Advertisement

The State of Protonation of the Proximal Histidyl Imidazole in Horseradish Peroxidase

  • Gerd N. La Mar
  • V. P. Chacko
  • Jeffrey S. de Ropp
Conference paper
Part of the NATO Advanced Study Institutes Series book series (ASIC, volume 89)

Abstract

The ease of formation of iron(IV) complexes in horseradish peroxidase as well as in other hemoproteins has been cited to support the view that in these proteins the proximal histidyl imidazole is deprotonated. However, most of the supporting evidence for this proposal has been indirect. From a detailed comparison of the proton nmr spectra of horseradish peroxidase in several oxidation/spin/ligation states with other hemoproteins and model compounds, it is shown hereby direct detection of the N1H signal, that the proximal histidyl imidazole in horseradish peroxidase is definitely not deprotonated, but most likely involved in hydrogen bonding interactions with the protein in at least the reduced and the cyanide-ligated states.

Keywords

Sperm Whale Contact Shift Proximal Histidine Heme Methyl Unpaired Spin Density 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Perutz, M.F. and Ten Eyck, L.F.: 1971, Cold Saving Harbor Symp. Quant. Biol. 36, pp. 295–310.Google Scholar
  2. 2.
    Morrison, M. and Schonbaum, G.R.: 1976, Ann. Rev. Biochem. 45, pp. 86–127.CrossRefGoogle Scholar
  3. 3.
    Nicholls, P.: 1962, Biochim. Biophys. Acta, 60, pp. 217–228.CrossRefGoogle Scholar
  4. 4.
    Valentine, J.S., Sheridan, R.P., Allen, L.C. and Kahn, P.: 1979, Proc. Nat. Acad. Sci. U.S.A. 76, pp. 1009–1013.CrossRefGoogle Scholar
  5. 5.
    Teraoka, J and Kitagawa, T.: 1980, Biochem. Biophys. Res. Commun. 93, pp. 694–700.CrossRefGoogle Scholar
  6. 6.
    Stein, P., Mitchell, M. and Spiro, T.G.: 1980, J. Am. Chem. Soc. 102, pp. 7795–7797.CrossRefGoogle Scholar
  7. 7.
    Swartz, J.C., Stanford, M.A., Moy, J.N., Hoffman, B.M. and Valentine, J.S.: 1979, J. Am. Chem. Soc. 101, pp. 3396–3398.CrossRefGoogle Scholar
  8. 8.
    Mincey, T. and Traylor, T.G.: 1979, J. Am. Chem. Soc. 101, pp. 765–766.CrossRefGoogle Scholar
  9. 9.
    La Mar, G.N. and Walker, F.A.: 1978, The Porphyrins 4, pp. 61–157.Google Scholar
  10. 10.
    Jesson, J.P.: 1973, in “NMR of Paramagnetic Molecules,” La Mar, G.N., Horrocks, Jr., W.D. and Holm, R.H., eds., Academic Press, New York, pp. 1–52.Google Scholar
  11. 11.
    La Mar, G.N.: 1973, in “NMR of Paramagnetic Molecules,” La Mar, G.N. Horrocks, Jr., W.D. and Holm, R.H., eds., Academic Press, New York, pp. 85–126.Google Scholar
  12. 12.
    La Mar, G.N., Viscio, D.B., Smith, K.M., Caughey, W.S. and Smith, M.L.: 1978, J. Am. Chem. Soc. 100, pp. 8085–8092.CrossRefGoogle Scholar
  13. 13.
    La Mar, G.N.: 1979, in “Biological Applications of Magnetic Resonance,” Shulman, R.G., ed., Academic Press, New York, pp. 305–343.Google Scholar
  14. 14.
    Shulman, R.G., Glarum, S.H. and Karplus, M.: 1971, J. Mol. Biol. 57, pp. 93–115.CrossRefGoogle Scholar
