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Last modified: 16 April 1999

Bibliography on structural studies of globins, A-H

A B C D E F G H
  1. Abraham, D.J., Perutz, M.F. and Phillips, S.E.V. (1983a) Physiological and x­ray studies of potential antisickling agents. Proc. Natl. Acad. Sci. USA 80, 324-328.
  2. Abraham, D.J., Phillips, S.E.V. and Kennedy, P.E. (1983b) Methylphenylmercury: a novel heavy atom reagent for protein crystallography. J. Mol. Biol. 170, 249-252.
  3. Abraham, D.J., Peascoe, R.A., Randad, R.S. and Panikker, J. (1992) X­ray diffraction study of di and tetra­ligated T­state hemoglobin from high salt crystals. J. Mol. Biol. 227, 480-492.
  4. Abraham, D.J., Kister, J., Joshi, G.S., Marden, M.C. and Poyart, C. (1995) Intrinsic activity at the molecular level: E.J. Ariens' concept visualized. J. Mol. Biol. 248, 845-855.
  5. Achterhold, K., Keppler, C., van Bürck, U., Potzel, W., Schindelmann, P., Knapp, E.­W., Melchers, B., Chumakov, A.I., Baron, A.Q.R., Rüffer, R. and Parak, F. (1996) Temperature dependent inelastic X­ray scattering of synchrotron radiation on myoglobin analyzed by the Mössbauer effect. Eur. Biophys. J. 25, 43-46.
  6. Adachi, S., Sunohara, N., Ishimori, K. and Morishima, I. (1992) Structure and ligand binding properties of leucine 29(B10) mutants of human myoglobin. J. Biol. Chem. 267, 12614-12621.
  7. Adachi, S., Nagano, S., Ishimori, K., Watanabe, Y., Morishima, I., Egawa, T., Kitagawa, T. and Makino, R. (1993) Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site­directed mutagenesis as models for P­450, chloroperoxidase, and catalase. Biochemistry 32, 241-252.
  8. Adachi, K., Lai, C.H., Konitzer, P., Donahee, M., Campbell, A. and Surrey, S. (1994) Crystallization of recombinant hemoglobins with basic amino acid substitutions (Lys and Arg) at the ß6 position. Blood 84, 1309-1313.
  9. Adachi, S. and Morishima, I. (1992) Modification of the distal histidyl imidazole in myoglobin to N­tetrazole­substituted imidazole and its effects on the heme environmental structure and ligand binding properties. Biochemistry 31, 8613-8618.
  10. Adachi, S., Nagano, S., Watanabe, Y., Ishimori, K. and Morishima, I. (1991) Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site­directed mutagenesis: characterization and their catalytic activities. Biochem. Biophys. Res. Commun. 180, 138-144.
  11. Ahmad, M.B. and Kincaid, J.R. (1983) Haem disorder in modified myoglobins. Effect of reconstitution procedures. Biochem. J. 215, 117-122.
  12. Aime, S., Fasano, M., Paoletti, S., Cutruzzolà, F., Desideri, A., Bolognesi, M., Rizzi, M. and Ascenzi, P. (1996) Structural determinants of fluoride and formate binding to hemoglobin and myoglobin: crystallographic and 1H­NMR relaxometric study. Biophys. J. 70, 482-488.
  13. Alam, S.L. and Satterlee, J.D. (1994) Complete heme proton hyperfine resonance assignments of the Glycera dibranchiata component IV metcyano monomer hemoglobin. Biochemistry 33, 4008-4018.
  14. Alam, S.L., Dutton, D.P. and Satterlee, J.D. (1994) Expression of recombinant monomer hemoglobins (component IV) from the marine annelid Glycera dibranchiata: evidence for primary sequence positional regulation of heme rotational disorder. Biochemistry 33, 10337-10344.
  15. Alben, J.O., Beece, D., Bowne, S.F., Doster, W., Eisenstein, L., Frauenfelder, H., Good, D., McDonald, J.D., Marden, M.C., Moh, P.P., Reinisch, L., Reynolds, A.H., Shyamsunder, E. and Yue, K.T. (1982) Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures. Proc. Natl. Acad. Sci. USA 79, 3744-3748.
  16. Allocatelli, C.T., Cutruzzolà, F., Brancaccio, A., Brunori, M., Qin, J. and La Mar, G.N. (1993) Structural and functional characterization of sperm whale myoglobin mutants: role of arginine (E10) in ligand stabilization. Biochemistry 32, 6041-6049.
  17. Alter, G.M. (1983) Comparison of solution and crystalline state protein structures. Photoacoustic study of horse and human hemoglobins. J. Biol. Chem. 258, 14966-14973.
  18. Amiconi, G., Santucci, R., Coletta, M., Castellano, A.C., Giovannelli, A., Dell'Ariccia, M., Longa, S.D., Barteri, M., Burattini, E. and Bianconi, A. (1989) Influence of globin structure on the heme in dromedary carbonmonoxyhemoglobin. Biochemistry 28, 8547-8553.
  19. Anderson, N.L. (1974) Hemoglobin San Diego [ß109 (G11) Val->Met]. Crystal structure of the deoxy form. J. Clin. Invest. 53, 329-333.
  20. Anderson, N.L. (1976) Hemoglobin St. Louis [ß28 (B10) Leu->Gln]: crystal structure of the fully reduced (deoxy) form. J. Clin. Invest. 58, 1107-1109.
  21. Andersson, L.A., Loehr, T.M., Lim, A.R. and Mauk, A.G. (1984) Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron­chlorin prosthetic group. J. Biol. Chem. 259, 15340-15349.
  22. Anderton, C.L., Hester, R.E. and Moore, J.N. (1995) Resonance Raman spectroscopy reveals novel ligation properties of the porcine myoglobin double mutant H64V/V68H. Biochim. Biophys. Acta 1253, 1-4.
  23. Anderton, C.L., Hester, R.E. and Moore, J.N. (1997) A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy­myoglobins reveals the effects of polarity. Biochim. Biophys. Acta 1338, 107-120.
  24. Arents, G. and Love, W.E. (1989) Glycera dibranchiata hemoglobin. Structure and refinement at 1.5 Å resolution. J. Mol. Biol. 210, 149-161.
  25. Armstrong, R.S., Irwin, M.J. and Wright, P.E. (1980) Resonance Raman evidence for constrained heme structure in soybean leghemoglobin and its derivatives. Biochem. Biophys. Res. Commun. 95, 682-689.
  26. Arnold, E.V., Bohle, D.S. and Jordan, P.A. (1999) Reversible and irreversible hemichrome generation by the oxygenation of nitrosylmyoglobin. Biochemistry 38, 4750-4756.
  27. Arnone, A. (1976) X­ray and functional studies of hemoglobins Nancy and Cochin­Port­Royal. J. Biol. Chem. 251, 5875-5880.
  28. Arnone, A. and Perutz, M.F. (1974) Structure of inositol hexaphosphate-human deoxyhaemoglobin complex. Nature 249, 34-36.
  29. Arnone, A., Rogers, P., Blough, N.V., McGourty, J.L. and Hoffman, B.M. (1986) X­ray diffraction studies of a partially liganded hemoglobin, [alpha(FeII­CO)ß(MnII)]2. J. Mol. Biol. 188, 693-706.
  30. Arutiunian, E.G. (1981) Structure of leghemoglobin. Mol. Biol. (Moscow) 15, 27-44 (in Russian).
  31. Asakura, T., Adachi, K., Wiley, J.S., Fung, L.W., Ho, C., Kilmartin, J.V. and Perutz, M.F. (1976) Structure and function of haemoglobin Philly [Tyr C1 (35)ß->Phe]. J. Mol. Biol. 104, 185-195.
  32. Ascoli, F., Chiancone, E., Santucci, R. and Antonini, E. (1979) CD studies on the heme environment in erythrocruorins and chlorocruorins. FEBS Lett. 107, 117-120.
  33. Asher, S.A. (1981) Resonance Raman spectroscopy of hemoglobin. Methods Enzymol. 76, 371-413.
  34. Asher, S.A. (1993) UV resonance Raman spectroscopy for analytical, physical, and biophysical chemistry. Part 2. Anal. Chem. 65, 201A-210A.
  35. Asher, S.A., Larkin, P.J. and Teraoka, J. (1991) Ultraviolet resonance Raman and absorption difference spectroscopy of myoglobins: titration behavior of individual tyrosine residues. Biochemistry 30, 5944-5954.
  36. Atamian, M. and Bocian, D.F. (1987) Resonance Raman studies of acetylheme­reconstituted myoglobins. Characterization of 2­ versus 4­substituent/protein interactions. Biochemistry 26, 8319-8326.
  37. Austin, R.H. and Rothberg, L.J. (1994) Picosecond infrared spectroscopy of hemoglobin and myoglobin. Methods Enzymol. 232, 176-204.
