메뉴 건너뛰기




Volumn 285, Issue 4, 1999, Pages 1383-1388

Functional analysis of hemoglobin molecules locked in doubly liganded conformations

Author keywords

Allosteric effects; Hemoglobin; KNF model; MWC model; Silica gel

Indexed keywords

FERROUS ION; HEMOGLOBIN; NICKEL; PROTOPORPHYRIN; SILICA GEL;

EID: 0033614012     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2407     Document Type: Article
Times cited : (34)

References (28)
  • 2
    • 0031463937 scopus 로고    scopus 로고
    • T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride
    • Bettati S., Mozzarelli A. T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate, and chloride. J. Biol. Chem. 272:1997;32050-32055.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32050-32055
    • Bettati, S.1    Mozzarelli, A.2
  • 4
    • 0025979741 scopus 로고
    • Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching
    • Daugherty M. A., Shea M. A., Johnson J. A., LiCata V. J., Turner G. J., Ackers G. K. Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching. Proc. Natl Acad. Sci. USA. 88:1991;1110-1114.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1110-1114
    • Daugherty, M.A.1    Shea, M.A.2    Johnson, J.A.3    Licata, V.J.4    Turner, G.J.5    Ackers, G.K.6
  • 5
    • 0015240872 scopus 로고
    • Extensions of the allosteric model for haemoglobin
    • Edelstein S. J. Extensions of the allosteric model for haemoglobin. Nature. 230:1971;224-227.
    • (1971) Nature , vol.230 , pp. 224-227
    • Edelstein, S.J.1
  • 6
    • 0027128133 scopus 로고
    • Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method
    • Ellerby L. M., Nishida C. R., Nishida F., Yamanaka S. A., Dunn B., Valentine J. S., Zink J. I. Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method. Science. 255:1992;1113-1115.
    • (1992) Science , vol.255 , pp. 1113-1115
    • Ellerby, L.M.1    Nishida, C.R.2    Nishida, F.3    Yamanaka, S.A.4    Dunn, B.5    Valentine, J.S.6    Zink, J.I.7
  • 7
    • 0030907624 scopus 로고    scopus 로고
    • Can a two-state MWC allosteric model explain hemoglobin kinetics?
    • Henry E. R., Jones C. M., Hofrichter J., Eaton W. A. Can a two-state MWC allosteric model explain hemoglobin kinetics? Biochemistry. 36:1997;6511-6528.
    • (1997) Biochemistry , vol.36 , pp. 6511-6528
    • Henry, E.R.1    Jones, C.M.2    Hofrichter, J.3    Eaton, W.A.4
  • 8
    • 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. Advan. Protein Chem. 43:1992;153-312.
    • (1992) Advan. Protein Chem. , vol.43 , pp. 153-312
    • Ho, C.1
  • 10
    • 0016637031 scopus 로고
    • PH dependence of the Adair constants of human hemoglobin: Nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect
    • Imai K., Yonetani T. pH dependence of the Adair constants of human hemoglobin: nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect. J. Biol. Chem. 250:1975;2227-2231.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2227-2231
    • Imai, K.1    Yonetani, T.2
  • 11
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D. E., Nemethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 5:1966;365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 12
    • 0016210764 scopus 로고
    • Oxygen binding in cyanomet hybrid and normal hemoglobins: Applicability of sequential and two-state concerted models
    • Minton A. P. Oxygen binding in cyanomet hybrid and normal hemoglobins: applicability of sequential and two-state concerted models. Science. 184:1974;577-579.
    • (1974) Science , vol.184 , pp. 577-579
    • Minton, A.P.1
  • 13
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J., Wyman J., 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
  • 14
    • 0025801633 scopus 로고
    • Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect
    • Mozzarelli A., Rivetti C., Rossi G. L., Henry E. R., Eaton W. A. Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature. 351:1991;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
  • 15
    • 0014103899 scopus 로고
    • Spin-label study of hemoglobin conformation in solution
    • Ogawa S., McConnell H. M. Spin-label study of hemoglobin conformation in solution. Proc. Natl Acad. Sci. USA. 58:1967;19-26.