  15. 15.
    La Mar, G.N., Jackson, J.T. and Bartsch, R.G.: 1981, J. Am. Chem. Soc. 103, pp. 4405–4410.CrossRefGoogle Scholar
  16. 16.
    Keller, R.M. and Wüthrich, K.: 1978, Biochim. Biophys. Acta 533, pp. 195–208.Google Scholar
  17. 17.
    La Mar, G.N., de Ropp, J.S., Smith, K.M. and Langry, K.C.: 1980, J. Biol. Chem. 255, pp. 6646–6652.Google Scholar
  18. 18.
    La Mar, G.N., de Ropp, J.S., Smith, K.M. and Langry, K.C.: 1980, J. Am. Chem. Soc. 102,pp, 4833–4835.CrossRefGoogle Scholar
  19. 19.
    La Mar, G.N., de Ropp, J.S., Smith, K.M. and Langry, K.C.: 1981, J. Biol. Chem. 256, pp. 237–243.Google Scholar
  20. 20.
    Goff, H. and La Mar, G.N.: 1977, J. Am. Chem. Soc. 99, pp. 6599–6606.CrossRefGoogle Scholar
  21. 21.
    La Mar, G.N., Budd, D.L. and Goff, H.: 1977, Biochem. Biophys. Res. Commun. 77, pp. 104–110.CrossRefGoogle Scholar
  22. 22.
    Satterlee, J.D. and La Mar, G.N.: 1976, J. Am. Chem. Soc. 98, pp. 2804–2808.CrossRefGoogle Scholar
  23. 23.
    La Mar, G.N., Frye, J.S. and Satterlee, J.D.: 1976, Biochim. Biophys. Acta 428, pp. 78–90.Google Scholar
  24. 24.
    Cutnell, J.D., La Mar, G.N. and Kong, S.B.: 1981, J. Am. Chem. Soc. 103, pp. 3567 - 3572.CrossRefGoogle Scholar
  25. 25.
    La Mar, G.N., Cutnell, J.D. and Kong, S.B.: 1981, Biophys. J. 34, pp. 217–226.CrossRefGoogle Scholar
  26. 26.
    La Mar, G.N. and de Ropp, J.S.: J. Am. Chem. Soc. in press.Google Scholar
  27. 27.
    La Mar, G.N. and de Ropp, J.S.: 1979, Biochem. Biophys. Res. Commun. 90, pp. 36–41.CrossRefGoogle Scholar
  28. 28.
    Poulos, T.L. and Kraut, J.: 1980, J. Biol. Chem. 255, pp. 8199–8205.Google Scholar
  29. 29.
    Schejter, A., Lanir, A. and Epstein, N.: 1976, Arch. Biochem. Biophys. 174, pp. 36–44.CrossRefGoogle Scholar
  30. 30.
    de Ropp, J.S.: 1981, Ph.D. Thesis, University of California, Davis, pp. 191–224.Google Scholar
  31. 31.
    Woodward, C.K. and Hilton, B.D.: 1979, Ann. Rev. Biophys. Bioeng. 8, pp. 99–127.CrossRefGoogle Scholar
  32. 32.
    La Mar, G.N. and de Ropp, J.S.: unpublished results.Google Scholar
  33. 33.
    Sheard, B., Yamane, T. and Shulman, R.G.: 1970, J. Mol. Biol. 53, pp. 35–48.CrossRefGoogle Scholar
  34. 34.
    Chacko, V.P. and La Mar, G.N.: unpublished results.Google Scholar
  35. 35.
    Swift, T.J.: in “NMR of Paramagnetic Molecules,” La Mar, G.N., Horrocks, Jr., W.D. and Holm, R.H., eds., Academic Press, New York, pp. 53–83.Google Scholar
  36. 36.
    La Mar, G.N. and de Ropp, J.S.: to be published.Google Scholar
  37. 37.
    Satterlee, J.D. and Erman, J.E.: 1981, J. Am. Chem. Soc. 103, pp. 199–201.CrossRefGoogle Scholar

Copyright information

© D. Reidel Publishing Company 1982

Authors and Affiliations

  • Gerd N. La Mar
    • 1
  • V. P. Chacko
    • 1
  • Jeffrey S. de Ropp
    • 1
  1. 1.Department of ChemistryUniversity of CaliforniaDavisUSA

Personalised recommendations