Principles and Applications of 113Cd NMR to Biological Systems

  • Ian M. Armitage
  • James D. Otvos
Chapter

Abstract

Knowledge of the molecular details of the interactions between metal ions and biological macromolecules is of prime importance in unraveling the mechanisms of the numerous biological processes which are either dependent upon or deleteriously affected by various metals. Several physical techniques, most notably EPR and optical spectroscopy, have been extremely useful in providing insight into the structures of the many macromolecular complexes in nature which contain Fe, Co, Cu, Mn, or Mo as their native constituents. However, because these methods require the presence of a chromophoric and/or paramagnetic metal ion, they are not unfortunately applicable to the study of all valence states of these metal atoms or the many important systems whose functions depend upon the binding of diamagnetic metal ions such as Zn2+, Mg2+, and Ca2+. Although still in its infancy and not routinely available, extended x-ray absorption fine-structure spectroscopy (EXAFS) is potentially capable of providing detailed structural data concerning the electronic configuration and chemical environment of all of these metal atoms in macromolecular complexes in solution. An alternative and by far more readily available technique for studying the structural and functional details of macromolecular complexes with diamagnetic metal atoms is to substitute for the native metal the isotopically enriched, spin-1/2 113Cd nucleus and observe its nuclear magnetic resonance properties.

Keywords

Chemical Shift Chemical Exchange Metal Binding Site Oxygen Ligand Pulse Angle 
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.
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References