    • (1967) Proc. Natl Acad. Sci. USA , vol.58 , pp. 19-26
    • Ogawa, S.1    McConnell, H.M.2
  • 18
    • 0029163340 scopus 로고
    • Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels
    • Shibayama N., Saigo S. Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels. J. Mol. Biol. 251:1995;203-209.
    • (1995) J. Mol. Biol. , vol.251 , pp. 203-209
    • Shibayama, N.1    Saigo, S.2
  • 19
    • 0022966804 scopus 로고
    • Oxygen equilibrium study and light absorption spectra of Ni(II)-Fe(II) hybrid hemoglobins
    • Shibayama N., Morimoto H., Miyazaki G. Oxygen equilibrium study and light absorption spectra of Ni(II)-Fe(II) hybrid hemoglobins. J. Mol. Biol. 192:1986a;323-329.
    • (1986) J. Mol. Biol. , vol.192 , pp. 323-329
    • Shibayama, N.1    Morimoto, H.2    Miyazaki, G.3
  • 20
    • 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. 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. 192:1986b;331-336.
    • (1986) J. Mol. Biol. , vol.192 , pp. 331-336
    • Shibayama, N.1    Morimoto, H.2    Kitagawa, T.3
  • 21
    • 0023186282 scopus 로고
    • Proton nuclear magnetic resonance and spectrophotometric studies of nickel(II)-iron(II) hybrid hemoglobins
    • Shibayama N., Inubushi T., Morimoto H., Yonetani T. Proton nuclear magnetic resonance and spectrophotometric studies of nickel(II)-iron(II) hybrid hemoglobins. Biochemistry. 26:1987;2194-2201.
    • (1987) Biochemistry , vol.26 , pp. 2194-2201
    • Shibayama, N.1    Inubushi, T.2    Morimoto, H.3    Yonetani, T.4
  • 22
    • 0028942888 scopus 로고
    • Oxygen equilibrium properties of nickel(II)-iron(II) hybrid hemoglobins cross-linked between 82β1 and 82β2 lysyl residues by bis(3,5-dibromosalicyl)fumarate: Determination of the first two-step microscopic Adair constants for human hemoglobin
    • Shibayama N., Imai K., Morimoto H., Saigo S. Oxygen equilibrium properties of nickel(II)-iron(II) hybrid hemoglobins cross-linked between 82β1 and 82β2 lysyl residues by bis(3,5-dibromosalicyl)fumarate: determination of the first two-step microscopic Adair constants for human hemoglobin. Biochemistry. 34:1995a;4773-4780.
    • (1995) Biochemistry , vol.34 , pp. 4773-4780
    • Shibayama, N.1    Imai, K.2    Morimoto, H.3    Saigo, S.4
  • 23
    • 0028791577 scopus 로고
    • Mechanism of ligand binding to Ni(II)-Fe(II) hybrid hemoglobins
    • Shibayama N., Yonetani T., Regan R. M., Gibson Q. H. Mechanism of ligand binding to Ni(II)-Fe(II) hybrid hemoglobins. Biochemistry. 34:1995b;14658-14667.
    • (1995) Biochemistry , vol.34 , pp. 14658-14667
    • Shibayama, N.1    Yonetani, T.2    Regan, R.M.3    Gibson, Q.H.4
  • 26
    • 0000721403 scopus 로고
    • Characterization of partially ligated hemoglobins: NMR, ENDOR, CD, and stopped-flow studies of zinc-containing hemoglobin hybrids
    • Simolo K., Stucky G., Chen S., Bailey M., Scholes C., McLendon G. Characterization of partially ligated hemoglobins: NMR, ENDOR, CD, and stopped-flow studies of zinc-containing hemoglobin hybrids. J. Am. Chem. Soc. 107:1985;2865-2872.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2865-2872
    • Simolo, K.1    Stucky, G.2    Chen, S.3    Bailey, M.4    Scholes, C.5    McLendon, G.6
  • 27
    • 0015506515 scopus 로고
    • A mathematical model for structure-function relations in hemoglobin
    • Szabo A., Karplus M. A mathematical model for structure-function relations in hemoglobin. J. Mol. Biol. 72:1972;163-197.
    • (1972) J. Mol. Biol. , vol.72 , pp. 163-197
    • Szabo, A.1    Karplus, M.2
  • 28
    • 0027377056 scopus 로고
    • Oxygen equilibrium studies of cross-linked iron-cobalt hybrid hemoglobins: Models for partially ligated intermediates of cobalt hemoglobin
    • Tsuneshige A., Zhou Y.-X., Yonetani T. Oxygen equilibrium studies of cross-linked iron-cobalt hybrid hemoglobins: models for partially ligated intermediates of cobalt hemoglobin. J. Biol. Chem. 268:1993;23031-23040.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23031-23040
    • Tsuneshige, A.1    Zhou, Y.-X.2    Yonetani, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.