메뉴 건너뛰기




Volumn 76, Issue 3, 1999, Pages 1532-1536

Heterotropic effectors exert more significant strain on monoligated than on unligated hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

BEZAFIBRATE; CARBON MONOXIDE; CARBOXYHEMOGLOBIN; HEMOGLOBIN; LIGAND; PHYTIC ACID;

EID: 0033054114     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77312-1     Document Type: Article
Times cited : (12)

References (25)
  • 1
    • 0026671889 scopus 로고
    • X-ray diffraction study of di- and tetra-ligated T-state hemoglobin from high salt crystals
    • Abraham, D. J., R. A. Peascoe, R. S. Randad, and J. Panikker. 1992. X-ray diffraction study of di- 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
    • 0026569976 scopus 로고
    • Molecular code for cooperativity in hemoglobin
    • Ackers, G. K., M. L. Doyle, D. Myers, and M. A. Daugherty. 1992. Molecular code for cooperativity in hemoglobin. Science. 255:54-63.
    • (1992) Science , vol.255 , pp. 54-63
    • Ackers, G.K.1    Doyle, M.L.2    Myers, D.3    Daugherty, M.A.4
  • 4
    • 0014250343 scopus 로고
    • Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin
    • Benesch, R., R. E. Benesch, and C. I. Yu. 1968. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Natl. Acad. Sci. USA. 59:526-532.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.59 , pp. 526-532
    • Benesch, R.1    Benesch, R.E.2    Yu, C.I.3
  • 5
    • 0021051045 scopus 로고
    • Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism
    • Gelin, B. R., A. W.-M. Lee, and M. Karplus. 1983. Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. J. Mol. Biol. 171:489-559.
    • (1983) J. Mol. Biol. , vol.171 , pp. 489-559
    • Gelin, B.R.1    Lee, A.W.-M.2    Karplus, M.3
  • 9
    • 0027362732 scopus 로고
    • Modulated excitation of singly ligated carboxyhemoglobin
    • Liao, D., J. Jiang, M. Zhao, and F. A. Ferrone. 1993. Modulated excitation of singly ligated carboxyhemoglobin. Biophys. J. 65:2059-2067.
    • (1993) Biophys. J. , vol.65 , pp. 2059-2067
    • Liao, D.1    Jiang, J.2    Zhao, M.3    Ferrone, F.A.4
  • 10
    • 0022854187 scopus 로고
    • Testing the two-state model: Anomalous effector binding to human hemoglobin
    • Marden, M. C., E. S. Hazard, and Q. H. Gibson. 1986. Testing the two-state model: anomalous effector binding to human hemoglobin. Biochemistry. 25:7591-7596.
    • (1986) Biochemistry , vol.25 , pp. 7591-7596
    • Marden, M.C.1    Hazard, E.S.2    Gibson, Q.H.3
  • 11
    • 0024281313 scopus 로고
    • T-state hemoglobin with four ligands bound
    • Marden, M. C., J. Kister, B. Bohn, and C. Poyart. 1988. T-state hemoglobin with four ligands bound. Biochemistry. 27:1659-1664.
    • (1988) Biochemistry , vol.27 , pp. 1659-1664
    • Marden, M.C.1    Kister, J.2    Bohn, B.3    Poyart, C.4
  • 12
    • 0017138398 scopus 로고
    • Oxygenation-linked subunit interactions in human hemoglobin: Experimental studies on the concentration dependence of oxygenation curves
    • Mills, F. C., M. L. Johnson, and G. K. Ackers. 1976. Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves. Biochemistry. 15: 5350-5362.
    • (1976) Biochemistry , vol.15 , pp. 5350-5362
    • Mills, F.C.1    Johnson, M.L.2    Ackers, G.K.3
  • 13
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., J. Wyman, and J.-P. Changeux. 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
  • 14
    • 0001244916 scopus 로고
    • e(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures
    • e(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures. Proc. Natl. Acad. Sci. USA. 77:2033-2037.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2033-2037
    • Nagai, K.1    Kitagawa, T.2
