TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 24 March 1997
Last modified: 16 April 1999

Reviews on structure and function of globins

Reviews

  1. Ackers, G.K., Doyle, M.L., Myers, D. and Daugherty, M.A. (1992) Molecular code for cooperativity in hemoglobin. Science 255, 54-63.
  2. Alayash, A.I. and Cashon, R.E. (1995) Hemoglobin and free radicals: implications for the development of a safe blood substitute. Mol. Med. Today 1, 122-127.
  3. Andrin, C. and Spencer, C. (1994) The intricacies of ß­globin gene expression. Biochem. Cell Biol. 72, 377-380.
  4. Antonini, E. and Chiancone, E. (1977) Assembly of multisubunit respiratory proteins. Annu. Rev. Biophys. Bioeng. 6, 239-271.
  5. Arnold, E.V. and Bohle, D.S. (1996) Isolation and oxygenation reactions of nitrosylmyoglobins. Methods Enzymol. 269, 41-55.
  6. Aronson, H.E., Royer, W.E. and Hendrickson, W.A. (1994) Quantification of tertiary structural conservation despite primary sequence drift in the globin fold. Protein Science 3, 1706-1711.
  7. Baldwin, J.M. (1975) Structure and function of haemoglobin. Prog. Biophys. Mol. Biol. 29, 225-320.
  8. Barrick, D. (1995) Depletion and replacement of protein metal ligands. Curr. Opin. Biotechnol. 6, 411-418.
  9. Bayer, E. and Schretzmann, P. (1967) Reversible Oxygenierung von Metallkomplexen. Structure and Bonding 2, 181-250.
  10. Bemski, G. (1997) Contribution of Electron Paramagnetic Resonance to the studies of hemoglobin: The nitrosylhemoglobin system. Mol. Biol. Rep. 24, 263-269.
  11. Blau, C.A. and Stamatoyannopoulos, G. (1994) Hemoglobin switching and its clinical implications. Curr. Opin. Hematol. 1, 136-142.
  12. Bolognesi, M., Bordo, D., Rizzi, M., Tarricone, C. and Ascenzi, P. (1997) Nonvertebrate hemoglobins: structural bases for reactivity. Prog. Biophys. Mol. Biol. 68, 29-68.
  13. Brittain, T. (1991) Cooperativity and allosteric regulation in non­mammalian vertebrate haemoglobins. Comp. Biochem. Physiol. B 99, 731-740.
  14. Bunn, H.F. (1978) Mutant hemoglobins having elongated chains. Hemoglobin 2, 1-28.
  15. Buse, G. (1971) The present position of hemoglobin research. Angew. Chem. Int. Ed. Engl. 10, 663-673.
  16. Clementi, M.E., Condo, S.G., Castagnola, M. and Giardina, B. (1994) Hemoglobin function under extreme life conditions. Eur. J. Biochem. 223, 309-317.
  17. Coates, M.L. (1975) Hemoglobin function in the vertebrates: an evolutionary model. J. Mol. Evol. 6, 285-307.
  18. Cupane, A., Leone, M., Vitrano, E. and Cordone, L. (1995) Low temperature optical absorption spectroscopy: An approach to the study of stereodynamic properties of hemeproteins. Eur. Biophys. J. 23, 385-398.
  19. Dixon, B. and Pohajdak, B. (1992) Did the ancestral globin gene of plants and animals contain only two introns? Trends Biochem. Sci. 17, 486-488.
  20. Dyer, R.B., Gai, F., Woodruff, W.H., Gilmanshin, R. and Callender, R.H. (1998) Infrared studies of fast events in protein folding. Acc. Chem. Res. 31, 709-716.
  21. Eaton, W.A., Henry, E.R., Hofrichter, J. and Mozzarelli, A. (1999) Is cooperative oxygen binding by hemoglobin really understood? Nature Struct. Biol 6, 351-358.
