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Volumn 360, Issue 3, 2006, Pages 690-701

1.25 Å Resolution Crystal Structures of Human Haemoglobin in the Oxy, Deoxy and Carbonmonoxy Forms

Author keywords

conflict; function; NMR; nuclear magnetic resonance; X ray crystallography

Indexed keywords

ALPHA GLOBIN; BETA GLOBIN; CARBOXYHEMOGLOBIN; DEOXYHEMOGLOBIN; GLYCINE; HEMOGLOBIN; HISTIDINE; LIGAND; OXYGEN; OXYHEMOGLOBIN; IRON;

EID: 33745571654     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.05.036     Document Type: Article
Times cited : (264)

References (70)
  • 1
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature 228 (1970) 726-739
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 2
    • 0015529611 scopus 로고
    • Nature of haem-haem interaction
    • Perutz M.F. Nature of haem-haem interaction. Nature 237 (1972) 495-499
    • (1972) Nature , vol.237 , pp. 495-499
    • Perutz, M.F.1
  • 3
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and Changeux J.-P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12 (1965) 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 4
    • 0022634647 scopus 로고
    • Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding
    • Perutz M.F., Fermi G., Abraham D.J., Poyart C., and Bursaux E. Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding. J. Am. Chem. Soc. 108 (1986) 1064-1078
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1064-1078
    • Perutz, M.F.1    Fermi, G.2    Abraham, D.J.3    Poyart, C.4    Bursaux, E.5
  • 5
    • 0015515865 scopus 로고
    • X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin
    • Arnone A. X-ray diffraction study of binding of 2,3-diphosphoglycerate to human deoxyhaemoglobin. Nature 237 (1972) 146-149
    • (1972) Nature , vol.237 , pp. 146-149
    • Arnone, A.1
  • 6
    • 0025343392 scopus 로고
    • Effectors of hemoglobin. Separation of allosteric and affinity factors
    • Marden M.C., Bohn B., Kister J., and Poyart C. Effectors of hemoglobin. Separation of allosteric and affinity factors. Biophys. J. 57 (1990) 397-403
    • (1990) Biophys. J. , vol.57 , pp. 397-403
    • Marden, M.C.1    Bohn, B.2    Kister, J.3    Poyart, C.4
  • 7
    • 0037054844 scopus 로고    scopus 로고
    • Heterotropic effectors control the hemoglobin function by interacting with its T and R states-A new view on the principle of allostery
    • Tsuneshige A., Park S., and Yonetani T. Heterotropic effectors control the hemoglobin function by interacting with its T and R states-A new view on the principle of allostery. Biophys. Chem. 98 (2002) 49-63
    • (2002) Biophys. Chem. , vol.98 , pp. 49-63
    • Tsuneshige, A.1    Park, S.2    Yonetani, T.3
  • 8
    • 0037064138 scopus 로고    scopus 로고
    • Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-Å resolution. A novel allosteric binding site in R-state hemoglobin
    • Shibayama N., Miura S., Tame J.R.H., Yonetani T., and Park S.Y. Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-Å resolution. A novel allosteric binding site in R-state hemoglobin. J. Biol. Chem. 277 (2002) 38791-38796
    • (2002) J. Biol. Chem. , vol.277 , pp. 38791-38796
    • Shibayama, N.1    Miura, S.2    Tame, J.R.H.3    Yonetani, T.4    Park, S.Y.5
  • 9
    • 31344438645 scopus 로고    scopus 로고
    • R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35
    • Yokoyama T., Neya S., Tsuneshige A., Yonetani T., Park S.Y., and Tame J.R.H. R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35. J. Mol. Biol. 356 (2006) 790-801
    • (2006) J. Mol. Biol. , vol.356 , pp. 790-801
    • Yokoyama, T.1    Neya, S.2    Tsuneshige, A.3    Yonetani, T.4    Park, S.Y.5    Tame, J.R.H.6
  • 10
    • 0011689871 scopus 로고
    • Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli
    • Nagai K., Perutz M.F., and Poyart C. Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli. Proc. Natl Acad. Sci. USA 82 (1985) 7252-7255
