Simulation of the EMR Spectra of High-Spin Iron in Proteins

  • Betty J. Gaffney
  • Harris J. Silverstone
Part of the Biological Magnetic Resonance book series (BIMR, volume 13)

Abstract

Very detailed information about the energy levels and orientations of d orbitals in heme proteins has been obtained by combining EMR studies of paramagnetic samples with other structural information from X-ray crystallography and optical studies. As a result, the chemistry of heme enzymes can be discussed in detail. While the aim of this chapter is to review progress in bringing the chemistry of mononuclear iron centers in nonheme proteins to a similar level of knowledge, our understanding of line shape analysis for high-spin iron is dominated by the vast literature on heme samples. We begin this introduction with some of the history of EMR spectroscopy of methemoglobin and metmyoglobin.

Keywords

Microwave Anisotropy Tyrosine Sodium Chloride Superoxide 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Aasa, R., 1970, J. Chem. Phys. 52:3919–3930.CrossRefGoogle Scholar
  2. Aasa, R., and Vänngård, T., 1975, J. Magn. Res. 19:308–315.Google Scholar
  3. Aisen, P., Pinkowitz, R. A., and Leibman, A., 1972. Ann. New York Acad. Sci. 222:337–346.CrossRefGoogle Scholar
  4. Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C., 1988, Proc. Natl. Acad. Sci. USA 85:8487–8491.PubMedCrossRefGoogle Scholar
  5. Alpert, Y., Couder, Y., Tuchendler, J., and Thome, H., 1973, Biochim. Biophys. Acta 322:34–37.PubMedCrossRefGoogle Scholar
  6. Axelrod, B., Cheesbrough, T. M., and Laakso, S., 1981, Meth. Enzymol. 71:441–451.CrossRefGoogle Scholar
  7. Bailey, S., Evans, R. W., Garratt, R. C., Gorinsky, B., Hasnain, S., Horsburgh, C., Jhoti, H., Lindley, P. F., Mydin, A., Sarra, R., and Watson, J. L., 1988, Biochem. 27:5804–5812.CrossRefGoogle Scholar
  8. Baker, E. N., Anderson, B. F., Baker, H. M., Haridas, M., Norris, G. E., Rumball, S. V., and Smith, C. A., 1990, Pure Appl. Chem. 62:1067–1070.CrossRefGoogle Scholar
  9. Belford, R. L., and Belford, G. G., 1973, J. Chem. Phys. 59:853–854.CrossRefGoogle Scholar
  10. Bennett, J. E., and Ingram, D. J. E., 1956, Nature 275:275–276.CrossRefGoogle Scholar
  11. Bennett, J. E., Gibson, J. F., and Ingram, D. J. E., 1957, Proc. Roy. Soc. (London) A 240:67–82.CrossRefGoogle Scholar
  12. Bennett, J. E., Gibson, J. F. and Ingram, D. J. E., Haughton, T. M., Kerkut, G. A., and Munday, K. A., 1961, Proc. Roy. Soc. (London) A 262:395–408.CrossRefGoogle Scholar
  13. Bleaney, B., and Trenam, R. S., 1954, Proc. Roy. Soc. (London) A 223:1.CrossRefGoogle Scholar
  14. Bloom, L. M., Benkovic, S. J., and Gaffney, B. J., 1986, Biochem. 25:4204–4210.CrossRefGoogle Scholar
  15. Blumberg, W. E., 1967, The EPR of high spin Fe3+ in rhombic fields, in Magnetic Resonance in Biological Systems (A. Ehrenberg, B. G. Malmström, and T. Vänngård, eds.), Pergamon, Oxford, pp. 119–133.Google Scholar