  1. Ackerman, J. J. H., Orr, T. V., Bartuska, V. J., and Maciel, G. E., 1979, J. Amer. Chem. Soc. 101: 341.CrossRefGoogle Scholar
  2. Anderson, R. A., Kennedy, F. S., and Vallee, B. L., 1976, Biochemistry 15: 3710.PubMedCrossRefGoogle Scholar
  3. Andersen, R. D., Winter, W. P., Maher, J. J., and Bernstein, I. A., 1978, Biochem. J. 174: 327.PubMedGoogle Scholar
  4. Applebury, M. L., and Coleman, J. E., 1969, J. Biol. Chem. 244: 709.Google Scholar
  5. Applebury, M. L., Johnson, B. P., and Coleman, J. E., 1970, J. Biol. Chem. 245: 4968.Google Scholar
  6. Armitage, I. M., Pajer, R. T., Schoot Uiterkamp, A. J. M., Chlebowski, J. F., and Coleman, J. E., 1976, J. Am. Chem. Soc. 98: 5710.CrossRefGoogle Scholar
  7. Armitage, I. M., Schoot Uiterkamp, A. J. M., Chlebowski, J. F., and Coleman, J. E., 1978, J. Magn. Reson. 29: 375.Google Scholar
  8. Bailey, D. B., Ellis, P. D., Cardin, A. D., and Behnke, W. D., 1978, J. Am. Chem. Soc. 100: 5236.CrossRefGoogle Scholar
  9. Bailey, D. B., Ellis, P. D., and Fee, J. A., 1980, Biochemistry 19: 591.PubMedCrossRefGoogle Scholar
  10. Bauer, R., Limkilde, P., and Johansen, J. T., 1976, Biochemistry 15: 334.PubMedCrossRefGoogle Scholar
  11. Becker, J. W., Reeke, G. N. Jr., Cunningham, B. A., and Edelman, G. M., 1976, Nature 259: 406.PubMedCrossRefGoogle Scholar
  12. Block, W. and Bickar, D., 1978 J. Biol Chem. 253: 6211.Google Scholar
  13. Block, W. and Schlesinger, M. J., 1973, J. Biol. Chem. 248: 5794.Google Scholar
  14. Bobsein, B. R., and Myers, R. J., 1980, J. Amer. Chem. Soc. 102: 2454.CrossRefGoogle Scholar
  15. Bosron, W. F., Anderson, R. A., Falk, M. C., Kennedy, F. S., and Vallee, B. L., 1977, Biochemistry 16: 610.PubMedCrossRefGoogle Scholar
  16. Bosron, W. F., Kennedy, F. S., and Vallee, B. L., 1975, Biochemistry 14: 2275.PubMedCrossRefGoogle Scholar
  17. Bradshaw, R. A., Cancedda, F., Ericsson, L. H., Newman, P. A., Piccoli, S. P., Schlesinger, M. J., Shriefer, K., and Walsh, K. A., 1981, Proc. Natl. Acad. Sci. 78: 3473.PubMedCrossRefGoogle Scholar
  18. Campbell, I. D., Dobson, C. M., Williams, R. J. P., and Wright, P. E., 1975, FEBS Lett., 57: 96.PubMedCrossRefGoogle Scholar
  19. Cardin, A. D., Ellis, P. D., Odom, J. D., and Howard, J. W., Jr., 1975, J. Amer. Chem. Soc. 97: 1672.CrossRefGoogle Scholar
  20. Cheung, T. T. P., Worthington, L., DuBois Murphy, P., and Gerstein, B. C., 1980, J. Magn. Reson. 41:158.Google Scholar
  21. Cheung, W. Y., 1980, Science 207: 19.PubMedCrossRefGoogle Scholar
  22. Chlebowski, J. F., Armitage, I. M., Tusa, P. P., and Coleman, J. E., 1976 J. BioL Chem. 251:1207.Google Scholar
  23. Chlebowski, J. F., Armitage, I. M., and Coleman, J. E., 1977, J. Biol. Chem. 252: 7053.Google Scholar
  24. Chlebowski, J. F., and Coleman, J. E., 1976, J. Biol. Chem. 251: 1202.Google Scholar
  25. Chlebowski, J. F., and Coleman, J. E., 1979, Abstracts of Papers, 178th National Meeting of the American Chemical Society, Washington, D.C., Sept. 9–14, Biol. 035, American Chemical Society, Washington, D.C.Google Scholar
  26. Chlebowski, J. F., and Mabrey, S., 1977, J. BioL Chem. 252: 7042.PubMedGoogle Scholar
  27. Coleman, J. E.,1980, Current Concepts of the Mechanism of Action of Carbonic Anhydrase, in: Biophysics and Physiology of Carbon Dioxide (Bauer, Gros, Bartels, eds.), pp. 133–150, Springer-Verlag, Heidelberg.Google Scholar
  28. Coleman, J. E., Armitage, I. M., Chlebowski, J. F., Otvos, J. D., and Schoot Uiterkamp, A. J. M., 1979, Multinuclear NMR Approaches to the Solution Structure of Alkaline Phosphatase: “C, 19F, ”P, and 13Cd NMR, in: Biological Applications of Magnetic Resonance ( R. G. Shulman, ed.), pp. 345–395, Academic Press, New York.Google Scholar
  29. Coleman, J. E., and Chlebowski, J. F.,1979, Molecular Properties and Mechanism of Alkaline Phosphatase, in: Advances in Inorganic Biochemistry (G. L. Eichhorn and L. G. Marzilli, eds.), pp. 1–66, Elsevier/North Holland, New York.Google Scholar
  30. Coleman, J. E., and Vallee, B. L., 1964, Biochemistry 3: 1874.PubMedCrossRefGoogle Scholar