  38. Bakan, D.A., Saltman, P., Theriault, Y. and Wright, P.E. (1991) Kinetics and mechanisms of reduction of Cu(II) and Fe(III) complexes by soybean leghemoglobin alpha. Biochim. Biophys. Acta 1079, 182-196.
  39. Balko, B. (1981) Application of Mössbauer spectroscopy to hemoglobin studies. Methods Enzymol. 76, 329-354.
  40. Banci, L., Bertini, I., Marconi, S. and Pierattelli, R. (1993) 1H­NMR study of reduced heme proteins myoglobin and cytochrome P450. Eur. J. Biochem. 215, 431-437.
  41. Banci, L., Pierattelli, R. and Turner, D.L. (1995) Determination of haem electronic structure in cytochrome b5 and metcyanomyoglobin. Eur. J. Biochem. 232, 522-527.
  42. Bardakdjian­Michau, J., Galacteros, F. and Craescu, C.T. (1990) Functional and NMR studies of Hb Sassari (Asp­126alpha->His). Role of the inter­subunit contacts in the affinity control of human hemoglobin. Biochim. Biophys. Acta 1041, 250-253.
  43. Barrick, D. (1994) Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His­93->Gly. Biochemistry 33, 6546-6554.
  44. Bashford, D., Case, D.A., Dalvit, C., Tennant, L. and Wright, P.E. (1993) Electrostatic calculations of side­chain pKa values in myoglobin and comparison with NMR data for histidines. Biochemistry 32, 8045-8056.
  45. Bellelli, A. and Brunori, M. (1994) Optical measurements of quaternary structural changes in hemoglobin. Methods Enzymol. 232, 56-71.
  46. Bellelli, A., Lendaro, E., Ippoliti, R., Regan, R., Gibson, Q.H. and Brunori, M. (1993) Ligand binding and slow structural changes in chlorocruorin from Spirographis spallanzanii. Biochemistry 32, 7635-7643.
  47. Benko, B. and Yu, N.T. (1983) Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: Detection of Fe(III)-NO stretching, Fe(III)-N-O bending, and Fe(II)-N-O bending vibrations. Proc. Natl. Acad. Sci. USA 80, 7042-7046.
  48. Bennett, J.E. and Ingram, D.J.E. (1956) Analysis of crystalline hæmoglobin derivatives by paramagnetic resonance. Nature 177, 275-276.
  49. Bettati, S., Kwiatkowski, L.D., Kavanaugh, J.S., Mozzarelli, A., Arnone, A., Rossi, G.L. and Noble, R.W. (1997) Structure and oxygen affinity of crystalline des­His­146ß human hemoglobin in the T state. J. Biol. Chem. 272, 33077-33084.
  50. Bettati, S., Mozzarelli, A. and Perutz, M.F. (1998) Allosteric mechanism of haemoglobin: Rupture of salt­bridges raises the oxygen affinity of the T­structure. J. Mol. Biol. 281, 581-585.
  51. Bianconi, A., Congiu­Castellano, A., Dell'Ariccia, M., Giovannelli, A., Morante, S., Burattini, E. and Durham, P.J. (1986) Local Fe site structure in the tense­to­relaxed transition in carp deoxyhemoglobin: a XANES (x­ray absorption near edge structure) study. Proc. Natl. Acad. Sci. USA 83, 7736-7740.
  52. Biram, D. and Hester, R.E. (1994) Resonance Raman spectroscopic studies of ligated mutant myoglobins. Biochim. Biophys. Acta 1204, 207-216.
  53. Birnbaum, G.I., Evans, S.V., Przybylska, M. and Rose, D.R. (1994) 1.70 Å resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix. Acta Crystallogr. D50, 283-289.
  54. Bisig, D.A., Di Iorio, E.E., Diederichs, K., Winterhalter, K.H. and Piontek, K. (1995) Crystal structure of Asian elephant (Elephas maximus) cyano­metmyoglobin at 1.78­Å resolution. Phe29(B10) accounts for its unusual ligand binding properties. J. Biol. Chem. 270, 20754-20762.
  55. Bizzarri, A.R. and Cannistraro, S. (1992) Solvent effects on myoglobin conformational substates as studied by electron paramagnetic resonance. Biophys. Chem. 42, 79-85.
  56. Bizzarri, A.R. and Cannistraro, S. (1993) Solvent modulation of the structural heterogeneity in FeIII myoglobin samples: A low temperature EPR investigation. Eur. Biophys. J. 22, 259-267.
  57. Bizzarri, A.R., Bacci, M. and Cannistraro, S. (1993) Distribution of the iron­heme displacement as resulting from myoglobin conformational substrates: An AOM approach to the interpretation of the EPR spectra. Biophys. Chem. 46, 117-129.
  58. Björling, S.C., Goldbeck, R.A., Paquette, S.J., Milder, S.J. and Kliger, D.S. (1996) Allosteric intermediates in hemoglobin. 1. Nanosecond time­resolved circular dichroism spectroscopy. Biochemistry 35, 8619-8627.
  59. Bluemke, D.A., Carragher, B., Potel, M.J. and Josephs, R. (1988) Structural analysis of polymers of sickle cell hemoglobin. II. Sickle hemoglobin macrofibers. J. Mol. Biol. 199, 333-348.
  60. Bluhm, M.M., Bodo, G., Dintzis, H.M. and Kendrew, J.C. (1958) The crystal structure of myoglobin. IV. A Fourier projection of sperm­whale myoglobin by the method of isomorphous replacement. Proc. R. Soc. Lond. A246, 369-389.
  61. Blumberg, W.E. (1981) The study of hemoglobin by electron paramagnetic resonance spectroscopy. Methods Enzymol. 76, 312-329.
  62. Bodo, G., Dintzis, H.M., Kendrew, J.C. and Wyckoff, H.W. (1959) The crystal structure of myoglobin. V. A low­resolution three­dimensional Fourier synthesis of sperm­whale myoglobin crystals. Proc. R. Soc. Lond. A253, 70-102.
  63. Boffi, A., Ilari, A., Spagnuolo, C. and Chiancone, E. (1996) Unusual affinity of cyanide for ferrous and ferric Scapharca inaequivalvis homodimeric hemoglobin. Equilibria and kinetics of the reaction. Biochemistry 35, 8068-8074.
  64. Boffi, A., Chiancone, E., Takahashi, S. and Rousseau, D.L. (1997a) Stereochemistry of the Fe(II)- and Fe(III)-cyanide complexes of the homodimeric Scapharca inaequivalvis hemoglobin. A resonance Raman and FTIR study. Biochemistry 36, 4505-4509.
  65. Boffi, A., Chiancone, E., Peterson, E.S., Wang, J., Rousseau, D.L. and Friedman, J.M. (1997b) Dynamics of cyanide binding to ferrous Scapharca inaequivalvis homodimeric hemoglobin. Biochemistry 36, 4510-4514.
  66. Boffi, A., Zamparelli, C., Verzili, D., Ilari, A. and Chiancone, E. (1997c) Effect of the vinyl-globin interactions on the temperature­dependent broadening of the Soret spectra: A study with horse myoglobin and Scapharca dimeric hemoglobin reconstituted with unnatural 2,4­heme derivatives. Arch. Biochem. Biophys. 340, 43-51.
  67. Bogumil, R., Hunter, C.L., Maurus, R., Tang, H.L., Lee, H., Lloyd, E., Brayer, G.D., Smith, M. and Mauk, A.G. (1994) FTIR analysis of the interaction of azide with horse heart myoglobin variants. Biochemistry 33, 7600-7608.
  68. Bogumil, R., Maurus, R., Hildebrand, D.P., Brayer, G.D. and Mauk, A.G. (1995) Origin of the pH8­dependent spectroscopic properties of pentacoordinate metmyoglobin variants. Biochemistry 34, 10483-10490.
  69. Bolognesi, M., Coda, A., Gatti, G., Ascenzi, P. and Brunori, M. (1985) Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution. J. Mol. Biol. 183, 113-115.
  70. Bolognesi, M., Onesti, S., Gatti, G., Coda, A., Ascenzi, P. and Brunori, M. (1989) Aplysia limacina myoglobin. Crystallographic analysis at 1.6 Å resolution. J. Mol. Biol. 205, 529-544.
  71. Bolognesi, M., Coda, A., Frigerio, F., Gatti, G., Ascenzi, P. and Brunori, M. (1990) X­ray crystal structure of the fluoride derivative of Aplysia limacina ferric myoglobin at 2.0 Å resolution. Stabilization of the fluoride ion by hydrogen bonding to Arg66 (E10). J. Mol. Biol. 213, 621-625.
  72. Bolton, W. and Perutz, M.F. (1970) Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution. Nature 228, 551-552.
  73. Bolton, W., Cox, J.M. and Perutz, M.F. (1968) Structure and function of haemoglobin. IV. A three­dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 Å resolution. J. Mol. Biol. 33, 283-297.
  74. Bonaventura, C., Tesh, S., Faulkner, K.M., Kraiter, D. and Crumbliss, A.L. (1998) Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge ß2(NA2)His->Arg. Biochemistry 37, 496-506.