  16. Boyington, J. C., Gaffney, B. J., and Amzel, L. M., 1990, J. Biol. Chem. 265:12771–12773.PubMedGoogle Scholar
  17. Boyington, J. C., Gaffney, B. J., and Amzel, L. M., 1993 (submitted).Google Scholar
  18. Brill, A. S., Fiamingo, F. G., and Hampton, D. A., 1978, Characterization of high-spin ferric states in heme proteins, in Frontiers of Biological Energetics, Vol. 2 (P. L. Dutton et al., eds.), Academic Press, NY, pp. 1025–1033.CrossRefGoogle Scholar
  19. Brill, A. S., Fiamingo, F. G., and Hampton, D. A., 1986, J. Inorg. Biochem. 28:137–143.PubMedCrossRefGoogle Scholar
  20. Carlioz, A., Ludwig, M. L., Stallings, W. C., Fee, J. A., Steinman, H. M, and Touati, D., 1988, J. Biol. Chem. 263:1555–1562.PubMedGoogle Scholar
  21. Coffman, R. E., 1975, J. Phys. Chem. 79:1129–1136.CrossRefGoogle Scholar
  22. de Groot, J. J. M. C., Veldink, G. A., Vliegenthart, J. F. G., Boldingh, J., Wever, R. and van Gelder, B. F., 1975, Biochim. Biophys. Acta 377:71–79.PubMedCrossRefGoogle Scholar
  23. Doctor, K. S., Gaffney, B. J., Alvarez, G., and Silverstone, H. J., 1993, J. Phys. Chem. 97:3028– 3033.CrossRefGoogle Scholar
  24. Dubach, J., Gaffney, B. J., More, K., Eaton, G. R., and Eaton, S. S., 1991, Biophys. J. 59:1091–1100.PubMedCrossRefGoogle Scholar
  25. Dunham, W. R., Carroll, R. T., Thompson, J. F., Sands, R. H., and Funk, M. O., 1990, Euro. J. Biochem. 190:611–617.CrossRefGoogle Scholar
  26. Egmond, M. R., Finazzi-Agrò, A., Fasella, P. M., Veldink, G. A., and Vliegenthart, J. F. G., 1975, Biochim. Biophys. Acta 397:43–49.PubMedCrossRefGoogle Scholar
  27. Eisenberger, P., and Pershan, P. S. 1966, J. Chem. Phys. 45:2832–2835.PubMedCrossRefGoogle Scholar
  28. Eisenberger, P., and Pershan, P. S., 1967, J. Chem. Phys. 47:3327–3333.PubMedCrossRefGoogle Scholar
  29. Fee, J. A., McClune, G. J., Lees, A. C., Zidovetski, R. and Pecht, I., 1981, Israel J. Chem. 21:54–58.Google Scholar
  30. Feher, E., 1964, Phys. Rev. 136A:145–157.CrossRefGoogle Scholar
  31. Feher, G., 1970, Electron Paramagnetic Resonance with Applications to Selected Problems in Biology (Les Houches Lectures, 1969), Gordon and Breach, New York.Google Scholar
  32. Fiamingo, F. G., Brill, A. S., Hampton, D. A., and Thorkildsen, R., 1989, Biophys. J. 55:67–77.PubMedCrossRefGoogle Scholar
  33. Fisher, D. B., Kirkwood, R., and Kaufman, S., 1972, J. Biol. Chem. 247:5161–5167.PubMedGoogle Scholar
  34. Gaffney, B. J., 1990, Contribution of iron to protein folding and catalysis in lipoxygenase, in Abstracts of the XIV International Conference on Magnetic Resonance in Biological Systems (Warwick, England), p. P9–6.Google Scholar
  35. Gaffney, B. J., Mavrophilipos, D. V., and Doctor, K. S., 1993, Biophys. J. 64:773–783.PubMedCrossRefGoogle Scholar
