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Molinas, M.F.; De Candia, A.; Szajnman, S.H.; Rodríguez, J.B.; Martí, M.; Pereira, M.; Teixeira, M.; Todorovic, S.; Murgida, D.H. "Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films" (2011) Physical Chemistry Chemical Physics. 13(40):18088-18098
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Abstract:

The subunit II of the caa 3 oxygen reductase from Rhodothermus marinus contains, in addition to the Cu A center, a c-type heme group in the cytochrome c domain (Cyt-D) that is the putative primary electron acceptor of the enzyme. In this work we have combined surface-enhanced resonance Raman (SERR) spectroelectrochemistry, molecular dynamics (MD) simulations and electron pathway calculations to assess the most likely interaction domains and electron entry/exit points of the truncated Cyt-D of subunit II in the reactions with its electron donor, HiPIP and electron acceptor, Cu A. The results indicate that the transient interaction between Cyt-D and HiPIP relies upon a delicate balance of hydrophobic and polar contacts for establishing an optimized electron transfer pathway that involves the exposed edge of the heme group and guaranties efficient inter-protein electron transfer on the nanosecond time scale. The reorganization energy of ca. 0.7 eV was determined by time-resolved SERR spectroelectrochemistry. The intramolecular electron transfer pathway in integral subunit II from Cyt-D to the Cu A redox center most likely involves the iron ligand histidine 20 as an electron exit point in Cyt-D. © the Owner Societies 2011.

Registro:

Documento: Artículo
Título:Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films
Autor:Molinas, M.F.; De Candia, A.; Szajnman, S.H.; Rodríguez, J.B.; Martí, M.; Pereira, M.; Teixeira, M.; Todorovic, S.; Murgida, D.H.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE (CONICET-UBA), Ciudad Universitaria, Pab. 2 piso 1, C1428EHA-Buenos Aires, Argentina
Departamento de Química Orgánica, UMYMFOR (CONICET-FCEyN), Ciudad Universitaria, Pab. 2 piso 3, C1428EHA-Buenos Aires, Argentina
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República (EAN), 2780-157 Oeiras, Portugal
Palabras clave:cytochrome a; cytochrome c; cytochrome c oxidase; cytochrome caa(3); article; chemistry; electron transport; enzymology; metabolism; molecular dynamics; protein subunit; protein tertiary structure; Raman spectrometry; Rhodothermus; Cytochrome c Group; Cytochromes a; Cytochromes a3; Electron Transport; Molecular Dynamics Simulation; Protein Structure, Tertiary; Protein Subunits; Rhodothermus; Spectrum Analysis, Raman
Año:2011
Volumen:13
Número:40
Página de inicio:18088
Página de fin:18098
DOI: http://dx.doi.org/10.1039/c1cp21925a
Título revista:Physical Chemistry Chemical Physics
Título revista abreviado:Phys. Chem. Chem. Phys.
ISSN:14639076
CODEN:PPCPF
CAS:cytochrome a, 9035-34-1; cytochrome c, 9007-43-6, 9064-84-0; cytochrome c oxidase, 72841-18-0, 9001-16-5; Cytochrome c Group; Cytochromes a, 9035-34-1; Cytochromes a3; Protein Subunits; cytochrome caa(3)
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v13_n40_p18088_Molinas

Referencias:

  • Garcia-Horsman, J.A., Barquera, B., Rumbley, J., Ma, J., Gennis, R.B., (1994) J. Bacteriol., 176, pp. 5587-5600
  • Pereira, M.M., Teixeira, M., (2004) Biochim. Biophys. Acta, Bioenerg., 1655, pp. 241-247
  • Wikstrom, M., (2004) Biochim. Biophys. Acta, Bioenerg., 1655, pp. 241-247
  • Sousa, F.L., Alves, R.J., Pereira-Leal, J.B., Teixeira, M., Pereira, M.M., (2011) PLoS One, 6, p. 19117
  • Sousa, F.L., Alves, R.J., Teixeira, M., Pereira-Leal, J.B., Pereira, M.M., (2010) Biochim. Biophys. Acta, Bioenerg., 1797, p. 101
  • Pereira, M.M., Sousa, F.L., Verissimo, A.F., Teixeira, M., (2008) Biochim. Biophys. Acta, Bioenerg., 1777, pp. 929-934
  • Pereira, M.M., Santana, M., Teixeira, M., (2001) Biochim. Biophys. Acta, Bioenerg., 1505, pp. 185-208
  • Kaila, V.R.I., Verkhovsky, M.I., Wikstrom, M., (2010) Chem. Rev., 110, pp. 7062-7081
  • Pereira, M.M., Bandeiras, T.M., Fernandes, A.S., Lemos, R.S., Melo, A.M.P., Teixeira, M., (2004) J. Bioenerg. Biomembr., 36, pp. 93-105
  • Pereira, M.M., Sousa, F.L., Teixeira, M., Nyquist, R.M., Heberle, J., (2006) FEBS Lett., 580, pp. 1350-1354
  • Soares, C.M., Baptista, A.M., Pereira, M.M., Teixeira, M., (2004) JBIC, J. Biol. Inorg. Chem., 9, pp. 124-134
  • Sigurdson, H., Namslauer, A., Pereira, M.M., Teixeira, M., Brzezinski, P., (2001) Biochemistry, 40, pp. 10578-10585
  • Santana, M., Pereira, M.M., Elias, N.P., Soares, C.M., Teixeira, M., (2001) J. Bacteriol., 183, pp. 687-699
  • Pereira, M.M., Verkhovskaya, M.L., Teixeira, M., Verkhovsky, M.I., (2000) Biochemistry, 39, pp. 6336-6340
  • Pereira, M.M., Santana, M., Soares, C.M., Mendes, J., Carita, J.N., Fernandes, A.S., Saraste, M., Teixeira, M., (1999) Biochim. Biophys. Acta, Bioenerg., 1413, pp. 1-13
  • Srinivasan, V., Rajendran, C., Sousa, F.L., Melo, A.M.P., Saraiva, L.M., Pereira, M.M., Santana, M., Michel, H., (2005) J. Mol. Biol., 345, pp. 1047-1057
  • Verissimo, A.F., Sousa, F.L., Baptista, A.M., Teixeira, M., Pereira, M.M., (2008) Biophys. J., 95, pp. 4448-4455
  • Stelter, M., Melo, A.M.P., Hreggvidsson, G.O., Hjorleifsdottir, S., Saraiva, L.M., Teixeira, M., Archer, M., (2010) JBIC, J. Biol. Inorg. Chem., 15, pp. 303-313
  • Ly, H.K., Sezer, M., Wisitruangsakul, N., Feng, J.J., Kranich, A., Millo, D., Weidinger, I.M., Hildebrandt, P., (2011) FEBS J., 278, pp. 1382-1390
  • Alvarez-Paggi, D., Martin, D.F., Debiase, P.M., Hildebrandt, P., Marti, M.A., Murgida, D.H., (2010) J. Am. Chem. Soc., 132, pp. 5769-5778
  • Paggi, D.A., Martin, D.F., Kranich, A., Hildebrandt, P., Marti, M.A., Murgida, D.H., (2009) Electrochim. Acta, 54, pp. 4963-4970
  • Kranich, A., Ly, H.K., Hildebrandt, P., Murgida, D.H., (2008) J. Am. Chem. Soc., 130, pp. 9844-9848
  • Murgida, D.H., Hildebrandt, P., (2008) Chem. Soc. Rev., 37, pp. 937-945
  • Jablonkai, I., Oroszlan, P., (2005) Chem. Phys. Lipids, 133, pp. 103-112
  • Natrajan, A., Ferrara, J.D., Youngs, W.J., Sukenik, C.N., (1987) J. Am. Chem. Soc., 109, pp. 7477-7483
  • Friedman, L., Shani, A., (1974) J. Am. Chem. Soc., 96, pp. 7101-7103
  • Tamura, M., Kochi, J., (1971) Synthesis, pp. 303-305
  • Grochol, J., Dronov, R., Lisdat, F., Hildebrandt, P., Murgida, D.H., (2007) Langmuir, 23, pp. 11289-11294
  • Murgida, D.H., Hildebrandt, P., (2005) Phys. Chem. Chem. Phys., 7, pp. 3773-3784
  • Rai, B., Sathish, P., Malhotra, C.P., Pradip, Ayappa, K.G., (2004) Langmuir, 20, pp. 3138-3144
  • Park, S., Schulten, K., (2004) J. Chem. Phys., 120, pp. 5946-5961
  • Onufriev, A., Bashford, D., Case, D.A., (2004) Proteins: Struct., Funct., Bioinf., 55, pp. 383-394
  • Ly, H.K., Marti, M.A., Martin, D.F., Alvarez-Paggi, D., Meister, W., Kranich, A., Weidinger, I.M., Murgida, D.H., (2010) ChemPhysChem, 11, pp. 1225-1235
  • Berendsen, H.J.C., Postma, J.P.M., Vangunsteren, W.F., Dinola, A., Haak, J.R., (1984) J. Chem. Phys., 81, pp. 3684-3690
  • Beratan, D.N., Onuchic, J.N., Winkler, J.R., Gray, H.B., (1992) Science, 258, pp. 1740-1741
  • Beratan, D.N., Onuchic, J.N., Betts, J.N., Bowler, B.E., Gray, H.B., (1990) J. Am. Chem. Soc., 112, pp. 7915-7921
  • Baker, N.A., Sept, D., Joseph, S., Holst, M.J., McCammon, J.A., (2001) Proc. Natl. Acad. Sci. U. S. A., 98, pp. 10037-10041
  • Hu, S.Z., Morris, I.K., Singh, J.P., Smith, K.M., Spiro, T.G., (1993) J. Am. Chem. Soc., 115, pp. 12446-12458
  • Kranich, A., Naumann, H., Molina-Heredia, F.P., Moore, H.J., Lee, T.R., Lecomte, S., De La Rosa, M.A., Murgida, D.H., (2009) Phys. Chem. Chem. Phys., 11, pp. 7390-7397
  • Zuo, P., Albrecht, T., Barker, P.D., Murgida, D.H., Hildebrandt, P., (2009) Phys. Chem. Chem. Phys., 11, pp. 7430-7436
  • Bandeiras, T.M., Refojo, P.N., Todorovic, S., Murgida, D.H., Hildebrandt, P., Bauer, C., Pereira, M.M., Teixeira, M., (2009) Biochim. Biophys. Acta, Bioenerg., 1787, pp. 37-45
  • Todorovic, S., Pereira, M.M., Bandeiras, T.M., Teixeira, M., Hildebrandt, P., Murgida, D.H., (2005) J. Am. Chem. Soc., 127, pp. 13561-13566
  • Murgida, D.H., Hildebrandt, P., (2004) Acc. Chem. Res., 37, pp. 854-861
  • Marcus, R.A., (1965) J. Chem. Phys., 43, pp. 679-701
  • Nahir, T.M., Bowden, E.F., (1996) J. Electroanal. Chem., 410, pp. 9-13
  • Avila, A., Gregory, B.W., Niki, K., Cotton, T.M., (2000) J. Phys. Chem. B, 104, pp. 2759-2766
  • Khoshtariya, D.E., Dolidze, T.D., Shushanyan, M., Davis, K.L., Waldeck, D.H., Van Eldik, R., (2010) Proc. Natl. Acad. Sci. U. S. A., 107, pp. 2757-2762
  • Niki, K., Hardy, W.R., Hill, M.G., Li, H., Sprinkle, J.R., Margoliash, E., Fujita, K., Gray, H.B., (2003) J. Phys. Chem. B, 107, pp. 9947-9949
  • Yue, H.J., Khoshtariya, D., Waldeck, D.H., Grochol, J., Hildebrandt, P., Murgida, D.H., (2006) J. Phys. Chem. B, 110, pp. 19906-19913
  • Murgida, D.H., Hildebrandt, P., (2001) J. Am. Chem. Soc., 123, pp. 4062-4068
  • Battistuzzi, G., Borsari, M., Bortolotti, C.A., Di Rocco, G., Ranieri, A., Sola, M., (2007) J. Phys. Chem. B, 111, pp. 10281-10287
  • Sarma, S., Digate, R.J., Goodin, D.B., Miller, C.J., Guiles, R.D., (1997) Biochemistry, 36, pp. 5658-5668
  • Nahir, T.M., Clark, R.A., Bowden, E.F., (1994) Anal. Chem., 66, pp. 2595-2598
  • Saccucci, T.M., Rusling, J.F., (2001) J. Phys. Chem. B, 105, pp. 6142-6147
  • Shafiey, H., Ghourchian, H., Mogharrab, N., (2008) Biophys. Chem., 134, pp. 225-231
  • Song, S., Clark, R.A., Bowden, E.F., Tarlov, M.J., (1993) J. Phys. Chem., 97, pp. 6564-6572
  • Takayama, S.J., Irie, K., Tai, H.L., Kawahara, T., Hirota, S., Takabe, T., Alcaraz, L.A., Yamamoto, Y., (2009) JBIC, J. Biol. Inorg. Chem., 14, pp. 821-828
  • Wei, J.J., Liu, H.Y., Niki, K., Margoliash, E., Waldeck, D.H., (2004) J. Phys. Chem. B, 108, pp. 16912-16917
  • Kummerle, R., Gaillard, J., Kyritsis, P., Moulis, J.M., (2001) JBIC, J. Biol. Inorg. Chem., 6, pp. 446-451