  75. Bonaventura, C., Godette, G., Tesh, S., Holm, D.E., Bonaventura, J., Crumbliss, A.L., Pearce, L.L. and Peterson, J. (1999) Internal electron transfer between hemes and Cu(II) bound at cysteine ß93 promotes methemoglobin reduction by carbon monoxide. J. Biol. Chem. 274, 5499-5507.
  76. Bondoc, L.L. and Timkovich, R. (1989) Structural characterization of nitrimyoglobin. J. Biol. Chem. 264, 6134-6145.
  77. Bondon, A., Petrinko, P., Sodano, P. and Simonneaux, G. (1986) 31P chemical shifts as structural probes for heme environments. 31P­NMR study of the binding of trimethyl phosphine to various hemoglobins and myoglobins. Biochim. Biophys. Acta 872, 163-166.
  78. Bondon, A., Sodano, P., Simonneaux, G. and Craescu, C.T. (1987) Phosphines as a new structural probe of hemoglobin. 1H­NMR evidence for perturbations in the ß heme pocket induced by a thiol reagent. Biochim. Biophys. Acta 914, 289-293.
  79. Borgstahl, G.E., Rogers, P.H. and Arnone, A. (1994a) The 1.8 Å structure of carbonmonoxy­ß4 hemoglobin. Analysis of a homotetramer with the R quaternary structure of liganded alpha2ß2 hemoglobin. J. Mol. Biol. 236, 817-830.
  80. Borgstahl, G.E., Rogers, P.H. and Arnone, A. (1994b) The 1.9 Å structure of deoxy ß4 hemoglobin. Analysis of the partitioning of quaternary­associated and ligand­induced changes in tertiary structure. J. Mol. Biol. 236, 831-843.
  81. Boyes­Watson, J. and Perutz, M.F. (1943) X­ray analysis of hæmoglobin. Nature 151, 714-716.
  82. Boyes­Watson, J., Davidson, E. and Perutz, M.F. (1947) An X­ray study of horse methaemoglobin. I. Proc. R. Soc. Lond. A191, 83-132.
  83. Boyiri, T., Safo, M.K., Danso­Danquah, R.E., Kister, J., Poyart, C. and Abraham, D.J. (1995) Bisaldehyde allosteric effectors as molecular ratchets and probes. Biochemistry 34, 15021-15036.
  84. Bracete, A.M., Sono, M. and Dawson, J.H. (1991) Effects of cyanogen bromide modification of the distal histidine on the spectroscopic and ligand binding properties of myoglobin: magnetic circular dichroism spectroscopy as a probe of distal water ligation in ferric high­spin histidine­bound heme proteins. Biochim. Biophys. Acta 1080, 264-270.
  85. Braden, B.C., Arents, G., Padlan, E.A. and Love, W.E. (1994) Glycera dibranchiata hemoglobin. X­ray structure of carbonmonoxide hemoglobin at 1.5 Å resolution. J. Mol. Biol. 238, 42-53.
  86. Bragg, W.L. and Perutz, M.F. (1952a) The external form of the haemoglobin molecule. I. Acta Crystallogr. 5, 277-283.
  87. Bragg, W.L. and Perutz, M.F. (1952b) The external form of the haemoglobin molecule. II. Acta Crystallogr. 5, 323-328.
  88. Bragg, W.L. and Perutz, M.F. (1952c) The structure of haemoglobin. I. Proc. R. Soc. Lond. A213, 425-435.
  89. Bragg, W.L. and Perutz, M.F. (1954) The structure of haemoglobin. VI. Fourier transform on the 010 plane. Proc. R. Soc. Lond. A225, 315-329.
  90. Bragg, W.L., Howells, E.R. and Perutz, M.F. (1952) Arrangement of polypeptide chains in horse methaemoglobin. Acta Crystallogr. 5, 136-141.
  91. Bragg, W.L., Howells, E.R. and Perutz, M.F. (1954) The structure of haemoglobin. II. Proc. R. Soc. Lond. A222, 33-44.
  92. Brittain, T., Baker, A.R., Butler, C.S., Little, R.H., Lowe, D.J., Greenwood, C. and Watmough, N.J. (1997) Reaction of variant sperm­whale myoglobins with hydrogen peroxide: The effects of mutating a histidine residue in the haem distal pocket. Biochem. J. 326, 109-115.
  93. Brucker, E.A., Olson, J.S., Phillips, G.N., Jr., Dou, Y. and Ikeda­Saito, M. (1996) High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin. J. Biol. Chem. 271, 25419-25422.
  94. Brunel, C., Bondon, A. and Simonneaux, G. (1992) Electron­transfer self­exchange kinetics of trimethylphosphine horse­heart myoglobin. Biochim. Biophys. Acta 1101, 73-78.
  95. Brunel, C., Bondon, A. and Simonneaux, G. (1993) Trimethylphosphine binding to horse­heart and sperm­whale myoglobins. Kinetics, proton magnetic resonance assignment and nuclear Overhauser effect investigation of the heme pocket. Eur. J. Biochem. 214, 405-414.
  96. Brzozowski, A., Derewenda, Z., Dodson, E., Dodson, G., Grabowski, M., Liddington, R., Skarzynski, T. and Vallely, D. (1984) Bonding of molecular oxygen to T state human haemoglobin. Nature 307, 74-76.
  97. Bucci, C.F. and Bucci, E. (1975) Conformational studies on the ß subunits of human hemoglobin and their arginyl­COOH peptides. Biochemistry 14, 4451-4458.
  98. Bucci, E., Razynska, A., Kwansa, H., Gryczynski, Z., Collins, J.H., Fronticelli, C., Unger, R., Braxenthaler, M., Moult, J., Ji, X. and Gilliland, G. (1996) Positive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin. Biochemistry 35, 3418-3425.
  99. Busch, M.R., Maskalick, D.G., Neireiter, G.W.,Harris, D.E. and Gurd, F.R. (1985) Aliphatic semisynthetic variants of the amino­terminal residue of sperm whale myoglobin: enrichment with 13C and determination and interpretation of terminal pK values. Biochemistry 24, 6707-6716.
  100. Busse, S.C. and Jue, T. (1994) Two­dimensional NMR characterization of the deoxymyoglobin heme pocket. Biochemistry 33, 10934-10943.
  101. Camardella, L., Caruso, C., D'Avino, R., di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G. and Perutz, M.F. (1992) Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. J. Mol. Biol. 224, 449-460.
  102. Cameron, A.D., Smerdon, S.J., Wilkinson, A.J., Habash, J., Helliwell, J.R., Li, T. and Olson, J.S. (1993) Distal pocket polarity in ligand binding to myoglobin: deoxy and carbonmonoxy forms of a threonine68 (E11) mutant investigated by X­ray crystallography and infrared spectroscopy. Biochemistry 32, 13061-13070.
  103. Carragher, B., Bluemke, D.A., Gabriel, B., Potel, M.J. and Josephs, R. (1988) Structural analysis of polymers of sickle cell hemoglobin. I. Sickle hemoglobin fibers. J. Mol. Biol. 199, 315-331.
  104. Carson, W.M., Bowers, T.R., Kitto, G.B. and Hackert, M.L. (1979) Preliminary crystallographic data on monomeric and dimeric hemoglobins from the sea cucumber, Molpadia arenicola. J. Biol. Chem. 254, 7400-7402.
  105. Carver, T.E., Brantley, R.E., Singleton, E.W., Arduini, R.M., Quillin, M.L., Phillips, G.N., Jr. and Olson, J.S. (1992) A novel site­directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate. J. Biol. Chem. 267, 14443-14450.
  106. Casale, E., Lionetti, C., Coda, A., Merli, A., Ascenzi, P., Wittenberg, J.B. and Bolognesi, M. (1991) Crystallization and preliminary data for the ferric form of Lucina pectinata hemoglobin I. J. Mol. Biol. 222, 447-449.
  107. Caughey, W.S., Shimada, H., Choc, M.G. and Tucker, M.P. (1981) Dynamic protein structures: infrared evidence for four discrete rapidly interconverting conformers at the carbon monoxide binding site of bovine heart myoglobin. Proc. Natl. Acad. Sci. USA 78, 2903-2907.
  108. Cavagnero, S., Dyson, H.J. and Wright, P.E. (1999) Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin. J. Mol. Biol. 285, 269-282.
  109. Cerda­Colón, J.F., Silfa, E. and López­Garriga, J.J. (1998) Unusual rocking freedom of the heme in the hydrogen sulfide­binding hemoglobin from Lucina pectinata. J. Am. Chem. Soc. 120, 9312-9317.
  110. Cerdonio, M., Morante, S. and Vitale, S. (1981) Magnetic susceptibility of hemoglobins. Methods Enzymol. 76, 354-371.
  111. Chacko, V.P., La Mar, G.N., Gersonde, K. and Sick, H. (1986) Proton­magnetic­resonance investigation of the dynamics of the conformational transition in allosteric monomeric insect hemoglobins. Eur. J. Biochem. 161, 375-381.