  31. Csopak, H. and Falk, K. E., 1974, Biochim. Biophys. Acta. 359: 22.PubMedCrossRefGoogle Scholar
  32. Doddrell, D., Glushko, V., and Allerhand, A., 1972, J. Chem. Phys. 56: 3683.CrossRefGoogle Scholar
  33. Douzou, P., Balny, G., and Franks, F., 1978, Biochimie 60: 151.PubMedCrossRefGoogle Scholar
  34. Drakenberg, T., Lindman, B., Cave, A., and Parello, J., 1978, FEBS Lett. 92: 346.PubMedCrossRefGoogle Scholar
  35. Edelman, G. M., Cunningham, B. A., Reeke, G. N., Jr., Becker, J. W., Waxdal, M. J., and Wang, J. L., 1972, Proc. Nat. Acad. Sci USA 69: 2580.PubMedCrossRefGoogle Scholar
  36. Eklund, H., Nordström, B., Zeppezauer, E., Söderlund, G., Ohlsson, I., Boiwe, T., and Bränden, C.-I., 1974, FEBS Lett. 44: 200.PubMedCrossRefGoogle Scholar
  37. Forsén, S., Thulin, E., Drakenberg, T., Krebs, J., and Seamon, K., 1980, FEBS Lett. 117: 189.PubMedCrossRefGoogle Scholar
  38. Forsén, S., Thulin, E., and Lilja, H., 1979, FEBS Lett. 104: 123.PubMedCrossRefGoogle Scholar
  39. Freeman, R. and Hill, H. D. W., 1975, Determination of Spin—Spin Relaxation Times in High-Resolution NMR, in: Dynamic Nuclear Magnetic Resonance Spectroscopy ( L. Jackman and F. A. Cotton, eds.), pp. 131–162, Academic Press, New York.CrossRefGoogle Scholar
  40. Freeman, R., and Morris, G. A., 1979, Bull. Magn. Reson. 1: 5.Google Scholar
  41. Griffith, E. H., Hunt, G. W., and Amma, E. L., 1976, J. Chem. Soc., Chem. Commun.,432.Google Scholar
  42. Haberkorn, R. A., Que, L. Jr., Gillum, W. O., Holm, R. H., Liu, C. S., Lord, R. C., 1976, Inorg. Chem. 15: 2408.CrossRefGoogle Scholar
  43. Hardman, K. D., and Ainsworth, C. F., 1972, Biochemistry 11: 4910.PubMedCrossRefGoogle Scholar
  44. Huang, I.-Y., Tsunoo, H., Kimura, M., Nakashima, H., and Yoshida, A., 1979, Primary Structure of Mouse Liver Metallothionein-I and -II, in: Metallothionein ( J. H. R. Kägi and M. Nordberg, eds.), pp. 169–172, Birkhäuser, Basle.Google Scholar
  45. Huang, I.-Y., Yoshida, A., Tsunoo, H., and Nakajima, H., 1977, J. Biol. Chem. 252: 8217.Google Scholar
  46. Hull, W. E., Halford, S. E., Gutfreund, H., and Sykes, B. D., 1976, Biochemistry, 15: 1557.Google Scholar
  47. Hull, W. E., and Sykes, B. D., 1976, Biochemistry 15: 1535.PubMedCrossRefGoogle Scholar
  48. Jonsson, N.B.-H., Tibell, L. A. E., Evelhoch, J. L., Bell, S. J., and Sudmeier, J. L., 1980, Proc. Natl. Acad. Sci. USA 77: 3269.PubMedCrossRefGoogle Scholar
  49. Kägi, J. H. R., Himmelhoch, S. R., Whanger, P. D., Bethune, J. L., and Vallee, B. L., 1974, J. Biol. Chem. 249: 3537.PubMedGoogle Scholar
  50. Kägi, J. H. R., and Vallee, B. L., 1961, J. Biol. Chem. 236: 2435.PubMedGoogle Scholar
  51. Kissling, M. M., and Kägi, J. H. R., 1977, FEBS Lett. 82: 247.PubMedCrossRefGoogle Scholar
  52. Kojima, Y., Berger, C., and Kägi, J. H. R., 1979, The Amino Acid Sequence of Equine Metallothioneins, in: Metallothionein ( J. H. R. Kägi and M. Nordberg, eds.), pp. 153–161, Birkhäuser, Basle.Google Scholar
  53. Kojima, Y., Berger, C., Vallee, B. L., and Kägi, J. H. R., 1976, Proc. Natl. Acad. Sci., USA 73: 3413.PubMedCrossRefGoogle Scholar
  54. Kojima, Y., and Kägi, J. H. R., 1978, Trends Biochem. Sci. 3: 90.CrossRefGoogle Scholar
  55. Kostelnik, R. J. and Bothner-By, A. A., 1974, J. Magn. Reson. 14: 141.Google Scholar
  56. Lerch, K., Animer, D., and Olafson, R. W., 1982, J. Biol. Chem. (in press).Google Scholar
  57. Liao, M.-J., and Prestegard, J. H., 1979, Biochem. Biophys, Acta 550: 157.CrossRefGoogle Scholar
  58. Lindskog, S., Henderson, L. E., Kannan, K. K., Liljas, A., Nyman, P. O., and Strandberg, B., 1971, in: The Enzymes, 3rd ed., (P. D. Boyer, ed.), Vol. 5, pp. 587–665, Academic Press, New York.Google Scholar
  59. Maciel, G. E., and Borzo, M., 1973, J. Chem. Soc., Chem. Commun., 394.Google Scholar
  60. Maren, T. H., Rayburn, C. S., and Liddell, N. E., 1976, Science 191: 469.PubMedCrossRefGoogle Scholar
  61. Moews, P. C., and Kretzinger, R. H., 1975, J. Mol. Biol. 91: 201.PubMedCrossRefGoogle Scholar
  62. Nordberg, M., and Kojima, Y., 1979, Report from the First International Meeting onGoogle Scholar
