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Volumn 9, Issue 4, 2000, Pages 683-692

Oxygen binding by α(Fe2+)2β(Ni2+)2 hemoglobin crystals

Author keywords

Allosteric models; Hemoglobin crystals; Microspectrophotometry; Oxygen binding; X ray crystallography

Indexed keywords

FERROUS ION; HEMOGLOBIN; HEMOGLOBIN ALPHA CHAIN; HEMOGLOBIN BETA CHAIN; NICKEL; OXYGEN;

EID: 17944384230     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.4.683     Document Type: Article
Times cited : (16)

References (49)
  • 1
    • 0026671889 scopus 로고
    • X-ray diffraction study of di-ligated and tetra-ligated T-state hemoglobin from high salt crystals
    • Abraham DJ, Peascoe RA, Randad RS, Panikker J. 1992. X-ray diffraction study of di-ligated and tetra-ligated T-state hemoglobin from high salt crystals. J Mol Biol 227:480-492.
    • (1992) J Mol Biol , vol.227 , pp. 480-492
    • Abraham, D.J.1    Peascoe, R.A.2    Randad, R.S.3    Panikker, J.4
  • 2
    • 0031800335 scopus 로고    scopus 로고
    • Deciphering the molecular code of hemoglobin allostery
    • Ackers GK. 1998. Deciphering the molecular code of hemoglobin allostery. Adv Prot Chem 51:185-253.
    • (1998) Adv Prot Chem , vol.51 , pp. 185-253
    • Ackers, G.K.1
  • 5
    • 0018215404 scopus 로고
    • Sequence of oxygen binding by hemoglobin
    • Asakura T, Lau PW. 1978. Sequence of oxygen binding by hemoglobin. Proc Natl Acad Sci USA 75:5462-5465.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5462-5465
    • Asakura, T.1    Lau, P.W.2
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite - Programs for protein crystallography
    • Bailey S. 1994. The CCP4 suite - Programs for protein crystallography. Acta Crystallogr Sect D 50:760-763.
    • (1994) Acta Crystallogr Sect D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 8
    • 0031463937 scopus 로고    scopus 로고
    • T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride
    • Bettati S, Mozzarelli A. 1997. T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride. J Biol Chem 272:32050-32055.
    • (1997) J Biol Chem , vol.272 , pp. 32050-32055
    • Bettati, S.1    Mozzarelli, A.2
  • 9
    • 0032575762 scopus 로고    scopus 로고
    • Allosteric mechanism of haemoglobin: Rupture of salt-bridges raises the oxygen affinity of the T structure
    • Bettati S, Mozzarelli A, Perutz MF. 1998. Allosteric mechanism of haemoglobin: Rupture of salt-bridges raises the oxygen affinity of the T structure. J Mol Biol 281:581-585.
    • (1998) J Mol Biol , vol.281 , pp. 581-585
    • Bettati, S.1    Mozzarelli, A.2    Perutz, M.F.3
  • 10
    • 0029798672 scopus 로고    scopus 로고
    • Oxygen binding by single crystals of hemoglobin: The problem of cooperativity and inequivalence of alpha and beta subunits
    • Bettati S, Mozzarelli A, Rivetti C, Rossi GL, Tsuneshige A, Yonetani T, Eaton WA, Henry ER. 1996. Oxygen binding by single crystals of hemoglobin: The problem of cooperativity and inequivalence of alpha and beta subunits. Proteins 25:425-437.
    • (1996) Proteins , vol.25 , pp. 425-437
    • Bettati, S.1    Mozzarelli, A.2    Rivetti, C.3    Rossi, G.L.4    Tsuneshige, A.5    Yonetani, T.6    Eaton, W.A.7    Henry, E.R.8
  • 12
    • 0015117916 scopus 로고
    • A controlled-environment culture system for high resolution light microscopy
    • Dvorak JA, Stotler WF. 1971. A controlled-environment culture system for high resolution light microscopy. Exp Cell Res 68:144-148.
