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Modulation of Cytochrome c-Membrane Interaction by the Physical State of the Membrane and the Redox State of Cytochrome c


초록

Association of cytochrome c with anionic membranes involved both electrostatic and hydrophobic interactions and their relative contributions depended on the physical state of the membrane and the redox state of cyto-chromec.Hydrophobic interaction was favored by the membranes in gel phase, by the membranes with a large curvature, and by the membranes with a high surface charge density. Ferrocytochrome c was less dissociable by NaCl than ferricytochrome c suggesting that a lower protein stability is beneficial for hydrophobic interac-tion.Hydrophobic interaction induced larger structural perturbations on cytochrome c as monitored by the loss of the Fe-Met bond and by the increase in the distance between heme and Trp-59. When bound to anionic mem-branes,spin-labeled cytochrome c showed an electron paramagnetic resonance spectrum with two or more components, providing a direct evidence for multiple conformations of bound cytochrome c.

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참고문헌

  1. J. Cell Biol. v.113 Cortese, J. D.;Voglino, A. L.;Hackenbrock, C. R.
  2. Biochim. Biophys. Acta v.1228 Cortese, J. D.;Voglino, A. L.;Hackenbrock, C. R.
  3. Biochemistry v.37 Cortese, J. D.;Voglino, A. L.;Hackenbrock, C. R.
  4. Biochimie v.76 Pinheiro, T. J. T.
  5. Biochemistry v.30 Muga, A.;Mantsch, H. H.;Surewicz, W. K.
  6. Biophys. J. v.65 Heimburg, T.; Marsh, D
  7. Biochemistry v.36 Pinheiro, T. J. T.;Elove, G. A.;Watts, A.;Roder, H.
  8. FEBS Lett. v.360 de Jongh, H. H. J.;Ritsema, T.;Killian, J. A.
  9. Biochemistry v.31 Spooner, P. J. R.;Watts, A.
  10. Biochemistry v.15 Birrell, G. B.;Griffith, O. H.
  11. Biochemistry v.33 Pinheiro, T. J. T.;Watts, A.
  12. Biochemistry v.30 Heimburg, T.;Hildebrandt, P.;Marsh, D.
  13. Biochemistry v.33 Heimburg, T.;Biltonen, R. L.
  14. Biochemistry v.33 Pinheiro, T. J. T.;Watts, A.
  15. J. Biol. Chem. v.243 Sherman, F.;Stewart, J. W.;Parker, J. H.;Inhaber, J.;Shipman, N.;Putterman, G. J.;Gardisky, R. L.;Margoliash, E.
  16. Protein Expr. Purif. v.3 Koshy, T. I.;Luntz, T. L.;Garber, E. A. C.;Margoliash, E.
  17. J. Biochem. Mol. Biol. v.29 Min, T.;Park, N.-h.;Park, H. Y.;Hong, S.-J.;Han, S.
  18. Methods Enzymol. v.10 Yonetani, T.
  19. J. Biol. Chem. v.270 Rytomaa, M.;Kinnunen, P. K. J.
  20. Biochemistry v.26 Mustonen, P.;Virtanen, J. A.;Somerharju, P. J.;Kinnunen, P. K. J.
  21. J. Biol. Chem. v.269 Rytomaa, M.;Kinnunen, P. K. J.
  22. Biochemistry v.33 Snel, M. M. E.;de Kruijff, B.;Marsh, D.
  23. J. Biol. Chem. v.267 Rytomaa, M.;Mustonen, P.;Kinnunen, P. K. J.
  24. Biofizika v.22 Ksenzhek, O. S.;Koganov, M. M.;Gevod, V. S.
  25. Biochim. Biophys. Acta v.862 Waltham, M. C.;Cornell, B. A.;Smith, R.
  26. Biophys. J. v.67 Snel, M. M. E.;Marsh, D.
  27. Nature v.322 no.756 Prats, M.;Teissie, J.;Tocanne, J.-F.
  28. J. Biol. Chem. v.273 no.9443 Davidson, W. S.;Jonas, A.;Clayton, D. F.;George, J. M.
  29. J. Biol. Chem. v.273 Geng, D.;Chura, J.;Roberts, M. F.
  30. Biochim. Biophys. Acta v.932 Szebeni, J.;Tollin, G.

피인용 문헌

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