  22. Erskine, R.W. and Field, B.O. (1976) Reversible oxygenation. Structure and Bonding 28, 1-50.
  23. Evans, T., Felsenfeld, G. and Reitman, M. (1990) Control of globin gene transcription. Annu. Rev. Cell Biol. 6, 95-124.
  24. Fantoni, A., Farace, M.G. and Gambari, R. (1981) Embryonic hemoglobins in man and other mammals. Blood 57, 623-633.
  25. Frantzen, F. (1997) Chromatographic and electrophoretic methods for modified hemoglobins. J. Chromatogr. B699, 269-286.
  26. Garnica, A.D. (1981) Trace metals and hemoglobin metabolism. Ann. Clin. Lab. Sci. 11, 220-228.
  27. Giardina, B., Messana, I., Scatena, R. and Castagnola, M. (1995) The multiple functions of hemoglobin. Crit. Rev. Biochem. Mol. Biol. 30, 165-196.
  28. Goldanskii, V.I., Krupianskii, Yu.F. and Frolov, E.N. (1983) Role of conformational sub­states on the reaction capacity of protein molecules. Mol. Biol. (Moscow) 17, 532-542.
  29. Gruebele, M., Sabelko, J., Ballew, R. and Ervin, J. (1998) Laser temperature jump induced protein refolding. Acc. Chem. Res. 31, 699-707.
  30. Guillochon, D., Esclade, L., Cambou, B. and Thomas, D. (1984) Hydroxylation by hemoglobin­containing systems: activities and regioselectivities. Ann. N. Y. Acad. Sci. 434, 214-218.
  31. Harkness, D.R. (1980) Hematological and clinical features of sickle cell diseases: a review. Hemoglobin 4, 313-334.
  32. Hendrickson, W.A. and Royer, W.E. (1986) Principles in the assembly of annelid erythrocruorins. Biophys. J. 49, 177-189.
  33. Henry, E.R., Jones, C.M., Hofrichter, J. and Eaton, W.A. (1997) Can a two­state MWC allosteric model explain hemoglobin kinetics? Biochemistry 36, 6511-6528.
  34. Henry, Y., Lepoivre, M., Drapier, J.­C., Ducrocq, C., Boucher, J.­L. and Guissani, A. (1993) EPR characterization of molecular targets for NO in mammalian cells and organelles. FASEB J. 7, 1124-1134.
  35. Hsia, C.C. (1998) Respiratory function of hemoglobin. New Engl. J. Med. 338, 239-247.
  36. Huisman, T.H. and Schroeder, W.A. (1970a) I. Alteration in the properties of human hemoglobin A by variation in structure: A correlation of structure and function. CRC Crit. Rev. Clin. Lab. Sci. 1, 473-489.
  37. Huisman, T.H. and Schroeder, W.A. (1970b) II. Binding of organic phosphates to hemoglobin. CRC Crit. Rev. Clin. Lab. Sci. 1, 490-501.
  38. Huisman, T.H. and Schroeder, W.A. (1970c) III. Hemoglobin heterogeneity and structural genes. CRC Crit. Rev. Clin. Lab. Sci. 1, 502-514.
  39. Huisman, T.H. and Schroeder, W.A. (1970d) IV. The chemical heterogeneity of the chain from human fetal hemoglobin. CRC Crit. Rev. Clin. Lab. Sci. 1, 514-526.
  40. Imai, K., Shih, D.T., Tame, J., Nagai, K. and Miyazaki, G. (1989) Structural and functional consequences of amino acid substitutions in hemoglobin as manifested in natural and artificial mutants. Protein Seq. Data Anal. 2, 81-86.
  41. Kalyanaraman, B. (1996) Detection of nitric oxide by electron spin resonance in chemical, photochemical, cellular, physiological, and pathophysiological systems. Methods Enzymol. 268, 168-187.