    • (1971) Exp Cell Res , vol.68 , pp. 144-148
    • Dvorak, J.A.1    Stotler, W.F.2
  • 14
    • 84941485112 scopus 로고
    • Das gleichgewicht zwischen hämoglobin und sauerstoff
    • Haurowitz F. 1938. Das Gleichgewicht zwischen Hämoglobin und Sauerstoff, Hoppe-Seyler Z Physiol Chem 254:266-274.
    • (1938) Hoppe-Seyler Z Physiol Chem , vol.254 , pp. 266-274
    • Haurowitz, F.1
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr Sect A 47:110-119.
    • (1991) Acta Crystallogr Sect A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical methods in proteins containing subunits
    • Koshland DE, Nemethy G, Filmer D. 1966. Comparison of experimental binding data and theoretical methods in proteins containing subunits. Biochemistry 5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 19
    • 0023850148 scopus 로고
    • Analysis of proton release in oxygen binding by hemoglobin: Implications for the cooperative mechanism
    • Lee A, Karplus M, Poyart C, Bursaux E. 1988. Analysis of proton release in oxygen binding by hemoglobin: Implications for the cooperative mechanism. Biochemistry 27:1285-1301.
    • (1988) Biochemistry , vol.27 , pp. 1285-1301
    • Lee, A.1    Karplus, M.2    Poyart, C.3    Bursaux, E.4
  • 20
    • 0023876537 scopus 로고
    • Structure of the liganded T state of haemoglobin identifies the origin of cooperative oxygen binding
    • Liddington R, Derewenda Z, Dodson G, Harris D. 1988. Structure of the liganded T state of haemoglobin identifies the origin of cooperative oxygen binding. Nature 331:725-728.
    • (1988) Nature , vol.331 , pp. 725-728
    • Liddington, R.1    Derewenda, Z.2    Dodson, G.3    Harris, D.4
  • 21
    • 0026620795 scopus 로고
    • High-resolution crystal-structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(α-oxy)haemoglobin and T(met)haemoglobin
    • Liddington R, Derewenda Z, Dodson E, Hubbard R, Dodson G. 1992. High-resolution crystal-structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(α-oxy)haemoglobin and T(met)haemoglobin. J Mol Biol 228:551-579.
    • (1992) J Mol Biol , vol.228 , pp. 551-579
    • Liddington, R.1    Derewenda, Z.2    Dodson, E.3    Hubbard, R.4    Dodson, G.5
  • 22
    • 0015370270 scopus 로고
    • Functional nonequivalence of α and β hemes in human hemoglobin
    • Lindstrom TR, Ho C. 1972. Functional nonequivalence of α and β hemes in human hemoglobin. Proc Natl Acad Sci USA 69:1707-1710.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 1707-1710
    • Lindstrom, T.R.1    Ho, C.2
  • 23
    • 0025299882 scopus 로고
    • Structure of deoxy-quaternary hemoglobin with liganded β subunits
    • Luisi B, Liddington B, Fermi G, Shibayama N. 1990. Structure of deoxy-quaternary hemoglobin with liganded β subunits. J Mol Biol 214:7-14.
    • (1990) J Mol Biol , vol.214 , pp. 7-14
    • Luisi, B.1    Liddington, B.2    Fermi, G.3    Shibayama, N.4
  • 24
    • 0024319829 scopus 로고
    • Structure of hemoglobin in the deoxy quaternary state with ligand bound at the α haems
    • Luisi B, Shibayama N. 1989. Structure of hemoglobin in the deoxy quaternary state with ligand bound at the α haems. J Mol Biol 206:723-736.
    • (1989) J Mol Biol , vol.206 , pp. 723-736
    • Luisi, B.1    Shibayama, N.2
  • 25
    • 0025343392 scopus 로고
    • Effectors of hemoglobin: Separation of allosteric and affinity factors
    • Marden MC, Bohn B, Kister J, Poyart C. 1990. Effectors of hemoglobin: Separation of allosteric and affinity factors. Biophys J 57:397-403.