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7252-7255
    • Nagai, K.1    Perutz, M.F.2    Poyart, C.3
  • 11
    • 0023640484 scopus 로고
    • Distal residues in the oxygen binding site of haemoglobin studied by protein engineering
    • Nagai K., Luisi B., Shih D., Miyazaki G., Imai K., Poyart C., et al. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nature 329 (1987) 858-860
    • (1987) Nature , vol.329 , pp. 858-860
    • Nagai, K.1    Luisi, B.2    Shih, D.3    Miyazaki, G.4    Imai, K.5    Poyart, C.6
  • 13
    • 0025760849 scopus 로고
    • Functional role of the distal valine (E11) residue of alpha subunits in human haemoglobin
    • Tame J., Shih D.T., Pagnier J., Fermi G., and Nagai K. Functional role of the distal valine (E11) residue of alpha subunits in human haemoglobin. J. Mol. Biol. 218 (1991) 761-767
    • (1991) J. Mol. Biol. , vol.218 , pp. 761-767
    • Tame, J.1    Shih, D.T.2    Pagnier, J.3    Fermi, G.4    Nagai, K.5
  • 14
    • 0024468312 scopus 로고
    • The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin
    • Mathews A.J., Rohlfs R.J., Olson J.S., Tame J., Renaud J.P., and Nagai K. The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin. J. Biol. Chem. 264 (1989) 16573-16583
    • (1989) J. Biol. Chem. , vol.264 , pp. 16573-16583
    • Mathews, A.J.1    Rohlfs, R.J.2    Olson, J.S.3    Tame, J.4    Renaud, J.P.5    Nagai, K.6
  • 15
    • 0021027685 scopus 로고
    • Structure of human oxyhaemoglobin at 2.1 Å resolution
    • Shaanan B. Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171 (1983) 31-59
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 16
    • 0034641754 scopus 로고    scopus 로고
    • NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin
    • Lukin J.A., Simplaceanu V., Zou M., Ho N.T., and Ho C. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin. Proc. Natl Acad. Sci. USA 97 (2000) 10354-10358
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10354-10358
    • Lukin, J.A.1    Simplaceanu, V.2    Zou, M.3    Ho, N.T.4    Ho, C.5
  • 17
    • 0018838712 scopus 로고
    • The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution
    • Baldwin J.M. The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution. J. Mol. Biol. 136 (1980) 103-128
    • (1980) J. Mol. Biol. , vol.136 , pp. 103-128
    • Baldwin, J.M.1
  • 19
    • 0023042853 scopus 로고
    • X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution
    • Kuriyan J., Wilz S., Karplus M., and Petsko G.A. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution. J. Mol. Biol. 192 (1986) 133-154
    • (1986) J. Mol. Biol. , vol.192 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 20
    • 0032078092 scopus 로고    scopus 로고
    • Human carboxyhemoglobin at 2.2 A resolution: structure and solvent comparisons of R-state, R2-state and T-state hemoglobins
    • Vasquez G.B., Ji X., Fronticelli C., and Gilliland G.L. Human carboxyhemoglobin at 2.2 A resolution: structure and solvent comparisons of R-state, R2-state and T-state hemoglobins. Acta Crystallog. sect. D 54 (1998) 355-366
    • (1998) Acta Crystallog. sect. D , vol.54 , pp. 355-366
    • Vasquez, G.B.1    Ji, X.2    Fronticelli, C.3    Gilliland, G.L.4
  • 21
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
    • Fermi G., Perutz M.F., Shaanan B., and Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175 (1984) 159-174
    • (1984) J. Mol. Biol. , vol.175 , pp. 159-174
    • Fermi, G.1    Perutz, M.F.2    Shaanan, B.3    Fourme, R.4
  • 22
    • 0033923460 scopus 로고    scopus 로고
    • The structures of deoxy human haemoglobin and the mutant Hb Tyr α42His at 120 K
    • Tame J.R.H., and Vallone B. The structures of deoxy human haemoglobin and the mutant Hb Tyr α42His at 120 K. Acta Crystallog. sect. D 56 (2000) 805-811
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 805-811