  63. Metallothionein and other Low Molecular Weight Metal-Binding Proteins, in: Metallo-thionein (J. H. R. Kägi and M. Nordberg, eds.), pp. 41–124, Birkhäuser, Basle.Google Scholar
  64. Olafson, R. W., Kearns, A., and Sim, R. G., 1979b, Comp. Biochem. Physiol. 62: 417.Google Scholar
  65. Olafson, R. W., Sim, R. G., and Boto, K. G., 1979a, Comp. Biochem. Physiol. 62: 407.Google Scholar
  66. Otvos, J. D., Alger, J. R., Coleman, J. E., and Armitage, I. M., 1979a, J. Biol. Chem. 254: 1778.PubMedGoogle Scholar
  67. Otvos, J. D., and Armitage, I. M., 1979, J. Amer. Chem. Soc. 101: 7734.CrossRefGoogle Scholar
  68. Otvos, J. D., Armitage, I. M Chlebowski, J. F., and Coleman, J. E., 1979b, J. Biol. Chem. 254: 4707.PubMedGoogle Scholar
  69. Otvos, J. D., and Armitage, I. M., 1980a, Biochemistry 19: 4021.PubMedCrossRefGoogle Scholar
  70. Otvos, J. D., and Armitage, I. M., 1980b, Biochemistry 19: 4031.PubMedCrossRefGoogle Scholar
  71. Otvos, J. D., and Armitage, I. M., 1980c, Proc. Natl. Acad. Sci. USA 77:7094. Otvos, J. D., and Browne, D. T., 1980, Biochemistry 19: 4011.Google Scholar
  72. Otvos, J. D., and Armitage, I. M., 1982, Elucidation of Metallothionein Structure by “’Cd NMR, in Biochemical Structure Determination by NMR (A. A. Bothner-By and B. D. Sykes, eds.), pp. Marcel Dekker, New York.Google Scholar
  73. Palmer, A. R., Bailey, D. B., Behnke, W. D., Cardin, A. D., Yang, P. P., and Ellis, P. D., 1980, Biochemistry 19: 5063.PubMedCrossRefGoogle Scholar
  74. Pantoliano, M. W., McDonnell, P. J. and Valentine, J. S., 1979, J. Am. Chem. Soc. 101: 6454.CrossRefGoogle Scholar
  75. Plocke, D. J., Levinthal, C., and Vallee, B. L., 1962, Biochemistry 1: 373.PubMedCrossRefGoogle Scholar
  76. Potter, J. D. and Gergely, J., 1975,1 Biol. Chem. 250:4628.Google Scholar
  77. Quiocho, F. A. and Lipscomb, W. N., 1971, Advan. Protein Chem. 25: 1.CrossRefGoogle Scholar
  78. Reid, T. W. and Wilson, I. B., 1971, E. coli Alkaline Phosphatase, in: The Enzymes ( P. D. Boyer, ed.) Vol. 4, pp. 373–417, Academic Press, New York.Google Scholar
  79. Richardson, J. S., Thomas, K. A., and Richardson, D. C., 1975a, Biochem. Biophys. Res. Commun. 63: 986.PubMedCrossRefGoogle Scholar
  80. Richardson, J. S., Thomas, K. A., Rubin, B. H., and Richardson, D. C., 1975b, Proc. Natl. Acad. Sci. USA 72: 1349.Google Scholar
  81. Schoot Uiterkamp, A. J. M., Armitage, I. M., and Coleman, J. E., 1980, J. Biol. Chem. 255: 3911.Google Scholar
  82. Shapiro, S. G., Squibb, K. S., Markowitz, L. A., and Cousins, R. J., 1978, Biochem. J. 175: 833.PubMedGoogle Scholar
  83. Simpson, R. T. and Vallee, B. L., 1968, Biochemistry 7: 4343.PubMedCrossRefGoogle Scholar
  84. Sokolowski, G., and Weser, V., 1975, Hoppe-Seyler’s Z. Physiol. Chem. 356: 1715.PubMedCrossRefGoogle Scholar
  85. Sowadski, J. M., Foster, B. A., and Wyckoff, H. W., 1981, J. Mol. Biol. 150: 245.PubMedCrossRefGoogle Scholar
  86. Sudmeier, J. L., and Bell, S. J., 1977, J. Am. Chem. Soc. 99: 4499.CrossRefGoogle Scholar
  87. Sytkowski, A. J., and Vallee, B. L., 1979, Biochemistry 18: 4095.PubMedCrossRefGoogle Scholar
  88. Taylor, J. S., Lau, C. Y., Applebury, M. L. and Coleman, J. E., 1973, J. Biol. Chem. 248: 6216.PubMedGoogle Scholar
  89. Tsunoo, H., Kino, K., Nakajima, H., Hata, A., Huang, I.-Y., and Yoshida, A., 1978, J. Biol. Chem. 253: 4172.Google Scholar
  90. Valentine, J. S., Pantoliano, M. W., McDonnell, P. J., Burger, A. R., and Lippard, S. J., 1979, Proc. Natl. Acad. Sci. USA 76: 4245.PubMedCrossRefGoogle Scholar
  91. Vasak, M., 1980, J. Am. Chem. Soc. 102: 3953.CrossRefGoogle Scholar
  92. Weiner, R. E., Chlebowski, J. F., Haffner, P. H., and Coleman, J. E., 1979, J. Biol. Chem. 254: 9739.PubMedGoogle Scholar
  93. Winge, D. R., Premakumar, R., and Rajagopalan, K. V., 1978, Arch. Biochem. Biophys. 188: 466.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1982

Authors and Affiliations

  • Ian M. Armitage
    • 1
  • James D. Otvos
    • 1
  1. 1.The Department of Molecular Biophysics and BiochemistryYale UniversityNew HavenUSA

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