  36. Gebbhard, M. S., Deaton, D. C., Koch, S. A., Millar, M., and Solomon, E. I., 1990, J. Am. Chem. Soc. 112:2217–2231.CrossRefGoogle Scholar
  37. Gottschall, D., Dietrich, R. F., Benkovic, S. J., and Shiman, R., 1982, J. Biol. Chem. 257:845–849.PubMedGoogle Scholar
  38. Griffith, J. S., 1964, Biopolymers S1:35–46.Google Scholar
  39. Hampton, D. A., and Brill, A. S., 1979, Biophys. J. 25:301–312.PubMedCrossRefGoogle Scholar
  40. Helcké, G. A., Ingram, D. J. E., and Slade, E. F., 1968, Proc. Roy. Soc. (London) 169:275–288.CrossRefGoogle Scholar
  41. Hoffman, B. M., 1991, Acct. Chem. Res. 24:164–170.CrossRefGoogle Scholar
  42. Howard, J. B., and Rees, D. C., 1991, Adv. Protein Chem. 42:199–280.PubMedCrossRefGoogle Scholar
  43. Ingram, D. J. E., Gibson, J. F., and Perutz, M. F., 1956, Nature 178:906–908.PubMedCrossRefGoogle Scholar
  44. Kendrew, J. C., and Parrish, R. G., 1956, Proc. Roy. Soc. (London) 238:305–324.Google Scholar
  45. Kotani, M., 1968, Adv. Quantum Chem. 4:227–266.CrossRefGoogle Scholar
  46. Levin, P. D., and Brill, A. S., 1988, J. Phys. Chem. 92:5103–5110.CrossRefGoogle Scholar
  47. Mavrophilipos, D. V., 1986, Characterization of the iron environment of lipoxygenase (Ph.D. thesis), Johns Hopkins University, Baltimore, Maryland.Google Scholar
  48. Mavrophilipos, D. V., and Gaffney, B. J., 1985, Biophys. J. 47:401a.Google Scholar
  49. McGavin, D. G., and Tennant, W. C., 1985, J. Magn. Res. 61:321–332.Google Scholar
  50. Michel, H., Epp, O., and Diesenhofer, J., 1986, EMBO J. 5:2445–2451.PubMedGoogle Scholar
  51. Minge, J., Mombourquette, M. J., and Weil, J. A., 1990, Phys. Rev. B 42:33–36.CrossRefGoogle Scholar
  52. Ohlendorf, D. H., Lipscomb, J. D., and Weber, P. C., 1988, Nature 336:403–405.PubMedCrossRefGoogle Scholar
  53. Pilbrow, J. R., 1984, Magn. Res. 58:186–203.Google Scholar
  54. Pilbrow, J. R., 1990, Transition Ion Electron Paramagnetic Resonance, Clarendon Press, Oxford.Google Scholar
  55. Pistorius, E. K., Axelrod, B. and Palmer, G., 1976, J. Biol. Chem. 251:7144–7148.PubMedGoogle Scholar
  56. Poole, C. P., Jr., Farach, H. A., and Jackson, W. K., 1974, J. Chem. Phys. 61:2220–2221.CrossRefGoogle Scholar
  57. Princiotto, J. V., and Zapolski, E. J., 1975, Nature 255:87–88.PubMedCrossRefGoogle Scholar
  58. Schilstra, M. J., Veldink, G. A., Verhagen, J., and Vliegenthart, J. F. G., 1992, Biochemistry 31: 7692–7699.PubMedCrossRefGoogle Scholar
  59. Schlabach, M. R., and Bates, G. W., 1975, J. Biol. Chem. 250:2182–2188.PubMedGoogle Scholar
  60. Scholes, C. P., 1970, J. Chem. Phys. 52:4890–4895.CrossRefGoogle Scholar
  61. Scholes, C. P., Lapidot, A., Mascarenhas, R., Inubushi, T., Isaacson, R. A., and Feher, G., 1982, J. Am. Chem. Soc. 104:2724–2735.CrossRefGoogle Scholar
  62. Schewe, T., Wiesner, T., and Rappoport, S. M., 1986, Adv. Enzymol. Related Areas Mol. Biol. 58:192–271.Google Scholar