  42. Kapp, O.H., Moens, L., Vanfleteren, J., Trotman, C.N.A., Suzuki, T. and Vinogradov, S.N. (1995) Alignment of 700 globin sequences: Extent of amino acid substitution and its correlation with variation in volume. Protein Science 4, 2179-2190.
  43. Karlsson, S. and Nienhuis, A.W. (1985) Developmental regulation of human globin genes. Annu. Rev. Biochem. 54, 1071-1108.
  44. Kavsan, V.M. and Zolotukhin, S.B. (1982) Structure of human globin genes. Mol. Biol. (Moscow) 16, 1-27.
  45. Labie, D. and Wajcman, H. (1972) Les hemoglobines instables. [Unstable hemoglobins] Biochimie 54, 625-631.
  46. Lalaiants, I.E. and Milovanova, L.S. (1990) Valine substitution. Biofizika (Moscow) 35, 231-235.
  47. Lamy, J.N., Green, B.N., Toulmond, A., Wall, J.S., Weber, R.E. and Vinogradov, S.N. (1996) Giant hexagonal bilayer hemoglobins. Chem. Rev. 96, 3113-3124.
  48. Leder, P., Konkel, D., Leder, A. and Nishioka, Y. (1982) Globin genes: a paradigm of gene structure, function, and evolution. Natl. Cancer Inst. Monogr. 60, 49-54.
  49. Lim, M., Jackson, T.A. and Anfinrud, P.A. (1997) Modulating carbon monoxide binding affinity and kinetics in myoglobin: The roles of the distal histidine and the heme pocket docking site. J. Biol. Inorg. Chem. 2, 531-536.
  50. Mangum, C.P. (1985) Oxygen transport in invertebrates. Am. J. Physiol. 248, R505-R514.
  51. Manning, J.M., Dumoulin, A., Li, X. and Manning, L.R. (1998) Normal and abnormal protein subunit interactions in hemoglobins. J. Biol. Chem. 273, 19359-19362.
  52. Marden, M.C., Griffon, N. and Poyart, C. (1995) Oxygen delivery and autoxidation of hemoglobin. Transfus. Clin. Biol. 2, 473-480.
  53. Marden, M.C., Kiger, L., Poyart, C. and Edelstein, S.J. (1998) Identifying the conformational state of bi­liganded haemoglobin. Cell. Mol. Life Sci. 54, 1365-1384.
  54. Martin, D.I.K., Fiering, S. and Groudine, M. (1996) Regulation of ß­globin gene expression: straightening out the locus. Curr. Opin. Genet. Dev. 6, 488-495.
  55. Martz, E. (1997) Hemoglobin. http://www.umass.edu/microbio/chime/hemoglob/2frmcont.htm.
  56. Mattevi, A., Rizzi, M. and Bolognesi, M. (1996) New structures of allosteric proteins revealing remarkable conformational changes. Curr. Opin. Struct. Biol. 6, 824-829.
  57. Milner, P.F. and Wrightstone, R.N. (1981) The unstable hemoglobins: a review. Prog. Clin. Biol. Res. 51, 197-222.
  58. Moens, L., Vanfleteren, J., Van de Peer, Y., Peeters, K., Kapp, O.H., Czeluzniak, J., Goodman, M., Blaxter, M. and Vinogradov, S.N. (1996) Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure­function relationships. Mol. Biol. Evol. 13, 324-333.
  59. Moffat, K. (1980) Structure-function relationships in hemoglobins: scientific aspects. Tex. Rep. Biol. Med. 40, 191-198.
  60. Murayama, M. (1971) The chemical and the three­dimensional structure of human hemoglobin. Ann. Clin. Lab. Sci. 1, 1-9.
  61. Murray, L.P., Hofrichter, J., Henry, E.R. and Eaton, W.A. (1988) Time­resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin. Biophys. Chem. 29, 63-76.
  62. Nagai, K., Luisi, B. and Shih, D. (1988) Evolution of haemoglobin studied by protein engineering. Bioessays 8, 79-82.