    • (1990) Biophys J , vol.57 , pp. 397-403
    • Marden, M.C.1    Bohn, B.2    Kister, J.3    Poyart, C.4
  • 26
    • 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, Shibayama N. 1999. 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 292:1121-1136.
    • (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
  • 27
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux J-P. 1965. On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 28
    • 0002802966 scopus 로고    scopus 로고
    • Functional properties of immobilized proteins
    • Tokyo: Gordon and Breach Science Publishers. Forthcoming
    • Mozzarelli A, Bettati S. 2000. Functional properties of immobilized proteins. In: Advanced functional molecules and polymers. Tokyo: Gordon and Breach Science Publishers. Forthcoming.
    • (2000) Advanced Functional Molecules and Polymers
    • Mozzarelli, A.1    Bettati, S.2
  • 30
    • 0031048477 scopus 로고    scopus 로고
    • Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals
    • Mozzarelli A, Rivetti C, Rossi GL, Eaton WA, Henry ER. 1997. Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals. Protein Sci 6:484-489.
    • (1997) Protein Sci , vol.6 , pp. 484-489
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Eaton, W.A.4    Henry, E.R.5
  • 31
    • 0025801633 scopus 로고
    • Crystals of hemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect
    • Mozzarelli A, Rivetti C, Rossi GL, Henry ER, Eaton WA. 1991. Crystals of hemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature 351:416-419.
    • (1991) Nature , vol.351 , pp. 416-419
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Henry, E.R.4    Eaton, W.A.5
  • 33
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst Sect D 53:240-255.
    • (1997) Acta Cryst Sect D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 34
    • 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, Dodson G. 1996. Crystal structure of T state haemoglobin with oxygen bound at all four haems. J Mol Biol 256:775-792.
    • (1996) J Mol Biol , vol.256 , pp. 775-792
    • Paoli, M.1    Liddington, R.2    Tame, J.3    Wilkinson, A.4    Dodson, G.5
  • 35
    • 0000450916 scopus 로고
    • The oxygen equilibrium of hemoglobin and its structural interpretation
    • Pauling L. 1935. The oxygen equilibrium of hemoglobin and its structural interpretation. Proc Natl Acad Sci USA 21:186-191.
    • (1935) Proc Natl Acad Sci USA , vol.21 , pp. 186-191
    • Pauling, L.1
  • 36
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz MF. 1970. Stereochemistry of cooperative effects in haemoglobin. Nature 228:726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 37
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz MF. 1989. Mechanisms of cooperativity and allosteric regulation in proteins. Quart Rev Biophys 22:139-236.
    • (1989) Quart Rev Biophys , vol.22 , pp. 139-236
    • Perutz, M.F.1
  • 40
    • 0027197879 scopus 로고
    • Effect of chloride on oxygen binding to crystals of hemoglobin Rothschild (β37 Trp→Arg) in the T quaternary structure
    • Rivetti C, Mozzarelli A, Rossi GL, Kwiatkowski LD, Wierzba A, Noble RW. 1993b. Effect of chloride on oxygen binding to crystals of hemoglobin Rothschild (β37 Trp→Arg) in the T quaternary structure. Biochemistry 32:6411-6418.
    • (1993) Biochemistry , vol.32 , pp. 6411-6418
    • Rivetti, C.1    Mozzarelli, A.2    Rossi, G.L.3    Kwiatkowski, L.D.4    Wierzba, A.5    Noble, R.W.6