    • Tame, J.R.H.1    Vallone, B.2
  • 23
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sweet R.M., and Carter Jr. C.W. (Eds), Academic Press, Orlando
    • Sheldrick G.M., and Schneider T.R. SHELXL: High-resolution refinement. In: Sweet R.M., and Carter Jr. C.W. (Eds). Metods in Enzymololgy vol. 277 (1997), Academic Press, Orlando 319-343
    • (1997) Metods in Enzymololgy , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 24
    • 0027988868 scopus 로고
    • The T-to-R transformation in hemoglobin: a reevaluation
    • Srinivasan R., and Rose G.D. The T-to-R transformation in hemoglobin: a reevaluation. Proc. Natl Acad. Sci. USA 91 (1994) 11113-11117
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11113-11117
    • Srinivasan, R.1    Rose, G.D.2
  • 25
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • Schneider T.R. A genetic algorithm for the identification of conformationally invariant regions in protein molecules. Acta Crystallog. sect. D 58 (2002) 195-208
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 195-208
    • Schneider, T.R.1
  • 26
    • 0018361151 scopus 로고
    • Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism
    • Baldwin J., and Chothia C. Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129 (1979) 175-220
    • (1979) J. Mol. Biol. , vol.129 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 27
    • 3142618499 scopus 로고    scopus 로고
    • Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the Root effect
    • Yokoyama T., Chong K.T., Miyazaki G., Morimoto H., Shih D.T., Unzai S., et al. Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the Root effect. J. Biol. Chem. 279 (2004) 28632-28640
    • (2004) J. Biol. Chem. , vol.279 , pp. 28632-28640
    • Yokoyama, T.1    Chong, K.T.2    Miyazaki, G.3    Morimoto, H.4    Shih, D.T.5    Unzai, S.6
  • 28
    • 0016371412 scopus 로고
    • Studies on cobalt myoglobins and hemoglobins III. Electron paramagnetic resonance studies of reversible oxygenation of cobalt myoglobins and hemoglobins
    • Yonetani T., Yamamoto H., and Iizuka T. Studies on cobalt myoglobins and hemoglobins III. Electron paramagnetic resonance studies of reversible oxygenation of cobalt myoglobins and hemoglobins. J. Biol. Chem. 249 (1974) 2168-2174
    • (1974) J. Biol. Chem. , vol.249 , pp. 2168-2174
    • Yonetani, T.1    Yamamoto, H.2    Iizuka, T.3
  • 29
    • 0033574735 scopus 로고    scopus 로고
    • A steric mechanism for inhibition of CO binding to heme proteins
    • Kachalova G.S., Popov A.N., and Bartunik H.D. A steric mechanism for inhibition of CO binding to heme proteins. Science 284 (1999) 473-476
    • (1999) Science , vol.284 , pp. 473-476
    • Kachalova, G.S.1    Popov, A.N.2    Bartunik, H.D.3
  • 30
    • 0037173553 scopus 로고    scopus 로고
    • Theoretical study of the discrimination between O(2) and CO by myoglobin
    • Sigfridsson E., and Ryde U. Theoretical study of the discrimination between O(2) and CO by myoglobin. J. Inorg. Biochem. 91 (2002) 101-115
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 101-115
    • Sigfridsson, E.1    Ryde, U.2
  • 31
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • Vojtechovsky J., Chu K., Berendzen J., Sweet R.M., and Schlichting I. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77 (1999) 2153-2174
    • (1999) Biophys. J. , vol.77 , pp. 2153-2174
    • Vojtechovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet, R.M.4    Schlichting, I.5
  • 32
    • 0001793063 scopus 로고
    • Preparation of haemoglobin crystals
    • Perutz M.F. Preparation of haemoglobin crystals. J. Cryst. Growth 2 (1968) 54-56
    • (1968) J. Cryst. Growth , vol.2 , pp. 54-56
    • Perutz, M.F.1
  • 33
    • 0035943379 scopus 로고    scopus 로고
    • Reversible lattice packing illustrates the temperature dependence of macromolecular interactions