  112. Champion, P.M., Chiang, R., Münck, E., Debrunner, P.G. and Hager, L.P. (1975) Mössbauer investigations of high­spin ferrous heme proteins. II. Chloroperoxidase, horseradish peroxidase, and hemoglobin. Biochemistry 14, 4159-4166.
  113. Chan, N.­L., Rogers, P.H. and Arnone, A. (1998) Crystal structure of the S­nitroso form of liganded human hemoglobin. Biochemistry 37, 16459-16464.
  114. Chatfield, M.J. and La Mar, G.N. (1992) 1H nuclear magnetic resonance study of the prosthetic group in sulfhemoglobin. Arch. Biochem. Biophys. 295, 289-296.
  115. Chatfield, M.J., La Mar, G.N., Smith, K.M., Leung, H.K. and Pandey, R.K. (1988) Identification of the altered pyrrole in the isomeric sulfmyoglobins: Hyperfine shift patterns as indicators of ring saturation in ferric chlorins. Biochemistry 27, 1500-1507.
  116. Chi, Z. and Asher, S.A. (1998a) UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse myoglobin. Biochemistry 37, 2865-2872.
  117. Chi, Z. and Asher, S.A. (1998b) UV Raman determination of the environment and solvent exposure of Tyr and Trp residues. J. Phys. Chem. B102, 9595-9602.
  118. Chiancone, E. and Gibson, Q.H. (1989) Ligand binding to the dimeric hemoglobin from Scapharca inaequivalvis, a hemoglobin with a novel mechanism for cooperativity. J. Biol. Chem. 264, 21062-21065.
  119. Chiancone, E., Norne, J.­E. and Forsén, S. (1981) The use of NMR spectroscopy in studies of ion binding to hemoglobin. Methods Enzymol. 76, 552-559.
  120. Cho, N., Song, S. and Asher, S.A. (1994) UV resonance Raman and excited­state relaxation rate studies of hemoglobin. Biochemistry 33, 5932-5941.
  121. Choe, Y.S., Rao, S.I. and Ortiz de Montellano, P.R. (1994) Requirement of a second oxidation equivalent for ferryl oxygen transfer to styrene in the epoxidation catalyzed by myoglobin-H2O2. Arch. Biochem. Biophys. 314, 126-131.
  122. Christian, F., Unno, M., Sage, J.T., Champion, P.M., Chien, E. and Sligar, S.G. (1997) Spectroscopic effects of polarity and hydration in the distal heme pocket of deoxymyoglobin. Biochemistry 36, 11198-11204.
  123. Cocco, M.J. and Lecomte, J.T. (1990) Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study. Biochemistry 29, 11067-11072.
  124. Cocco, M.J. and Lecomte, J.T. (1994) The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS. Protein Science 3, 267-281.
  125. Cocco, M.J., Kao, Y.H., Phillips, A.T. and Lecomte, J.T. (1992) Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy. Biochemistry 31, 6481-6491.
  126. Coletta, M., Ascenzi, P., Smulevich, G., Mantini, A.R., Del Gaudio, R., Piscopo, M. and Geraci, G. (1992) Alteration of the proximal bond energy in the unliganded form of the homodimeric myoglobin from Nassa mutabilis. Kinetic and spectroscopic evidence. FEBS Lett. 296, 184-186.
  127. Coletta, M., Ascenzi, P., Polizio, F., Smulevich, G., Del Gaudio, R., Piscopo, M. and Geraci, G. (1998) Cooperative mechanism in the homodimeric myoglobin from Nassa mutabilis. Biochemistry 37, 2873-2878.
  128. Coletta, M., Angeletti, M., Ascone, I., Boumis, G., Castellano, A.C., Dell'Ariccia, M., Della Longa, S., De Sanctis, G., Priori, A.M., Santucci, R., Feis, A. and Amiconi, G. (1999) Heterotropic effectors exert more significant strain on monoligated than on unligated hemoglobin. Biophys. J. 76, 1532-1536.
  129. Collings, B.A. and Douglas, D.J. (1996) Conformation of gas­phase myoglobin ions. J. Am. Chem. Soc. 118, 4488-4489.
  130. Colotti, G., Verzili, D., Boffi, A. and Chiancone, E. (1994) Identification of the site of ferrocyanide binding involved in the intramolecular electron transfer process to oxidized heme in Scapharca dimeric hemoglobin. Arch. Biochem. Biophys. 311, 103-106.
  131. Condon, P.J. and Royer, W.E., Jr. (1994) Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7­Å resolution. J. Biol. Chem. 269, 25259-25267.
  132. Constantinidis, I. and Satterlee, J.D. (1987) Isoelectric focusing purity criteria and 1H NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata. Biochemistry 26, 7779-7786.
  133. Constantinidis, I., Satterlee, J.D., Pandey, R.K., Leung, H.K. and Smith, K.M. (1988) Assignment of selected hyperfine proton NMR resonances in the met forms of Glycera dibranchiata monomer hemoglobins and comparisons with sperm whale metmyoglobin. Biochemistry 27, 3069-3076.
  134. Conti, E., Casale, E., Ascenzi, P., Coletta, M., Condo, S.G., Merli, A., Giardina, B., Bordo, D. and Bolognesi, M. (1992) Structural study and preliminary crystallographic data for the hemoglobin from reindeer (Rangifer tarandus tarandus). Biochem. Biophys. Res. Commun. 187, 1063-1070.
  135. Conti, E., Moser, C., Rizzi, M., Mattevi, A., Lionetti, C., Coda, A., Ascenzi, P., Brunori, M. and Bolognesi, M. (1993) X­ray crystal structure of ferric Aplysia limacina myoglobin in different liganded states. J. Mol. Biol. 233, 498-508.
  136. Cooke, R.M. and Wright, P.E. (1987) Structural consequences of heme isomerism in monomeric hemoglobins from Glycera dibranchiata. Eur. J. Biochem. 166, 409-414.
  137. Cooke, R.M., Dalvit, C., Narula, S.S. and Wright, P.E. (1987) NMR studies of the heme pocket conformations of monomeric hemoglobins from Glycera dibranchiata. Implications for ligand binding. Eur. J. Biochem. 166, 399-408.
  138. Cordone, L., Ferrand, M., Vitrano, E. and Zaccai, G. (1999) Harmonic behavior of trehalose­coated carbon­monoxy-myoglobin at high temperature. Biophys. J. 76, 1043-1047.
  139. Couture, M., Das, T.K., Lee, H.C., Peisach, J., Rousseau, D.L., Wittenberg, B.A., Wittenberg, J.B. and Guertin, M. (1999) Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands. J. Biol. Chem. 274, 6898-6910.
  140. Craescu, C.T. and Mispelter, J. (1988) Assignment of proton resonances in the NMR spectrum of carbonmonoxy hemoglobin ß subunit tetramers. Eur. J. Biochem. 176, 171-178.
  141. Craescu, C.T. and Mispelter, J. (1989) Resonance assignments in the proton­NMR spectrum of carbonmonoxy hemoglobin by two­dimensional methods. Eur. J. Biochem. 181, 87-96.
  142. Craescu, C.T., Schaeffer, C., Mispelter, J., Garin, J. and Rosa, J. (1986a) High resolution NMR studies of histidine­substituted and histidine­perturbed hemoglobin variants. Histidine assignments, electrostatic interactions at the protein surface, and implications for hemoglobin S polymerization. J. Biol. Chem. 261, 7894-7901.
  143. Craescu, C.T., Poyart, C., Schaeffer, C., Garel, M.C., Kister, J. and Beuzard, Y. (1986b) Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra. J. Biol. Chem. 261, 14710-14716.
  144. Craescu, C.T., Schaeffer, C., Blouquit, Y. and Rosa, J. (1988) Proton NMR studies of human hemoglobin variants modified in the proximal side of ß heme pocket. Implications for the affinity control and cooperative mechanism. J. Biol. Chem. 263, 3250-3255.
  145. Craescu, C.T., Mispelter, J. and Blouquit, Y.(1990) Coupling of tertiary and quaternary changes in human hemoglobin: a 1D and 2D NMR study of hemoglobin Saint Mande (ßN102Y). Biochemistry 29, 3953-3958.
  146. Cretegny, I. and Edelstein, S.J. (1993) Double strand packing in hemoglobin S fibers. J. Mol. Biol. 230, 733-738.
  147. Cupane, A., Leone, M., Vitrano, E., Cordone, L., Hiltpold, U.R., Winterhalter, K.H., Yu, W. and Di Iorio, E.E. (1993) Structure­dynamics­function relationships in Asian elephant (Elephas maximus) myoglobin. An optical spectroscopy and flash photolysis study on functionally important motions. Biophys. J. 65, 2461-2472.
  148. Dalvit, C., Miura, S., de Young, A., Noble, R.W., Cerdonio, M. and Ho, C. (1984) A high­resolution proton nuclear­magnetic­resonance investigation of carp hemoglobin. Conformational differences between carp and human normal adult hemoglobins in solution. Eur. J. Biochem. 141, 255-259.