  • 41
    • 0024854847 scopus 로고
    • The 2.4-Å crystal-structure of Scapharca dimeric hemoglobin - Cooperatively based on directly communicating hemes at a novel subunit interface
    • Royer WE, Hendrickson WA, Chiancone E. 1989. The 2.4-Å crystal-structure of Scapharca dimeric hemoglobin - Cooperatively based on directly communicating hemes at a novel subunit interface. J Biol Chem 264:21052-21061.
    • (1989) J Biol Chem , vol.264 , pp. 21052-21061
    • Royer, W.E.1    Hendrickson, W.A.2    Chiancone, E.3
  • 42
    • 0024992934 scopus 로고
    • Structural transitions upon ligand binding in a cooperative dimeric hemoglobin
    • Royer WE, Hendrickson WA, Chiancone E. 1990. Structural transitions upon ligand binding in a cooperative dimeric hemoglobin. Science 249:518-521.
    • (1990) Science , vol.249 , pp. 518-521
    • Royer, W.E.1    Hendrickson, W.A.2    Chiancone, E.3
  • 43
    • 0017657283 scopus 로고
    • Properties of the T state of human oxyhemoglobin studied by laser photolysis
    • Sawicki CA, Gibson QH. 1977. Properties of the T state of human oxyhemoglobin studied by laser photolysis. J Biol Chem 252:7538-7547.
    • (1977) J Biol Chem , vol.252 , pp. 7538-7547
    • Sawicki, C.A.1    Gibson, Q.H.2
  • 44
    • 0022966804 scopus 로고
    • Oxygen equilibrium study and light absorption spectra of Ni(II)-Fe(II) hybrid hemoglobins
    • Shibayama N, Morimoto H, Kitagawa T. 1986a. Oxygen equilibrium study and light absorption spectra of Ni(II)-Fe(II) hybrid hemoglobins. J Mol Biol 192:322-329.
    • (1986) J Mol Biol , vol.192 , pp. 322-329
    • Shibayama, N.1    Morimoto, H.2    Kitagawa, T.3
  • 45
    • 0023022798 scopus 로고
    • Properties of chemically modified Ni(II)-Fe(II) hybrid hemoglobins. Ni(II) protoporphyrin IX as a model for a permanent deoxy-heme
    • Shibayama N, Morimoto H, Kitagawa T. 1986b. Properties of chemically modified Ni(II)-Fe(II) hybrid hemoglobins. Ni(II) protoporphyrin IX as a model for a permanent deoxy-heme. J Mol Biol 192:331-336.
    • (1986) J Mol Biol , vol.192 , pp. 331-336
    • Shibayama, N.1    Morimoto, H.2    Kitagawa, T.3
  • 46
    • 0030887993 scopus 로고    scopus 로고
    • +CN-)(αβ): No preferentially populating asymmetric hybrid at equilibrium
    • +CN-)(αβ): No preferentially populating asymmetric hybrid at equilibrium. Biochemistry 36:4375-4381.
    • (1997) Biochemistry , vol.36 , pp. 4375-4381
    • Shibayama, N.1    Morimoto, H.2    Saigo, S.3
  • 48
    • 0029163340 scopus 로고
    • Fixation of the quaternary structures of human adult hemoglobin by encapsulation in transparent porous silica gels
    • Shibayama N, Saigo S. 1995. Fixation of the quaternary structures of human adult hemoglobin by encapsulation in transparent porous silica gels. J Mol Biol 251:203-209.
    • (1995) J Mol Biol , vol.251 , pp. 203-209
    • Shibayama, N.1    Saigo, S.2
  • 49
    • 0030941242 scopus 로고    scopus 로고
    • Contribution of surface histidyl residues in the α-chain to the Bohr effect of human normal adult hemoglobin: Roles of global electrostatic effects
    • Sun DZP, Zou M, Ho NT, Ho C. 1997. Contribution of surface histidyl residues in the α-chain to the Bohr effect of human normal adult hemoglobin: Roles of global electrostatic effects. Biochemistry 36:6663-6673.
    • (1997) Biochemistry , vol.36 , pp. 6663-6673
    • Sun, D.Z.P.1    Zou, M.2    Ho, N.T.3    Ho, C.4


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