    • Juers D.H., and Matthews B.W. Reversible lattice packing illustrates the temperature dependence of macromolecular interactions. J. Mol. Biol. 311 (2001) 851-862
    • (2001) J. Mol. Biol. , vol.311 , pp. 851-862
    • Juers, D.H.1    Matthews, B.W.2
  • 34
    • 20944434880 scopus 로고    scopus 로고
    • Cryo-cooling in macromolecular crystallography: advantages, disadvantages and optimization
    • Juers D.H., and Matthews B.W. Cryo-cooling in macromolecular crystallography: advantages, disadvantages and optimization. Quart. Rev. Biophys. 37 (2004) 105-119
    • (2004) Quart. Rev. Biophys. , vol.37 , pp. 105-119
    • Juers, D.H.1    Matthews, B.W.2
  • 36
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin R.B. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl Acad. Sci. USA 83 (1986) 8069-8072
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.B.1
  • 37
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar S., Tsai C.-J., and Nussinov R. Factors enhancing protein thermostability. Protein Eng. 13 (2000) 179-191
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 38
    • 0016824616 scopus 로고
    • Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions
    • Ward K.B., Wishner B.C., Lattman E.E., and Love W.E. Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions. J. Mol. Biol. 98 (1975) 161-177
    • (1975) J. Mol. Biol. , vol.98 , pp. 161-177
    • Ward, K.B.1    Wishner, B.C.2    Lattman, E.E.3    Love, W.E.4
  • 39
    • 0030000410 scopus 로고    scopus 로고
    • Crystal structure of T state haemoglobin with oxygen bound at all four haems
    • Paoli M., Liddington R., Tame J., Wilkinson A., and Dodson G. Crystal structure of T state haemoglobin with oxygen bound at all four haems. J. Mol. Biol. 256 (1996) 775-792
    • (1996) J. Mol. Biol. , vol.256 , pp. 775-792
    • Paoli, M.1    Liddington, R.2    Tame, J.3    Wilkinson, A.4    Dodson, G.5
  • 40
    • 0031571593 scopus 로고    scopus 로고
    • Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state
    • Paoli M., Dodson G., Liddington R.C., and Wilkinson A.J. Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state. J. Mol. Biol. 271 (1997) 161-167
    • (1997) J. Mol. Biol. , vol.271 , pp. 161-167
    • Paoli, M.1    Dodson, G.2    Liddington, R.C.3    Wilkinson, A.J.4
  • 41
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin A at 1.7-Å resolution
    • Silva M.M., Rogers P.H., and Arnone A. A third quaternary structure of human hemoglobin A at 1.7-Å resolution. J. Biol. Chem. 267 (1992) 17248-172456
    • (1992) J. Biol. Chem. , vol.267 , pp. 17248-172456
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 42
    • 0034687668 scopus 로고    scopus 로고
    • Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin
    • Mueser T.C., Rogers P.H., and Arnone A. Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin. Biochemistry 39 (2000) 15353-15364
    • (2000) Biochemistry , vol.39 , pp. 15353-15364
    • Mueser, T.C.1    Rogers, P.H.2    Arnone, A.3
  • 43
    • 0141792364 scopus 로고    scopus 로고
    • Allosteric changes in protein structure computed by a simple mechanical model: hemoglobin T↔R2 transition
    • Xu C., Tobi D., and Bahar I. Allosteric changes in protein structure computed by a simple mechanical model: hemoglobin T↔R2 transition. J. Mol. Biol. 333 (2003) 153-168
    • (2003) J. Mol. Biol. , vol.333 , pp. 153-168
    • Xu, C.1    Tobi, D.2    Bahar, I.3
  • 46
    • 1842483305 scopus 로고    scopus 로고
    • The structure-function relationship of hemoglobin in solution at atomic resolution
    • Lukin J.A., and Ho C. The structure-function relationship of hemoglobin in solution at atomic resolution. Chem. Rev. 104 (2004) 1219-1230
    • (2004) Chem. Rev. , vol.104 , pp. 1219-1230
    • Lukin, J.A.1    Ho, C.2
  • 47
    • 0033214516 scopus 로고    scopus 로고
    • What is the true structure of liganded haemoglobin?