  149. Dalvit, C., Tennant, L. and Wright, P.E. (1987) 1H resonances of proximal histidine in CO complexes of hemoglobins provide a sensitive probe of coordination geometry. FEBS Lett. 213, 289-292.
  150. Daniels, B.V., Schoenborn, B.P. and Korszun, Z.R. (1997) A low­resolution low­temperature neutron diffraction study of myoglobin. Acta Crystallogr. D53, 544-550.
  151. Das, T.K., Khan, I., Rousseau, D.L. and Friedman, J.M. (1998) Preservation of the native structure in myoglobin at low pH by sol-gel encapsulation. J. Am. Chem. Soc. 120, 10268-10269.
  152. Das, T.K., Boffi, A., Chiancone, E. and Rousseau, D.L. (1999a) Hydroxide rather than histidine is coordinated to the heme in five­coordinate ferric Scapharca inaequivalvis hemoglobin. J. Biol. Chem. 274, 2916-2919.
  153. Das, T.K., Lee, H.C., Duff, S.M.G., Hill, R.D., Peisach, J., Rousseau, D.L., Wittenberg, B.A. and Wittenberg, J.B. (1999b) The heme environment in barley hemoglobin. J. Biol. Chem. 274, 4207-4212.
  154. Davies, M.J. (1991) Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta 1077, 86-90.
  155. Davies, M.J. and Puppo, A. (1992) Direct detection of a globin­derived radical in leghaemoglobin treated with peroxides. Biochem. J. 281, 197-201.
  156. Davies, M.J. and Puppo, A. (1993) Identification of the site of the globin­derived radical in leghaemoglobins. Biochim. Biophys. Acta 1202, 182-188.
  157. Deàk, J., Richard, L., Pereira, M., Chui, H.­L. and Miller, R.J.D. (1994) Picosecond phase grating spectroscopy: applications to bioenergetics and protein dynamics. Methods Enzymol. 232, 322-360.
  158. Deàk, J., Chui, H.­L., Lewis, C.M. and Miller, R.J.D. (1998) Ultrafast phase grating studies of heme proteins: Observation of the low­frequency modes directing functionally important protein motions. J. Phys. Chem. B102, 6621-6634.
  159. Decatur, S.M. and Boxer, S.G. (1995) 1H NMR characterization of myoglobins where exogenous ligands replace the proximal histidine. Biochemistry 34, 2122-2129.
  160. Decatur, S.M., DePillis, G.D. and Boxer, S.G. (1996a) Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands. Biochemistry 35, 3925-3932.
  161. Decatur, S.M., Franzen, S., DePillis, G.D., Dyer, R.B., Woodruff, W.H. and Boxer, S.G. (1996b) Trans effects in nitric oxide binding to myoglobin cavity mutant H93G. Biochemistry 35, 4939-4944.
  162. Deeb, R.S. and Peyton, D.H. (1991) 1H and 119Sn magnetic resonance study of the SnIV protoporphyrin IX complex of equine myoglobin. Structure of the porphyrin­binding pocket. J. Biol. Chem. 266, 3728-3733.
  163. Deeb, R.S. and Peyton, D.H. (1992) Proton NMR study of the interaction of tin(IV) protoporphyrin IX monomers and dimers with apomyoglobin. Biochemistry 31, 468-474.
  164. de Jongh, H.H.J., Goormaghtigh, E. and Ruysschaert, J.­M. (1997) Amide-proton exchange of water­soluble proteins of different structural classes studied at the submolecular level by infrared spectroscopy. Biochemistry 36, 13603-13610.
  165. de Haas, F., Taveau, J.­C., Boisset, N., Lambert, O., Vinogradov, S.N. and Lamy, J.N. (1996a) Three­dimensional reconstruction of the chlorocruorin of the polychaete annelid Eudistylia vancouverii. J. Mol. Biol. 255, 140-153.
  166. de Haas, F., Zal, F., Lallier, F.H., Toulmond, A. and Lamy, J.N. (1996b) Three­dimensional reconstruction of the hexagonal bilayer hemoglobin of the hydrothermal vent tube worm Riftia pachyptila by cryoelectron microscopy. Proteins 26, 241-256.
  167. de Haas, F., Zal, F., You, V., Lallier, F.H., Toulmond, A. and Lamy, J.N. (1996c) Three­dimensional reconstruction by cryoelectron microscopy of the giant hemoglobin of the polychaete worm Alvinella pompejana. J. Mol. Biol. 264, 111-120.
  168. de Haas, F., Kuchumov, A., Taveau, J.C., Boisset, N., Vinogradov, S.N. and Lamy, J.N. (1997) Three­dimensional reconstruction of native and reassembled Lumbricus terrestris extracellular hemoglobin. Localization of the monomeric globin chains. Biochemistry 36, 7330-7338.
  169. Della Longa, S., Girasole, M., Congiu Castellano, A., Bianconi, A., Kovtun, A.P. and Soldatov, A.V. (1998a) Spin­resolved X­ray absorption near edge structure (XANES) simulation of metmyoglobin. Eur. Biophys. J. 27, 541-548.
  170. Della Longa, S., Pin, S., Cortès, R., Soldatov, A.V. and Alpert, B. (1998b) Fe-heme conformations in ferric myoglobin. Biophys. J. 75, 3154-3162.
  171. De Sanctis, G., Falcioni, G., Grelloni, F., Desideri, A., Polizio, F., Giardina, B., Ascoli, F. and Brunori, M. (1991) Mini­myoglobin. Electron paramagnetic resonance and reversible oxygenation of the cobalt derivative. J. Mol. Biol. 222, 637-643.
  172. De Sanctis, G., Falcioni, G., Polizio, F., Desideri, A., Giardina, B., Ascoli, F. and Brunori, M. (1994) Mini­myoglobin: native­like folding of the NO­derivative. Biochim. Biophys. Acta 1204, 28-32.
  173. De Sanctis, G., Priori, A.M., Polizio, F., Ascenzi, P. and Coletta, M. (1998) ifferent structural effects of allosteric modulators on subunits of tetrameric ferrous nitrosylated human hemoglobin: an EPR spectroscopic study. J. Biol. Inorg. Chem. 3, 135-139.
  174. Desbois, A., Lutz, M. and Banerjee, R. (1979) Low­frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes. Biochemistry 18, 1510-1518.
  175. Desbois, A., Lutz, M. and Banerjee, R. (1981a) Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding. Biochim. Biophys. Acta 671, 177-183.
  176. Desbois, A., Lutz, M. and Banerjee, R. (1981b) Protoheme conformations in low­spin ferrohemoproteins. Resonance Raman spectroscopy. Biochim. Biophys. Acta 671, 184-192.
  177. DiFeo, T.J., Addison, A.W. and Stephanos, J.J. (1990) Kinetic and spectroscopic studies of haemoglobin and myoglobin from Urechis caupo. Distal residue effects. Biochem. J. 269, 739-747.
  178. Dodson, G.G., Richard, V.R., Tolley, S.P., Waller, D.A. and Weber, R.E. (1990) Crystallization of the rainbow trout (Salmo gairdneri) haemoglobin IV. J. Mol. Biol. 211, 691-692.
  179. Dong, A. and Caughey, W.S. (1994) Infrared methods for study of hemoglobin reactions and structures. Methods Enzymol. 232, 139-175.
  180. Dong, A., Huang, P., Zhao, X.­J., Sampath, V. and Caughey, W.S. (1994) Characterization of sites occupied by the anesthetic nitrous oxide within proteins by infrared spectroscopy. J. Biol. Chem. 269, 23911-23917.
  181. Dong, A., Huang, P., Caughey, B. and Caughey, W.S. (1995) Infrared analysis of ligand­ and oxidation­induced conformational changes in hemoglobins and myoglobins. Arch. Biochem. Biophys. 316, 893-898.
  182. Doster, W., Cusack, S. and Petry, W. (1989) Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature 337, 754-756.
  183. Dou, Y., Admiraal, S.J., Ikeda­Saito, M., Krzywda, S., Wilkinson, A.J., Li, T., Olson, J.S., Prince, R.C., Pickering, I.J. and George, G.N. (1995) Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64->Val/Val68->His double mutant. J. Biol. Chem. 270, 15993-16001.
  184. Doyle, M.A., Vitali, J., Wittenberg, J.B., Vinogradov, S.N., Walz, D.A., Edwards, B.F.P. and Martin, P.D. (1994) Crystallization of hemoglobins II and III of the symbiont­harboring clam Lucina pectinata. Acta Crystallogr. D50, 757-759.
  185. Eaton, W.A. and Hofrichter, J. (1981) Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods Enzymol. 76, 175-261.
  186. Egeberg, K.D., Springer, B.A., Martinis, S.A., Sligar, S.G., Morikis, D. and Champion, P.M. (1990) Alteration of sperm whale myoglobin heme axial ligation by site­directed mutagenesis. Biochemistry 29, 9783-9791.