  • 15
    • 0030000410 scopus 로고    scopus 로고
    • Crystal structure of T state haemoglobin with oxygen bound at all four haems
    • Paoli, M., R. Liddington, J. Tame, A. Wilkinson, and G. Dodson. 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
  • 16
    • 0032584325 scopus 로고    scopus 로고
    • A possible allosteric communication pathway identified through a resonance Raman study of four β37 mutants of human hemoglobin A
    • Peterson, E. S., and J. M. Friedman. 1998. A possible allosteric communication pathway identified through a resonance Raman study of four β37 mutants of human hemoglobin A. Biochemistry. 37:4346-4357.
    • (1998) Biochemistry , vol.37 , pp. 4346-4357
    • Peterson, E.S.1    Friedman, J.M.2
  • 17
    • 0026787413 scopus 로고
    • The association reaction between hemoglobin and carbon monoxide as studied by the isolation of the intermediates. Implications on the mechanism of cooperativity
    • Perrella, M., N. Davids, and L. Rossi-Bernardi. 1992. The association reaction between hemoglobin and carbon monoxide as studied by the isolation of the intermediates. Implications on the mechanism of cooperativity. J. Biol. Chem. 267:8744-8751.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8744-8751
    • Perrella, M.1    Davids, N.2    Rossi-Bernardi, L.3
  • 18
    • 0022634647 scopus 로고
    • Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding
    • Perutz, M. F., G. Fermi, D. J. Abraham, C. Poyart, and E. Bureaux. 1986. Hemoglobin as a receptor of drugs and peptides: x-ray studies of the stereochemistry of binding. J. Am. Chem. Soc. 108:1064-1078.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1064-1078
    • Perutz, M.F.1    Fermi, G.2    Abraham, D.J.3    Poyart, C.4    Bureaux, E.5
  • 19
    • 0020959160 scopus 로고
    • Bezafibrate lowers oxygen affinity of haemoglobin
    • Perutz, M. F., and C. Poyart. 1983. Bezafibrate lowers oxygen affinity of haemoglobin. Lancet. 881-882.
    • (1983) Lancet , pp. 881-882
    • Perutz, M.F.1    Poyart, C.2
  • 21
    • 0027381305 scopus 로고
    • Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 Å resolution
    • Richard, V., G. G. Dodson, and Y. Mauguen. 1993. Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 Å resolution. J. Mol. Biol. 233:270-274.
    • (1993) J. Mol. Biol. , vol.233 , pp. 270-274
    • Richard, V.1    Dodson, G.G.2    Mauguen, Y.3
  • 22
    • 0019765114 scopus 로고
    • Preparation of blood hemoglobins of vertebrates
    • Riggs, A. 1981. Preparation of blood hemoglobins of vertebrates. Methods Enzymol. 76:5-29.
    • (1981) Methods Enzymol. , vol.76 , pp. 5-29
    • Riggs, A.1
  • 23
    • 0021486088 scopus 로고
    • Tertiary-structure relaxation in hemoglobin: A transient Raman study
    • Scott, T. W., and J. M. Friedman. 1984. Tertiary-structure relaxation in hemoglobin: a transient Raman study. J. Am. Chem. Soc. 106: 5677-5687.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5677-5687
    • Scott, T.W.1    Friedman, J.M.2
  • 24
    • 0017113593 scopus 로고
    • Dissociation of CO from carboxyhemoglobin
    • Sharma, V. S., M. R. Schmidt, and H. M. Ranney. 1976. Dissociation of CO from carboxyhemoglobin. J. Biol. Chem. 251:4267-4272.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4267-4272
    • Sharma, V.S.1    Schmidt, M.R.2    Ranney, H.M.3
  • 25
    • 0021527182 scopus 로고
    • Linkage graphs: A study in the thermodynamics of macromolecules
    • Wyman, J. 1984. Linkage graphs: a study in the thermodynamics of macromolecules. Q. Rev. Biophys. 17:453-488.
    • (1984) Q. Rev. Biophys. , vol.17 , pp. 453-488
    • Wyman, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.