    • Tame J.R.H. What is the true structure of liganded haemoglobin?. Trends Biochem. Sci. 24 (1999) 372-377
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 372-377
    • Tame, J.R.H.1
  • 48
    • 0037110570 scopus 로고    scopus 로고
    • Allosteric effects of chloride ions at the intradimeric alpha1beta1 and alpha2beta2 interfaces of human hemoglobin
    • Rujan I.N., and Russu I.M. Allosteric effects of chloride ions at the intradimeric alpha1beta1 and alpha2beta2 interfaces of human hemoglobin. Proteins; Struct. Funct. Genet. 49 (2002) 413-419
    • (2002) Proteins; Struct. Funct. Genet. , vol.49 , pp. 413-419
    • Rujan, I.N.1    Russu, I.M.2
  • 49
    • 17644375152 scopus 로고    scopus 로고
    • Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions
    • Kavanaugh J.S., Rogers P.H., and Arnone A. Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions. Biochemistry 44 (2005) 6101-6121
    • (2005) Biochemistry , vol.44 , pp. 6101-6121
    • Kavanaugh, J.S.1    Rogers, P.H.2    Arnone, A.3
  • 50
    • 0038503269 scopus 로고    scopus 로고
    • Functional and spectroscopic characterization of half-liganded iron-zinc hybrid hemoglobin: evidence for conformational plasticity within the T state
    • Samuni U., Juszczak L., Dantsker D., Khan I., Friedman A.J., Perez-Gonzalez-de-Apodaca J., et al. Functional and spectroscopic characterization of half-liganded iron-zinc hybrid hemoglobin: evidence for conformational plasticity within the T state. Biochemistry 42 (2003) 8272-8288
    • (2003) Biochemistry , vol.42 , pp. 8272-8288
    • Samuni, U.1    Juszczak, L.2    Dantsker, D.3    Khan, I.4    Friedman, A.J.5    Perez-Gonzalez-de-Apodaca, J.6
  • 51
    • 0025299882 scopus 로고
    • Structure of deoxy-quaternary haemoglobin with liganded beta subunits
    • Luisi B., Liddington B., Fermi G., and Shibayama N. Structure of deoxy-quaternary haemoglobin with liganded beta subunits. J. Mol. Biol. 214 (1990) 7-14
    • (1990) J. Mol. Biol. , vol.214 , pp. 7-14
    • Luisi, B.1    Liddington, B.2    Fermi, G.3    Shibayama, N.4
  • 52
    • 0024319829 scopus 로고
    • Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems
    • Luisi B., and Shibayama N. Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems. J. Mol. Biol. 206 (1989) 723-736
    • (1989) J. Mol. Biol. , vol.206 , pp. 723-736
    • Luisi, B.1    Shibayama, N.2
  • 53
    • 0019876902 scopus 로고
    • Multiple T state conformations in a fish hemoglobin. Carbon monoxide binding to hemoglobin of Thunnus thynnus
    • Morris R.J., Neckameyer W.S., and Gibson Q.H. Multiple T state conformations in a fish hemoglobin. Carbon monoxide binding to hemoglobin of Thunnus thynnus. J. Biol. Chem. 256 (1981) 4598-4603
    • (1981) J. Biol. Chem. , vol.256 , pp. 4598-4603
    • Morris, R.J.1    Neckameyer, W.S.2    Gibson, Q.H.3
  • 54
    • 0033536620 scopus 로고    scopus 로고
    • Magnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme
    • Miyazaki G., Morimoto H., Yun K.M., Park S.Y., Nakagawa A., Minagawa H., and Shibayama N. Magnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme. J. Mol. Biol. 292 (1999) 1121-1136
    • (1999) J. Mol. Biol. , vol.292 , pp. 1121-1136
    • Miyazaki, G.1    Morimoto, H.2    Yun, K.M.3    Park, S.Y.4    Nakagawa, A.5    Minagawa, H.6    Shibayama, N.7
  • 55
    • 3042775268 scopus 로고    scopus 로고
    • Crystal structures of unliganded and half-liganded human hemoglobin derivatives cross-linked between Lys 82beta1 and Lys 82beta2
    • Park S.Y., Shibayama N., Hiraki T., and Tame J.R.H. Crystal structures of unliganded and half-liganded human hemoglobin derivatives cross-linked between Lys 82beta1 and Lys 82beta2. Biochemistry 43 (2004) 8711-8717
    • (2004) Biochemistry , vol.43 , pp. 8711-8717