  187. Eglinton, D.G., Gadsby, P.M., Sievers, G., Peterson, J. and Thomson, A.J. (1983) A comparative study of the low­temperature magnetic circular dichroism spectra of horse heart metmyoglobin and bovine liver catalase derivatives. Biochim. Biophys. Acta 742, 648-658.
  188. Eisenberger, P., Shulman, R.G., Brown, G.S. and Ogawa, S. (1976) Structure­function relations in hemoglobin as determined by X­ray absorption spectroscopy. Proc. Natl. Acad. Sci. USA 73, 491-495.
  189. Eisenberger, P., Shulman, R.G., Kincaid, B.M., Brown, G.S. and Ogawa, S. (1978) Extended X­ray absorption fine structure determination of iron-nitrogen distances in haemoglobin. Nature 274, 30-34.
  190. Eliezer, D. and Wright, P.E. (1996) Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263, 531-538.
  191. Eliezer, D., Yao, J., Dyson, H.J. and Wright, P.E. (1998) Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biol. 5, 148-155.
  192. Ellfolk, N. and Sievers, G. (1975) Circular dichroism of soybean leghemoglobin. Biochim. Biophys. Acta 405, 213-227.
  193. Ellfolk, N. and Perttila, U. (1978) Heme sulfuric anhydrides as soybean leghemoglobin structure probes. Biochim. Biophys. Acta 534, 153-159.
  194. Ellis, P.J., Appleby, C.A., Guss, J.M., Hunter, W.N., Ollis, D.L. and Freeman, H.C. (1997) Structure of ferric soybean leghemoglobin a nicotinate at 2.3 Å resolution. Acta Crystallogr. D53, 302-310.
  195. Emerson, S.D. and La Mar, G. (1990) Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two­dimensional NMR. Biochemistry 29, 1545-1556.
  196. Englander, S.W. and Englander, J.J. (1994) Structure and energy change in hemoglobin by hydrogen exchange labeling. Methods Enzymol. 232, 26-42.
  197. Ermler, U., Siddiqui, R.A., Cramm, R. and Friedrich, B. (1995) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. 14, 6067-6077.
  198. Esquerra, R.M., Goldbeck, R.A., Kim­Shapiro, D.B. and Kliger, D.S. (1998) Spectroscopic evidence for nanosecond protein relaxation after photodissociation of myoglobin-CO. Biochemistry 37, 17527-17536.
  199. Evans, S.V. and Brayer, G.D. (1988) Horse heart metmyoglobin. A 2.8­Å resolution three­dimensional structure determination. J. Biol. Chem. 263, 4263-4268.
  200. Evans, S.V. and Brayer, G.D. (1990) High­resolution study of the three­dimensional structure of horse heart metmyoglobin. J. Mol. Biol. 213, 885-897.
  201. Evans, S.V., Sishta, B.P., Mauk, A.G. and Brayer, G.D. (1994) Three­dimensional structure of cyanomet­sulfmyoglobin C. Proc. Natl. Acad. Sci. USA 91, 4723-4726.
  202. Falconi, M., Desideri, A., Cupane, A., Leone, M., Ciccotti, G., Peterson, E.S., Friedman, J.M., Gambacurta, A. and Ascoli, F. (1998) Structural and dynamic properties of the homodimeric hemoglobin from Scapharca inaequivalvis Thr­72->Ile mutant: Molecular dynamics simulation, low temperature visible absorption spectroscopy, and resonance Raman spectroscopy studies. Biophys. J. 75, 2489-2503.
  203. Fantl, W.J., Di Donato, A., Manning, J.M., Rogers, P.H. and Arnone, A. (1987) Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X­ray studies of carboxymethylated hemoglobin and X­ray studies of carbamino hemoglobin. J. Biol. Chem. 262, 12700-12713.
  204. Faulkner, K.M., Bonaventura, C. and Crumbliss, A.L. (1995) A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins. J. Biol. Chem. 270, 13604-13612.
  205. Fedorov, B.A. and Denesyuk, A.I. (1978) Sperm whale myoglobin structure in solution differs from its structure in crystal by a shift of the `hairpin' GH. FEBS Lett. 88, 114-117.
  206. Feis, A., Marzocchi, M.P., Paoli, M. and Smulevich, G. (1994) Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures. Biochemistry 33, 4577-4583.
  207. Fenwick, C.W. and English, A.M. (1996) Trapping and LC­MS identification of protein radicals formed in the horse heart metmyoglobin-H2O2 reaction. J. Am. Chem. Soc. 118, 12236-12237.
  208. Fermi, G. (1975) Three­dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5 Å resolution: refinement of the atomic model. J. Mol. Biol. 97, 237-256.
  209. Fermi, G. and Perutz, M.F. (1977) Structure of human fluoromethaemoglobin with inositol hexaphosphate. J. Mol. Biol. 114, 421-431.
  210. Fermi, G., Perutz, M.F., Dickinson, L.C. and Chien, J.C. (1982) Structure of human deoxy cobalt haemoglobin. J. Mol. Biol. 155, 495-505.
  211. Fermi, G., Perutz, M.F., Shaanan, B. and Fourme, R. (1984) The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175, 159-174.
  212. Fermi, G., Perutz, M.F. and Shulman, R.G. (1987) Iron distances in hemoglobin: comparison of x­ray crystallographic and extended x­ray absorption fine structure studies. Proc. Natl. Acad. Sci. USA 84, 6167-6168.
  213. Fermi, G., Perutz, M.F., Williamson, D., Stein, P. and Shih, D.T. (1992) Structure­function relationships in the low­affinity mutant haemoglobin Aalborg (Gly74 (E18)ß->Arg). J. Mol. Biol. 226, 883-888.
  214. Ferrone, F.A. (1994) Modulated excitation spectroscopy in hemoglobin. Methods Enzymol. 232, 292-321.
  215. Fitzgerald, P.M. and Love, W.E. (1979) Structure of deoxy hemoglobin C (ß6 Glu replaced by Lys) in two crystal forms. J. Mol. Biol. 132, 603-619.
  216. Franzen, S., Bohn, B., Poyart, C. and Martin, J.L. (1995a) Evidence for sub­picosecond heme doming in hemoglobin and myoglobin: A time­resolved resonance Raman comparison of carbonmonoxy and deoxy species. Biochemistry 34, 1224-1237.
  217. Franzen, S., Bohn, B., Poyart, C., DePillis, G., Boxer, S.G. and Martin, J.L. (1995b) Functional aspects of ultra­rapid heme doming in hemoglobin, myoglobin, and the myoglobin mutant H93G. J. Biol. Chem. 270, 1718-1720.
  218. Frauenfelder, H., Hartmann, H., Karplus, M., Kuntz, I.D., Jr., Kuriyan, J., Parak, F., Petsko, G.A., Ringe, D., Tilton, R.F., Jr., Connolly, M.L. and Max, N. (1987) Thermal expansion of a protein. Biochemistry 26, 254-261.
  219. Friedman, J.M. (1994) Time­resolved resonance Raman spectroscopy as probe for structure, dynamics, and reactivity in hemoglobin. Methods Enzymol. 232, 205-231.
  220. Frier, J.A. and Perutz, M.F. (1977) Structure of human foetal deoxyhaemoglobin. J. Mol. Biol. 112, 97-112.
  221. Fronticelli, C., Pechik, I., Brinigar, W.S., Kowalczyk, J. and Gilliland, G.L. (1994) Chloride ion independence of the Bohr effect in a mutant human hemoglobin ß (V1M+H2del). J. Biol. Chem. 269, 23965-23969.
  222. Fuchsman, W.H. and Appleby, C.A. (1979) CO and O2 complexes of soybean leghemoglobins: pH effects upon infrared and visible spectra. Comparisons with CO and O2 complexes of myoglobin and hemoglobin. Biochemistry 18, 1309-1321.
  223. Fung, L.W., Minton, A.P., Lindstrom, T.R., Pisciotta, A.V. and Ho, C. (1977) Proton nuclear magnetic resonance studies of hemoglobin M Milwaukee and their implications concerning the mechanism of cooperative oxygenation of hemoglobin. Biochemistry 16, 1452-1462.
  224. Gambacurta, A., Piro, M.C., Coletta, M., Clementi, M.E., Polizio, F., Desideri, A., Santucci, R. and Ascoli, F. (1995) A single mutation (Thr72->Ile) at the subunit interface is crucial for the functional properties of the homodimeric co­operative haemoglobin from Scapharca inaequivalvis. J. Mol. Biol. 248, 910-917.
  225. Gamcsik, M.P., Gerig, J.T. and Swenson, R.B. (1986) Fluorine­NMR studies of chimpanzee hemoglobin. Biochim. Biophys. Acta 874, 372-374.
  226. Gamcsik, M.P., Gerig, J.T. and Gregory, D.H. (1987) Fluorine nuclear magnetic resonance spectra of rabbit carbonmonoxyhemoglobin. Biochim. Biophys. Acta 912, 303-316.