  63. Singel, D. J., 1989, Multifrequency ESEEM: Perspectives and applications in Advanced EPR: Applications in Biology and Biochemistry (A. J. Hoff, ed.), Elsevier, Amsterdam, pp. 119– 134.Google Scholar
  64. Slappendel, S., Veldink, G. A., Vliegenthart, J. F. G., Aasa, R., and Malmström, B. G., 1980, Biochim. Biophys. Acta 642:30–39.Google Scholar
  65. Slappendel, S., Veldink, G. A., Vliegenthart, J. F. G., Aasa, R., and Malmström, B. G., 1981, Biochim. Biophys. Acta 667:77–86.PubMedCrossRefGoogle Scholar
  66. Slappendel, S., Aasa, R., Malmström, B. G., Verhagen, J., Veldink, G. A., and Vliegenthart, J. F. G., 1982a, Biochim. Biophys. Acta 708:259–265.CrossRefGoogle Scholar
  67. Slappendel, S., Malmström, B. G., Petersson, L., Ehrenberg, A., Veldink, G. A., and Vliegenthart, J. F. G., 1982b, Biochem. Biophys. Res. Commun. 108:673–677.PubMedCrossRefGoogle Scholar
  68. Smith, B. T., Boyle, J. M., Dongarra, J. J., Garbow, B. S., Ikebe, Y., Klema, V. C., and Moler, C. B., 1976, Matrix Eigensystem Routines-EISPACK Guide, 2nd ed., Springer-Verlag, New York.CrossRefGoogle Scholar
  69. Smith, C. A., Baker, H. M., and Baker, E. M., 1991, J. Mol. Biol. 219:155–159.PubMedCrossRefGoogle Scholar
  70. Snetsinger, P. A., Chasteen, N. D., and van Willigen, H., 1990, Am. Chem. Soc. 112:8155–8160.CrossRefGoogle Scholar
  71. Stoddard, B. L., Howell, P. L., Ringe, D., and Petsko, G. A., 1990, Biochem. 29:8885–8893.CrossRefGoogle Scholar
  72. Sweeney, W. V., Coucouvanis, D., and Coffman, R. E., 1973, J. Chem. Phys. 59:369–379.CrossRefGoogle Scholar
  73. Thomann, H., and Bernardo, M., 1993, Pulsed electron nuclear double and multiple resonance spectroscopy of metals in proteins and enzymes (Chapter 7, this volume).Google Scholar
  74. van Veen, G., 1978, J. Magn. Res. 30:91–109.Google Scholar
  75. Wallick, D. E., Bloom, L. M., Gaffney, B. J., and Benkovic, S. J., 1984, Biochem. 23:1295–1302.CrossRefGoogle Scholar
  76. Weger, M., 1960, Bell System Tech. J. 39:1013–1112.Google Scholar
  77. Weissbluth, M., 1967, Structure and Bonding 2:1–125.CrossRefGoogle Scholar
  78. Whittaker, J. W., and Solomon, E. I., 1988, J. Am. Chem. Soc. 110:5329–5339.CrossRefGoogle Scholar
  79. Woo, S. L. C., 1989, Biochemistry 28:1–7.PubMedCrossRefGoogle Scholar
  80. Yang, A.-S., and Gaffney, B. J., 1987, Biophys. J. 51:55–67.PubMedCrossRefGoogle Scholar
  81. Yewdall, S. J., Lawson, D. M., Artymiuk, P. J., Treffry, A., Harrison, P. M., Luzzago, A., Cesarni, G., Levi, S., and Arosio, P., 1990, Biochem. Soc. Trans. 18:1028–1029.PubMedGoogle Scholar
  82. Zhang, Y., Gebbhard, M. S., and Solomon, E. I., 1991, J. Am. Chem. Soc. 113:5162–5175.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Betty J. Gaffney
    • 1
  • Harris J. Silverstone
    • 1
  1. 1.Department of ChemistryThe Johns Hopkins UniversityBaltimoreUSA

Personalised recommendations