  63. Nagel, R.L. and Bookchin, R.M. (1974) Human hemoglobin mutants with abnormal oxygen binding. Semin. Hematol. 11, 385-403.
  64. Olson, J.S. and Phillips, G.N., Jr. (1997) Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand. J. Biol. Inorg. Chem. 2, 544-552.
  65. Orkin, S.H. and Kazazian, H.H., Jr. (1984) The mutation and polymorphism of the human ß­globin gene and its surrounding DNA. Annu. Rev. Genet. 18, 131-171.
  66. Paoletti, C. (1967) La structure des hemoglobines et ses implications fonctionnelles. [The structure of hemoglobins and its functional implications] Ann. Biol. Clin. (Paris) 25, 37-68.
  67. Pauling, L. (1980) The normal hemoglobins and the hemoglobinopathies: background. Tex. Rep. Biol. Med. 40, 1-7.
  68. Perutz, M.F. (1969) Structure and function of hemoglobin. Harvey Lect. 63, 213-261.
  69. Perutz, M.F. (1976) Structure and mechanism of haemoglobin. Br. Med. Bull. 32, 195-208.
  70. Perutz, M.F. (1979) Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. Annu. Rev. Biochem. 48, 327-386.
  71. Perutz, M.F. (1983) Species adaptation in a protein molecule. Mol. Biol. Evol. 1, 1-28.
  72. Perutz, M.F. (1989a) Myoglobin and haemoglobin: role of distal residues in reactions with haem ligands. Trends Biochem. Sci. 14, 42-44.
  73. Perutz, M.F. (1989b) Mechanisms of cooperativity and allosteric regulation in proteins. Q. Rev. Biophys. 22, 139-236.
  74. Perutz, M.F., Wilkinson, A.J., Paoli, M. and Dodson, G.G. (1998) The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu. Rev. Biophys. Biomol. Struct. 27, 1-34.
  75. Phillips, G.N., Jr. and Pettitt, B.M. (1995) Structure and dynamics of the water around myoglobin. Protein Science 4, 149-158.
  76. Poyart, C., Girard, F., Bursaux, E. and Bohn, B. (1981) Bases structurales des proprietes fonctionnelles de l'hemoglobine. [Structural basis for the functional properties of hemoglobin] Ann. Biol. Clin. (Paris) 39, 213-222.
  77. Proudfoot, N.J., Shander, M.H., Manley, J.L., Gefter, M.L. and Maniatis, T. (1980) Structure and in vitro transcription of human globin genes. Science 209, 1329-1336.
  78. Rachmilewitz, E.A. (1974) Denaturation of the normal and abnormal hemoglobin molecule. Semin. Hematol. 11, 441-462.
  79. Rahbar, S. (1980) Glycosylated hemoglobins. Tex. Rep. Biol. Med. 40, 373-385.
  80. Rieder, R.F. (1974) Human hemoglobin stability and instability: molecular mechanisms and some clinical correlations. Semin. Hematol. 11, 423-440.
  81. Rifkind, J.M. (1988) Hemoglobin. In Eichhorn, G.L. and Marzilli, L.G., Eds. Advances in Inorganic Biochemistry, vol. 7: Heme Proteins. Elsevier, New York, pp. 155-244.
  82. Riggs, A. (1965) Functional properties of hemoglobins. Physiol Rev. 45, 619-673.
  83. Rosa, J. (1981) Les genes de i'hemoglobine humaine et leur expression. [The genes of human hemoglobins and their expression] Nouv. Rev. Fr. Hematol. 23, 79-88.
  84. Rosa, J., Wacjman, H. and Beuzard, Y. (1971) Structure des hemoglobines normales. [Structure of normal hemoglobins] Nouv. Rev. Fr. Hematol. 11, 33-46.
  85. Rousseau, D.L. and Ondrias, M.R. (1983) Resonance Raman scattering studies of the quaternary structure transition in hemoglobin. Annu. Rev. Biophys. Bioeng. 12, 357-380.