  227. Genberg, L., Richard, L., McLendon, G. and Miller, R.J. (1991) Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales. Science 251, 1051-1054.
  228. Geraci, G. and Parkhurst, G. (1981) Circular dichroism spectra of hemoglobins. Methods Enzymol. 76, 262-275.
  229. Gerothanassis, I.P., Barrie, P.J., Momenteau, M. and Hawkes, G.E. (1994) Solid­state 13C NMR evidence for a large deviation from linearity of the Fe-C-O unit in the CO complex with myoglobin. J. Am. Chem. Soc. 116, 11944-11949.
  230. Gersonde, K., Kerr, E.A., Yu, N.T., Parish, D.W. and Smith, K.M. (1986) Resonance Raman investigation of CO­ligated monomeric insect hemoglobins. Direct evidence for reciprocal changes in iron-axial ligand bonds induced by allosteric transitions. J. Biol. Chem. 261, 8678-8685.
  231. Gersonde, K., Yu, N.T., Kerr, E.A., Smith, K.M. and Parish, D.W. (1987) Haem­rotational disorder in monomeric allosteric cyano­met insect haemoglobins monitored by resonance Raman spectroscopy. J. Mol. Biol. 194, 545-556.
  232. Gibson, Q.H., Bellelli, A., Regan, R., Sharma, P.K. and Vinogradov, S.N. (1992) Ligand binding by the chlorocruorin from Eudistylia vancouverii. J. Biol. Chem. 267, 11977-11981.
  233. Gilmanshin, R., Williams, S., Callender, R.H., Woodruff, W.H. and Dyer, R.B. (1997a) Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA 94, 3709-3713.
  234. Gilmanshin, R., Williams, S., Callender, R.H., Woodruff, W.H. and Dyer, R.B. (1997b) Fast events in protein folding: Relaxation dynamics and structure of the I form of apomyoglobin. Biochemistry 36, 15006-15012.
  235. Gilmanshin, R., Callender, R.H. and Dyer, R.B. (1998) The core of apomyoglobin E­form folds at the diffusion limit. Nature Struct. Biol. 5, 363-365.
  236. Giulivi, C. and Cadenas, E. (1993) The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects. FEBS Lett. 332, 287-290.
  237. Göran Eriksson, L.E. (1994) Binding of nitric oxide to intact human erythrocytes as monitored by electron paramagnetic resonance. Biochem. Biophys. Res. Commun. 203, 176-181.
  238. Goldbeck, R.A., Paquette, S.J., Björling, S.C. and Kliger, D.S. (1996) Allosteric intermediates in hemoglobin. 2. Kinetic modeling of HbCO photolysis. circular dichroism spectroscopy. Biochemistry 35, 8619-8627.
  239. Goto, Y. and Fink, A.L. (1994) Acid­induced folding of heme proteins. Methods Enzymol. 232, 3-15.
  240. Green, B.N., Kuchumov, A.R., Walz, D.A., Moens, L. and Vinogradov, S.N. (1998) A hierarchy of disulfide­bonded subunits: The quaternary structure of Eudistylia chlorocruorin. Biochemistry 37, 6598-6605.
  241. Green, D.W., Ingram, V.M. and Perutz, M.F. (1954) The structure of haemoglobin. IV. Sign determination by the isomorphous replacement method. Proc. R. Soc. Lond. A225, 287-307.
  242. Greer, J. and Perutz, M.F. (1971) Three dimensional structure of haemoglobin Rainier. Nature New Biol. 230, 261-264.
  243. Greer, J., Perutz, M.F. and Rumen, N. (1966) Lattice constants of lamprey haemoglobin. J. Mol. Biol. 18, 547-548.
  244. Gregoriou, V.G., Jayaraman, V., Hu, X. and Spiro, T.G. (1995) FT­IR difference spectroscopy of hemoglobins A and Kempsey: Evidence that a key quaternary interaction induces protonation of Aspß99. Biochemistry 34, 6876-6882.
  245. Gronenborn, A.M., Clore, G.M., Brunori, M., Giardina, B., Falcioni, G. and Perutz, M.F. (1984) Stereochemistry of ATP and GTP bound to fish haemoglobins. A transferred nuclear overhauser enhancement, 31P­nuclear magnetic resonance, oxygen equilibrium and molecular modelling study. J. Mol. Biol. 178, 731-742.
  246. Guarrera, L., Colotti, G., Boffi, A., Chiancone, E., Das, T.K., Rousseau, D.L. and Gibson, Q.H. (1998) The apolar distal histidine mutant (His69->Val) of the homodimeric Scapharca hemoglobin is in an R­like conformation. Biochemistry 37, 5608-5615.
  247. Gupta, R.K. (1976) Nuclear relaxation and gelation study of the interaction of organophosphates with human normal and sickle hemoglobins. In vitro gelation of sickle oxyhemoglobin in the presence of inositol hexaphosphate. J. Biol. Chem. 251, 6815-6822.
  248. Haouz, A., Glandieres, J.­M., Zentz, C., Pin, S., Ramstein, J., Tauc, P., Brochon, J.­C. and Alpert, B. (1998) Solvent effects on horse apomyoglobin dynamics. Biochemistry 37, 3013-3019.
  249. Hargrove, M.S., Barry, J.K., Brucker, E.A., Berry, M.B., Phillips, G.N., Olson, J.S., Arredondo­Peter, R., Dean, J.M., Klucas, R.V. and Sarath, G. (1997) Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants. J. Mol. Biol. 266, 1032-1042.
  250. Harrington, D.J., Adachi, K. and Royer, W.E., Jr. (1997) The high resolution crystal structure of deoxyhemoglobin S. J. Mol. Biol. 272, 398-407.
  251. Hartmann, H., Parak, F., Steigemann, W., Petsko, G.A., Ponzi, D.R. and Frauenfelder, H. (1982) Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K. Proc. Natl. Acad. Sci. USA 79, 4967-4971.
  252. Harutyunyan, E.H., Safonova, T.N., Kuranova, I.P., Popov, A.N., Teplyakov, A.V., Obmolova, G.V., Rusakov, A.A., Vainshtein, B.K., Dodson, G.G., Wilson, J.C. and Perutz, M.F. (1995) The structure of deoxy­ and oxy­leghaemoglobin from lupin. J. Mol. Biol. 251, 104-115.
  253. Harutyunyan, E.H., Safonova, T.N., Kuranova, I.P., Popov, A.N., Teplyakov, A.V., Obmolova, G.V.,Vainshtein, B.K., Dodson, G.G. and Wilson, J.C. (1996) The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins. J. Mol. Biol. 264, 152-161.
  254. Hashimoto, M., Ishimori, K., Imai, K., Miyazaki, G., Morimoto, H., Wada, Y. and Morishima, I. (1994) Site­directed mutagenesis in hemoglobin: functional and structural study of the intersubunit hydrogen bond of threonine­38(C3)alpha at the alpha1-ß2 interface in human hemoglobin. Biochemistry 32, 13688-13695.
  255. Hauksson, J.B., La Mar, G.N., Pande, U., Pandey, R.K., Parish, D.W., Singh, J.P. and Smith, K.M. (1990) 1H­NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type­isomers. Biochim. Biophys. Acta 1041, 186-194.
  256. Hayashi, T., Hitomi, Y. and Ogoshi, H. (1998) Artificial protein-protein complexation between a reconstituted myoglobin and cytochrome c. J. Am. Chem. Soc. 120, 4910-4915.
  257. Heidner, E.J., Ladner, R.C. and Perutz, M.F. (1976) Structure of horse carbonmonoxyhaemoglobin. J. Mol. Biol. 104, 707-722.
  258. Hendrickson, W.A., Love, W.E. and Murray, G.C. (1968) Crystal forms of lamprey hemoglobin and crystalline transitions between ligand states. J. Mol. Biol. 33, 829-842.
  259. Hendrickson, W.A., Love, W.E. and Karle, J. (1973) Crystal structure analysis of sea lamprey hemoglobin at 2 Å resolution. J. Mol. Biol. 74, 331-361.
  260. Hershberg, R.D. and Chance, B. (1975) Optical and magnetic resonance studies of formate binding to horse liver catalase and sperm whale myoglobin. Biochemistry 14, 3885-3891.
  261. Hewitt, J.A., Kilmartin, J.V., Eyck, L.F. and Perutz, M.F. (1972) Noncooperativity of the dimer in the reaction of hemoglobin with oxygen. Proc. Natl. Acad. Sci. USA 69, 203-207.
  262. Hildebrand, D.P., Burk, D.L., Maurus, R., Ferrer, J.C., Brayer, G.D. and Mauk, A.G. (1995a) The proximal ligand variant His93Tyr of horse heart myoglobin. Biochemistry 34, 1997-2005.
  263. Hildebrand, D.P., Ferrer, J.C., Tang, H.L., Smith, M. and Mauk, A.G. (1995b) Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin. Biochemistry 34, 11598-11605.
