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Paramagnetic Inversion of the Sign of the Interference Contribution to the Transverse Relaxation of the Imido Protons of the Coordinated Imidazoles in the Uniformly $^{15}N$ Labeled Cytochrome $c_3$


Abstract

In the spectrum of uniformly 15N labeled cytochrome c3, the relative linewidths of the doublet peaks of the 15N-coupled imido proton of the coordinated imidazole group were reversed on oxidation. This inversion was explained by the interference relaxation process between the electron-proton dipolar and 15N-1H dipolear interactions. The inversion can be used to assign the imido protons of the coordinated imidazole groups in heme proteins.

Keywords

References

  1. Nucleic Acids Res. v.10 Ruterjans, H.;Kaun, E.;Hull, W. E.;Limbach, H. H.
  2. J. Am. Chem. Soc. v.105 Goeron, M.;Leroy, J. L.;Griffey, R. H.
  3. J. Magn. Reson. v.61 Withers, S. G.;Madsen, N. B.;Sykes, B. D.
  4. J. Magn. Reson. v.60 Goldman, M.
  5. In Encyclopedia of Nuclear Magnetic Resonance v.6 Relaxation processes: cross correlation and interference terms Werbelow, L. G.;Grant, D. M.(eds.);Harris, R. K.(eds.)
  6. J. Am. Chem. Soc. v.118 Tjandra, N.;Szabo, A.;Bax, A.
  7. J. Magn. Reson v.127 Tessari, M.;Mulder, F. A. A.;Boelens, R.;Vuister, G. W.
  8. J. Am. Chem. Soc. v.119 Tessari, M.;Vis, H.;Boelens, R.;Kaptein, R.;Vulster, G. W.
  9. J. Am. Chem. Soc. v.119 Tjandra, N.;Bax, A.
  10. J. Biochem. Mol. Biol. v.33 no.6 Kim, A.;Shim, Y. B.;Kang, S. W.;Park, J. S.
  11. Biochim, Biophys. Acta v.243 Yagi, T.;Maruyama, K.
  12. J. Magn. Reson. v.64 Cross, K. J.;Wright, P. E.
  13. J. Mot Biol. v.246 Mandel, A. M.;Akke, M.;Palmer, A. G.
  14. J. Biochemistry v.32 Akke, M.;Skelton, N. J.;Kordel, J.;Palmer, A. G.;Chazin, W.
  15. Eur. J. Biochem. v.230 Tjandra, N.;Kuboniwa, H.;Ren, H.;Bax, A.
  16. Protein Sci. v.5 Ubbink, M.;Pfbhl, M.;Van Der Oost, J.;Berg, A.;Canters, G. W.
  17. Eur. J. Biochem. v.245 Kelly, G. P.;Muskett, F. W.;Whitford, D.
  18. Acta Cryst. v.B33 Fuess, H.;Hohlwein, D.;Mason, S. A.
  19. Principle of High Resolution NMR in Solids Mehring, M.
  20. In Encyclopedia of Nuclear Magnetic Resonance v.6 Proton chemical shift measurements in biological solids McDermott, A.;Ridenour, C. F.;Grant, D. M.(eds);Harris, R. K.(eds)
  21. J. Magn. Reson. B v.111 Ramarnoorthy, A.;Gierasch, L. M.;Opella, S. J.
  22. In NMR of Biological Research: Peptides and Proteins Wuthrich, K.
  23. J. Chem. Phys. v.29 McConnell, H. M.;Robertson, R. E.
  24. J. Biol. Inorg. Chem. v.2 Saigueiro, C. A.;Turner, D. L.;LeGall, J.;Xavier, A. V.
  25. J. Mol. Biol. v.172 Higuchi, Y.;Kusunoki, M.;Matsuura, Y.;Yasuoka, N.;Kakudo, M.

Cited by

  1. Nitrogen Isotope Labeled Tetraheme Cytochrome c3 on a Defined Medium vol.26, pp.2, 2001, https://doi.org/10.5012/bkcs.2005.26.2.278