  86. Ruckpaul, K. (1967) Struktur-Funktionsbeziehungen bei Hämoglobinanomalien. [Structural-functional relationsphps in hemoglobin anomalies] Dtsch. Gesundheitsw. 22, 1681-1686.
  87. Ruckpaul, K. (1969) Struktur-Funktionsbeziehungen abnormer Hämoglobine. II. [Structure-function relations of abnormal hemoglobins. II] Dtsch. Gesundheitsw. 24, 148-156.
  88. Ruckpaul, K. and Jänig, G.R. (1972) Beziehungen zwischen Strukur und Funktion abnormer Hämoglobine. [Relationships between structure and function of abnormal hemoglobins] Dtsch. Gesundheitsw. 27, 1057-1063.
  89. Sage, J.T. (1997) Myoglobin and CO: structure, energetics, and disorder. J. Biol. Inorg. Chem. 2, 537-543.
  90. Sanders, K.E., Ackers, G. and Sligar, S.G. (1996) Engineering and design of blood substitutes. Curr. Opin. Struct. Biol. 6, 534-540.
  91. Schapira, G., Kruh, J., Labie, D., Maleknia, N. and Blum, N. (1970) Le controle genetique de la biosynthese de l'hemoglobine et ses anomalies. [Genetic control of hemoglobin biosynthesis and its abnormalities] Ann. Med. Interne (Paris) 121, 619-623.
  92. Schrier, S.L. (1994) Thalassemia: pathophysiology of red cell changes. Annu. Rev. Med. 45, 211-218.
  93. Schroeder, W.A. (1977) The human gamma­chain variants. A review. Hemoglobin 1, 513-525.
  94. Schroeder, W.A. and Jones, R.T. (1965) Some aspects of the chemistry and function of human and animal hemoglobins. Fortschr. Chem. Org. Naturst. 23, 113-194.
  95. Serjeant, G.R. (1995) Natural history and determinants of clinical severity of sickle cell disease. Curr. Opin. Hematol. 2, 103-108.
  96. Shikama, K. (1985) Nature of the FeO2 bonding in myoglobin: An overview from physical to clinical biochemistry. Experientia 41, 701-706.
  97. Shikama, K. (1998) The molecular mechanism of autoxidation for myoglobin and hemoglobin: A venerable puzzle. Chem. Rev. 98, 1357-1374.
  98. Shikama, K., Matsuoka, A. and Iwaasa, H. (1995) The unique structures of protozoan myoglobin and yeast hemoglobin: An evolutionary diversity. Int. J. Biochem. Cell Biol. 27, 1107-1115.
  99. Shulman, R.G., Hopfield, J.J. and Ogawa, S. (1975) Allosteric interpretation of haemoglobin properties. Q. Rev. Biophys. 8, 325-420.
  100. Slebodnick, C. and Ibers, J.A. (1997) Myoglobin models and steric origins of the discrimination between O2 and CO. J. Biol. Inorg. Chem. 2, 521-525.
  101. Smith, D.W. (1980) The molecular biology of mammalian hemoglobin synthesis. Ann. Clin. Lab. Sci. 10, 116-122.
  102. Smith, R.P. (1991) Chemicals reacting with various forms of hemoglobin: biological significance, mechanisms, and determination. J. Forensic Sci. 36, 662-672.
  103. Spiro, T.G. (1985) Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. Adv. Protein Chem. 37, 111-159.
  104. Spiro, T.G. and Kozlowski, P.M. (1997) Will the real FeCO please stand up? J. Biol. Inorg. Chem. 2, 516-520.
  105. Spivak, V.A. (1986) Human hemoglobin: polymorphism, neutrality of variants, evolutionary aspect. Mol. Biol. (Moscow) 20, 789-797.