  264. Hille, R., Olson, J.S. and Palmer, G. (1979) Spectral transitions of nitrosyl hemes during ligand binding to hemoglobin. J. Biol. Chem. 254, 12110-12120.
  265. Hirota, S., Li, T., Phillips, G.N., Jr., Olson, J.S., Mukai, M. and Kitagawa, T. (1996) Perturbation of the Fe-O2 bond by nearby residues in heme pocket: Observation of vFe-O2 Raman bands for oxymyoglobin mutants. J. Am. Chem. Soc. 118, 7845-7846.
  266. Hirsch, R.E. (1994) Front­face fluorescence spectroscopy of hemoglobins. Methods Enzymol. 232, 231-246.
  267. Hirsch, R.E., Lin, M.J., Vidugiris, G.J.A., Huang, S., Friedman, J.M. and Nagel, R.L. (1996) Conformational changes in oxyhemoglobin C (Gluß6->Lys) detected by spectroscopic probing. J. Biol. Chem. 271, 372-375.
  268. Ho, C. and Russu, I.M. (1981) Proton nuclear magnetic resonance investigation of hemoglobins. Methods Enzymol. 76, 275-312.
  269. Ho, C. and Perussi, J.R. (1994) Proton nuclear magnetic resonance studies of hemoglobin. Methods Enzymol. 232, 97-139.
  270. Höök, F., Rodahl, M., Kasemo, B. and Brzezinski, P. (1998) Structural changes in hemoglobin during adsorption to solid surfaces: Effects of pH, ionic strength, and ligand binding. Proc. Natl. Acad. Sci. USA 95, 12271-12276.
  271. Hofrichter, J., Ansari, A., Jones, C.M., Deutsch, R.M., Sommer, J.H. and Henry, E.R. (1994) Ligand binding and conformational changes measured by time­resolved absorption spectroscopy. Methods Enzymol. 232, 387-415.
  272. Honzatko, R.B., Hendrickson, W.A. and Love, W.E. (1985) Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinus. J. Mol. Biol. 184, 147-164.
  273. Hori, H. and Yonetani, T. (1986) Nonequivalence in the electronic structure of the prosthetic groups between two alpha­subunits within deoxycobalthemoglobin as determined by single­crystal EPR spectroscopy. J. Biol. Chem. 261, 13693-13697.
  274. Hori, H., Ikeda­Saito, M. and Yonetani, T. (1981) Single crystal EPR of myoglobin nitroxide. Freezing­induced reversible changes in the molecular orientation of the ligand. J. Biol. Chem. 256, 7849-7855.
  275. Hori, H., Ikeda­Saito, M. and Yonetani, T. (1982) Ligand orientation of oxyproto­ and oxymesocobalt porphyrin­substituted myoglobin by single crystal EPR spectroscopy. J. Biol. Chem. 257, 3636-3642.
  276. Hori, H., Ikeda­Saito, M., Froncisz, W. and Yonetani, T. (1983) Analysis of powder and single crystal electron paramagnetic resonance spectra of deoxy myoglobins containing cobalt (II) proto­ and mesoporphyrins IX at various microwave frequencies. J. Biol. Chem. 258, 12368-12372.
  277. Hori, H., Fujii, M., Shiro, Y., Iizuka, T., Adachi, S. and Morishima, I. (1989) Single­crystal EPR study of novel azide complex of cyanogen bromide­modified myoglobin. Influence of specific modification of the heme distal histidyl residue on the ligand­binding structure. J. Biol. Chem. 264, 5715-5719.
  278. Hori, H., Tsubaki, M., Yu, N.T. and Yonetani, Y. (1991) Light absorption, electron paramagnetic resonance and resonance Raman characteristics of nitridochromium(V) protoporphyrin­IX and its reconstituted hemoproteins. Biochim. Biophys. Acta 1077, 392-399.
  279. Houston, T.E., Girling, R.L., Amma, E.L. and Huisman, T.H. (1978) Crystallography and oriented single crystal electron microscopy of hemoglobin deer II, a hemoglobin that exhibits matchstick­shaped erythrocytes. Biochim. Biophys. Acta 535, 413-417.
  280. Houston, T.E., Girling, R.L., Amma, E.L. and Huisman, T.H. (1979) Structure of human hemoglobin C: a disease with intraerythrocytic crystals. Biochim. Biophys. Acta 576, 497-501.
  281. Howells, E.R. and Perutz, M.F. (1954) The structure of haemoglobin. V. Imidazole­methaemoglobin: A further check of the signs. Proc. R. Soc. Lond. A225, 308-314.
  282. Hu, S., Smith, K.M. and Spiro, T.G. (1996) Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118, 12638-12646.
  283. Hu, X. and Spiro, T.G. (1997) Tyrosine and tryptophan structure markers in hemoglobin ultraviolet resonance Raman spectra: Mode assignments via subunit­specific isotope labeling of recombinant protein. Biochemistry 36, 15701-15712.
  284. Hu, X., Frei, H. and Spiro, T.G. (1996) Nanosecond step­scan FTIR spectroscopy of hemoglobin: Ligand recombination and protein conformational changes. Biochemistry 35, 13001-13005.
  285. Hu, X., Dick, L.A. and Spiro, T.G. (1998) Fourier transform infrared evidence against Aspß99 protonation in hemoglobin: Nature of the Tyralpha42-Aspß99 quaternary H­bond. Biochemistry 37, 9445-9448.
  286. Hu, X., Rodgers, K.R., Mukerji, I. and Spiro, T.G. (1998) New light on allostery: Dynamic resonance Raman spectroscopy of hemoglobin Kempsey. Biochemistry 38, 3462-3467.
  287. Huang, J., Leone, M., Boffi, A., Friedman, J.M. and Chiancone, E. (1996) Near­infrared spectra of Scapharca homodimeric hemoglobin: Characterization of the deoxy and photodissociated derivatives. Biophys. J. 70, 2924-2929.
  288. Huang, J., Juszczak, L.J., Peterson, E.S., Shannon, C.F., Yang, M., Huang, S., Vidugiris, G.V.A. and Friedman, J.M. (1999) The conformational and dynamic basis for ligand binding reactivity in hemoglobin Ypsilanti (ß99 Asp->Tyr): Origin of the quaternary enhancement effect. Biochemistry 38, 4514-4525.
  289. Huang, Y. and Ackers, G.K. (1996) Transformation of cooperative free energies between ligation systems of hemoglobin: Resolution of the carbon monoxide binding intermediates. Biochemistry 35, 704-718.
  290. Huang, Y., Pagnier, J., Magne, P., Baklouti, F., Kister, J., Delaunay, J., Poyart, C., Fermi, G. and Perutz, M.F. (1991) Structure and function of hemoglobin variants at an internal hydrophobic site: Consequences of mutations at the ß 27 (B9) position. Biochemistry 29, 7020-7023.
  291. Huang, Y., Yonetani, T., Tsuneshige, A., Hoffman, B.M. and Ackers, G.K. (1996a) Heterometallic hybrids of homometallic human hemoglobins. Proc. Natl. Acad. Sci. USA 93, 4425-4430.
  292. Huang, Y., Doyle, M.L. and Ackers, G.K. (1996b) The oxygen­binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc­containing hybrids. Biophys. J. 71, 2094-2105.
  293. Huang, Y., Koestner, M.L. and Ackers, G.K. (1996c) Heterotropic effects of chloride on the ligation microstates of hemoglobin at constant water activity. Biophys. J. 71, 2106-2116.
  294. Huang, Y., Koestner, M.L. and Ackers, G.K. (1997) Tertiary and quaternary chloride effects of the partially ligated (CN-met) hemoglobin intermediates. Biophys. Chem. 64, 157-173.
  295. Hubbard, S.R., Hendrickson, W.A., Lambright, D.G. and Boxer, S.G. (1990) X­ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution. J. Mol. Biol. 213, 215-218.
  296. Hughson, F.M., Wright, P.E. and Baldwin, R.L. (1990) Structural characterization of a partly folded apomyoglobin intermediate. Science 249, 1544-1548.
  297. Hui, H.L., Kavanaugh, J.S., Doyle, M.L., Wierzba, A., Rogers, P.H., Arnone, A., Holt, J.M., Ackers, G.K. and Noble, R.W. (1999) Structural and functional properties of human hemoglobins reassembled after synthesis in Escherichia coli. Biochemistry 38, 1040-1049. Crystallography
  298. Hunter, C.L., Lloyd, E., Eltis, L.D., Rafferty, S.P., Lee, H., Smith, M. and Mauk, A.G. (1997) Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5. Biochemistry 36, 1010-1017.
  299. Hurrell, J.G., Nicola, N.A., Broughton, W.J., Dilworth, M.J., Minasian, E. and Leach, S.J. (1976) Comparative structural and immunochemical properties of leghaemoglobins. Eur. J. Biochem. 66, 389-399.
Bibliography on structural studies of globins: I-P and Q-Z
Reviews on globins