Structure of Haemoglobin M Milwaukee, A Mutant Form Exhibiting Interaction Between Ferrous and Ferric Subunits

  • M. F. Perutz
  • P. D. Pulsinelli
  • Helen M. Ranney
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 28)


There are five different abnormal haemoglobins which cause methaemoglobinaemia. In four of these the action of methaemoglobin reductase is ineffective because either the proximal or the distal haem-linked histidines in one pair of subunits have been replaced by tyrosines, and in the fifth, known as haemoglobin M Milwaukee (Hb Mil), because valines Ell(67) β have been replaced by glutamic acids (Gerald and Efron, 1961).


Iron Atom Difference Spectrum Oxygen Affinity Ferrous Citrate Porphyrin Ring 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Brunori, M., Amiconi, G., Antonini, E., Wyman, J., and Winterhalter, K.H. (1970). Artificial intermediates in the reaction of haemoglobin. Functional and conformational properties of the cyanmet intermediates. J.Mol.Biol. 49: 461.PubMedCrossRefGoogle Scholar
  2. Edelstein, S.J. (1971). Extensions of the allosteric model for haemoglobin. Nature. 230: 224.PubMedCrossRefGoogle Scholar
  3. Gerald, P.S., and Efron, M.L. (1961). Chemical studies of several varieties of Hb M. Proc.Nat.Acad. Sci.US. 47: 1758.CrossRefGoogle Scholar
  4. Greer, J. (1971). Three-dimensional structure of abnormal human haemoglobins M Hyde Park and M Iwate. J.Mol.Biol. 59: 107.PubMedCrossRefGoogle Scholar
  5. Hayashi, A., Suzuki, T., Shimizu, A., Morimoto, H., and Watari, H. (1967). Changes in EPR spectra of M-type abnormal haemoglobins induced by deoxygenation and their implication for the haem-haem interaction. Biochim.Biophys.Acta. 147: 407PubMedGoogle Scholar
  6. Hayashi, A., Suzuki, T., Imai, K., Morimoto, H., and Watari, H. (1969). Properties of hemoglobin M Milwaukee-1 variant and its unique characteristic. Biochim.Biophys.Acta. 194: 6.PubMedGoogle Scholar
  7. Hoard, J.L. (1968). In: Structural Chemistry and Molecular Biology (edit, by Rich, A., and Davidson, N.) Freeman: San Francisco.Google Scholar
  8. Kendrew, J.C. (1963). Myoglobin and the structure of proteins. Science. 139: 1259.PubMedCrossRefGoogle Scholar
  9. Lindstrom, T.R., Ho, C., and Pisciotta, A.V. (1972). Nuclear magnetic resonance studies of haemoglobin M Milwaukee-1 and their implications to haem-haem interactions. Nature. In press.Google Scholar
  10. Monod, J., Wyman, J., and Changeux, J.P. (1965). On the nature of allosteric transitions: A plausible model. J.Mol.Biol. 12: 88.PubMedCrossRefGoogle Scholar
  11. Motakawa, Y., Hayashi, N., and Kikuchi, G. (1964). On the reactivity of hemoglobin M Iwate. Arch.Biochem.Biophys. 105: 612.CrossRefGoogle Scholar
  12. Muirhead, H., Cox, J.M., Mazzarella, L., and Perutz, M.F. (1967). Structure and function of haemoglobin. III. A three-dimensional Fourier synthesis of human deoxyhaemoglobin at 5.5 Å resolution. J.Mol.Biol. 28: 117.PubMedCrossRefGoogle Scholar
  13. Muirhead, H., and Greer, J. (1970). Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 3.5 8. resolution. Nature, 228: 516.PubMedCrossRefGoogle Scholar
  14. Perutz, M.F. (1968). Preparation of haemoglobin crystals. J.Cryst. Growth. 2: 54.CrossRefGoogle Scholar
  15. Perutz, M.F. (1970). Stereochemistry of cooperative effects in haemoglobin. Nature, 228: 726.PubMedCrossRefGoogle Scholar
  16. Perutz, M.F. (1972). The nature of haem-haem interaction. Nature. In press.Google Scholar
  17. Perutz, M.F., Liquori, A.M., and Eirich, F. (1951). X-ray and solubility studies of the haemoglobin of sickle-cell anaemia patients. Nature. 167: 929.PubMedCrossRefGoogle Scholar
  18. Richards, F.M. (1968). The matching of physical models to three- dimensional electron-density maps: A simple optical device. J.Mol.Biol. 37: 225.PubMedCrossRefGoogle Scholar
  19. Rubin, M.M., and Changeux, J.-P. (1966). On the nature of allosteric transitions: Implications of non-exclusive ligand binding. J.Mol.Biol. 21: 265.PubMedCrossRefGoogle Scholar
  20. Smith, D.W., and Williams, R.J.P. (1970). The spectra of ferric haems and haemoproteins. Structure and Bonding. 7: 1.CrossRefGoogle Scholar
  21. Udem, L., Ranney, H.M., Bunn, H.F., and Pisciotta, A. (1970). Some observations on the properties of hemoglobin M Milwaukee-1. J.Mol.Biol. 48: 489.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • M. F. Perutz
    • 1
  • P. D. Pulsinelli
    • 1
  • Helen M. Ranney
    • 2
  1. 1.MRC Laboratory of Molecular BiologyCambridgeEngland
  2. 2.Department of MedicineE.J. Meyer Memorial HospitalBuffaloUSA

Personalised recommendations