  106. Stamatoyannopoulos, G. (1972) The molecular basis of hemoglobin disease. Annu. Rev. Genet. 6, 47-70.
  107. Suzuki, T. and Imai, K. (1998) Evolution of myoglobin. Cell. Mol. Life Sci. 54, 979-1004.
  108. Telford, J.R., Wittung­Stafshede, P., Gray, H.B. and Winkler, J.R. (1998) Protein folding triggered by electron transfer. Acc. Chem. Res. 31, 755-763.
  109. Toulmond, A. (1985) Circulating respiratory pigments in marine animals. Symp. Soc. Exp. Biol. 39, 163-206.
  110. Vella, F. (1977) Variation in hemoglobin A2. Hemoglobin 1, 619-650.
  111. Vinogradov, S.N. (1985) The structure of invertebrate extracellular hemoglobins (erythrocruorins and chlorocruorins). Comp. Biochem. Physiol. B 82, 1-15.
  112. Vinogradov, S.N., Hall, B.C. and Shlom, J.M. (1976) Subunit homology in invertebrate hemoglobins: a primitive heme binding chain? Comp. Biochem. Physiol. B 53, 89-92.
  113. Vinogradov, S.N., Sharma, P.K. and Walz, D.A. (1991) Iron and heme contents of the extracellular hemoglobins and chlorocruorins of annelids. Comp. Biochem. Physiol. B 98, 187-194.
  114. Vinogradov, S.N., Walz, D.A. and Pohajdak, B. (1992) Organization of non­vertebrate globin genes. Comp. Biochem. Physiol. B 103, 759-773.
  115. Vinogradov, S.N., Walz, D.A., Pohajdak, B., Moens, L., Kapp, O.H., Suzuki, T. and Trotman, C.N. (1993) Adventitious variability? The amino acid sequences of nonvertebrate globins. Comp. Biochem. Physiol. B 106, 1-26.
  116. Weatherall, D.J., Wood, W.G., Jones, R.W. and Clegg, J.B. (1985) The developmental genetics of human hemoglobin. Prog. Clin. Biol. Res. 191, 3-25.
  117. Webster, D.A. (1988) Structure and function of bacterial hemoglobin and related proteins. In Eichhorn, G.L. and Marzilli, L.G., Eds. Advances in Inorganic Biochemistry, vol. 7: Heme Proteins. Elsevier, New York, pp. 245-265.
  118. Weissbluth, M. (1967) The physics of hemoglobin. Structure and Bonding 2, 1-125.
  119. Went, L.N. (1979) Abnormal hemoglobins caused by deletions: a review. Hemoglobin 3, 117-136.
  120. Winterbourn, C.C. (1990) Oxidative reactions of hemoglobin. Methods Enzymol. 186, 265-272.
  121. Wood, E.J. (1980) The oxygen transport and storage proteins of invertebrates. Essays Biochem. 16, 1-47.
  122. Wood, W.G. (1996) The complexities of ß globin gene regulation. Trends Genet. 12, 204-206.

Books

  1. Antonini, E. and Brunori, M. (1971) Hemoglobin and myoglobin in their reactions with ligands. North­Holland, Amsterdam.
  2. Antonini, E., Rossi­Bernardi, L. and Chiancone, E., Eds. (1981) Methods Enzymol. 76. Hemoglobins (Part A). Academic Press, San Diego.
  3. Blood and Tissue Oxygen Carriers. Springer­Verlag, Berlin.
  4. Everse, J., Vandegriff, K.D. and Winslow, R.M., Eds. (1994) Methods Enzymol. 231. Hemoglobins (Part B): Biochemical and Analytical Methods. Academic Press, San Diego.
  5. Everse, J., Vandegriff, K.D. and Winslow, R.M., Eds. (1994) Methods Enzymol. 232. Hemoglobins (Part C): Biophysical Methods. Academic Press, San Diego.

Nobel Prize

  1. Perutz, M.F. and Kendrew, J.C. The Nobel Prize in Chemistry 1962 "for their studies of the structures of globular proteins".
Bibliography on structural studies of globins: A-H, I-P and Q-Z