    • Park, S.Y.1    Shibayama, N.2    Hiraki, T.3    Tame, J.R.H.4
  • 56
    • 0026619765 scopus 로고
    • Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates
    • Ho C. Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates. Adv. Protein Chem. 43 (1992) 153-312
    • (1992) Adv. Protein Chem. , vol.43 , pp. 153-312
    • Ho, C.1
  • 57
    • 33645978391 scopus 로고    scopus 로고
    • Quaternary structure of carbonmonoxyhemoglobins in solution: structural changes induced by the allosteric effector inositol hexaphosphate
    • Gong Q., Simplaceanu V., Lukin J.A., Giovannelli J.L., Ho N.T., and Ho C. Quaternary structure of carbonmonoxyhemoglobins in solution: structural changes induced by the allosteric effector inositol hexaphosphate. Biochemistry 45 (2006) 5140-5148
    • (2006) Biochemistry , vol.45 , pp. 5140-5148
    • Gong, Q.1    Simplaceanu, V.2    Lukin, J.A.3    Giovannelli, J.L.4    Ho, N.T.5    Ho, C.6
  • 58
    • 0037072945 scopus 로고    scopus 로고
    • Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors
    • Yonetani T., Park S.I., Tsuneshige A., Imai K., and Kanaori K. Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors. J. Biol. Chem. 277 (2002) 34508-34520
    • (2002) J. Biol. Chem. , vol.277 , pp. 34508-34520
    • Yonetani, T.1    Park, S.I.2    Tsuneshige, A.3    Imai, K.4    Kanaori, K.5
  • 59
    • 0036899359 scopus 로고    scopus 로고
    • Structure of human carbonmonoxyhemoglobin at 2.16 Å: a snapshot of the allosteric transition
    • Safo M.K., Burnett J.C., Musayev F.N., Nokuri S., and Abraham D.J. Structure of human carbonmonoxyhemoglobin at 2.16 Å: a snapshot of the allosteric transition. Acta Crystallog. sect. D 58 (2002) 2031-2037
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 2031-2037
    • Safo, M.K.1    Burnett, J.C.2    Musayev, F.N.3    Nokuri, S.4    Abraham, D.J.5
  • 60
    • 0030582681 scopus 로고    scopus 로고
    • The crystal structure of horse deoxyhaemoglobin trapped in the high-affinity (R) state
    • Wilson J., Phillips K., and Luisi B. The crystal structure of horse deoxyhaemoglobin trapped in the high-affinity (R) state. J. Mol. Biol. 264 (1996) 743-756
    • (1996) J. Mol. Biol. , vol.264 , pp. 743-756
    • Wilson, J.1    Phillips, K.2    Luisi, B.3
  • 61
    • 0029062547 scopus 로고
    • Allosteric transition intermediates modelled by crosslinked haemoglobins
    • Schumacher M.A., Dixon M.M., Kluger R., Jones R.T., and Brennan R.G. Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature 375 (1995) 84-87
    • (1995) Nature , vol.375 , pp. 84-87
    • Schumacher, M.A.1    Dixon, M.M.2    Kluger, R.3    Jones, R.T.4    Brennan, R.G.5
  • 62
    • 20444417111 scopus 로고    scopus 로고
    • The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin
    • Safo M.K., and Abraham D.J. The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin. Biochemistry 44 (2005) 8347-8359
    • (2005) Biochemistry , vol.44 , pp. 8347-8359
    • Safo, M.K.1    Abraham, D.J.2
  • 64
    • 0141717848 scopus 로고    scopus 로고
    • The global allostery model of hemoglobin: an allosteric mechanism involving homotropic and heterotropic interactions
    • Yonetani T., and Tsuneshige A. The global allostery model of hemoglobin: an allosteric mechanism involving homotropic and heterotropic interactions. C.R. Biol. 326 (2003) 523-532
    • (2003) C.R. Biol. , vol.326 , pp. 523-532
    • Yonetani, T.1    Tsuneshige, A.2
  • 66
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 67
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276 (1997) 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 70
    • 13244281317 scopus 로고    scopus 로고
    • COOT: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. COOT: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


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