Byler, D.M., (1983) Biochem. Biophys. Res. Commun., 115, p. 391
  • Song, S., Clark, R.A., Bowden, E.F., Tarlov, M.J., (1993) J. Phys. Chem., 97, p. 6564
  • Clark, R.A., Bowden, E.F., (1997) Langmuir, 13, p. 559
  • Eddowes, M.J., Hill, H.A.O., (1979) J. Am. Chem. Soc., 101, p. 4461
  • Laviron, E., (1979) J. Electroanal. Chem., 101, p. 19
  • Leopold, M.C., Black, J.A., Bowden, E.F., (2002) Langmuir, 18, p. 978
  • Berghuis, A.M., Brayer, G.D., (1992) J. Mol. Biol., 223, p. 959
  • Feng, Z.Q., Imabayashi, S., Kakiuchi, T., Niki, K., (1997) J. Chem. Soc., Faraday Trans., 93, p. 1367
  • De Groot, M.T., Merkx, M., Koper, M.T.M., (2007) Langmuir, 23, p. 3832
  • Avila, A., Gregory, B.W., Niki, K., Cotton, T.M., (2000) J. Phys. Chem. B, 104, p. 2759
  • Yue, H.J., Khoshtariya, D., Waldeck, D.H., Grochol, J., Hildebrandt, P., Murgida, D.H., (2006) J. Phys. Chem. B, 110, p. 19906
  • Wei, J.J., Liu, H.Y., Dick, A.R., Yamamoto, H., He, Y.F., Waldeck, D.H., (2002) J. Am. Chem. Soc., 124, p. 9591
  • Dolidze, T.D., Rondinini, S., Verto-Va, A., Waldeck, D.H., Khoshtariya, D.E., (2007) Biopolymers, 87, p. 68
  • Kranich, A., Ly, K.H., Hildebrandt, P., Murgida, D.H., (2008) J. Am. Chem. Soc., , in press
  • Koppenol, W.H., Rush, J.D., Mills, J.D., Margoliash, E., (1991) Mol. Biol. Evol., 8, p. 545
  • Smith, C.P., White, H.S., (1992) Anal. Chem., 64, p. 2398
  • Valette, G., Hamelin, A., (1973) J. Electroanal. Chem., 45, p. 301
  • Shlepakov, A.V., Sevastyanov, E.S., (1978) Sov. Electrochem., 14, p. 243
  • Ramirez, P., Andreu, R., Cuesta, A., Calzado, C.J., Calvente, J.J., (2007) Anal. Chem., 79, p. 6473
  • Hamelin, A., (1983) J. Electroanal. Chem., 144, p. 365
  • Walczak, M.M., Chung, C.K., Stole, S.M., Widrig, C.A., Porter, M.D., (1991) J. Am. Chem. Soc., 113, p. 2370
  • Love, J.C., Estroff, L.A., Kriebel, J.K., Nuzzo, R.G., Whitesides, G.M., (2005) Chem. Rev., 105, p. 1103
  • Laibinis, P.E., Whitesides, G.M., Allara, D.L., Tao, Y.T., Parikh, A.N., Nuzzo, R.G., (1991) J. Am. Chem. Soc., 113, p. 7152
  • Bain, C.D., Troughton, E.B., Tao, Y.T., Evall, J., Whitesides, G.M., Nuzzo, R.G., (1989) J. Am. Chem. Soc., 111, p. 321

Citas:

---------- APA ----------
Wisitruangsakul, N., Zebger, I., Ly, K.H., Murgida, D.H., Ekgasit, S. & Hildebrandt, P. (2008) . Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy. Physical Chemistry Chemical Physics, 10(34), 5276-5286.
http://dx.doi.org/10.1039/b806528d
---------- CHICAGO ----------
Wisitruangsakul, N., Zebger, I., Ly, K.H., Murgida, D.H., Ekgasit, S., Hildebrandt, P. "Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy" . Physical Chemistry Chemical Physics 10, no. 34 (2008) : 5276-5286.
http://dx.doi.org/10.1039/b806528d
---------- MLA ----------
Wisitruangsakul, N., Zebger, I., Ly, K.H., Murgida, D.H., Ekgasit, S., Hildebrandt, P. "Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy" . Physical Chemistry Chemical Physics, vol. 10, no. 34, 2008, pp. 5276-5286.
http://dx.doi.org/10.1039/b806528d
---------- VANCOUVER ----------
Wisitruangsakul, N., Zebger, I., Ly, K.H., Murgida, D.H., Ekgasit, S., Hildebrandt, P. Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy. Phys. Chem. Chem. Phys. 2008;10(34):5276-5286.
http://dx.doi.org/10.1039/b806528d