Citas:

---------- APA ----------
Molinas, M.F., De Candia, A., Szajnman, S.H., Rodríguez, J.B., Martí, M., Pereira, M., Teixeira, M.,..., Murgida, D.H. (2011) . Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films. Physical Chemistry Chemical Physics, 13(40), 18088-18098.
http://dx.doi.org/10.1039/c1cp21925a
---------- CHICAGO ----------
Molinas, M.F., De Candia, A., Szajnman, S.H., Rodríguez, J.B., Martí, M., Pereira, M., et al. "Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films" . Physical Chemistry Chemical Physics 13, no. 40 (2011) : 18088-18098.
http://dx.doi.org/10.1039/c1cp21925a
---------- MLA ----------
Molinas, M.F., De Candia, A., Szajnman, S.H., Rodríguez, J.B., Martí, M., Pereira, M., et al. "Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films" . Physical Chemistry Chemical Physics, vol. 13, no. 40, 2011, pp. 18088-18098.
http://dx.doi.org/10.1039/c1cp21925a
---------- VANCOUVER ----------
Molinas, M.F., De Candia, A., Szajnman, S.H., Rodríguez, J.B., Martí, M., Pereira, M., et al. Electron transfer dynamics of Rhodothermus marinus caa 3 cytochrome c domains on biomimetic films. Phys. Chem. Chem. Phys. 2011;13(40):18088-18098.
http://dx.doi.org/10.1039/c1cp21925a