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Volumn 182, Issue 3, 2004, Pages 229-244

The Bohr effect of haemoglobin in vertebrates: An example of molecular adaptation to different physiological requirements

Author keywords

Bohr effect; Haemoglobin; Molecular adaptation; Vertebrates

Indexed keywords

CHLORIDE; HEMOGLOBIN; HEMOGLOBIN A; PROTON;

EID: 7944219982     PISSN: 00016772     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-201X.2004.01360.x     Document Type: Review
Times cited : (36)

References (82)
  • 1
    • 0001459583 scopus 로고
    • Hemoglobin and myoglobin in their reactions with ligands
    • A. Neuberger & E.L. Tatum (eds). North-Holland Publishing, Amsterdam
    • Antonini, E. & Brunori, M. 1971. Hemoglobin and myoglobin in their reactions with ligands. In: A. Neuberger & E.L. Tatum (eds), Frontiers of Biology, Vol. 21. North-Holland Publishing, Amsterdam.
    • (1971) Frontiers of Biology , vol.21
    • Antonini, E.1    Brunori, M.2
  • 2
    • 78651185507 scopus 로고
    • Studies on the relations between molecular and functional properties of hemoglobin. T. The influence of temperature on the Bohr effect in human and in horse hemoglobin
    • Antonini, E., Wyman, J., Brunori, M., Fronticelli, C., Bucci, E. & Rossi-Fanelli, A. 1965. Studies on the relations between molecular and functional properties of hemoglobin. T. The influence of temperature on the Bohr effect in human and in horse hemoglobin. J Biol Chem 240, 1096-1103.
    • (1965) J Biol Chem , vol.240 , pp. 1096-1103
    • Antonini, E.1    Wyman, J.2    Brunori, M.3    Fronticelli, C.4    Bucci, E.5    Rossi-Fanelli, A.6
  • 3
    • 0015991066 scopus 로고
    • X-ray studies of the interaction of CO2 with human deoxyhemoglobin
    • Arnone, A. 1974. X-ray studies of the interaction of CO2 with human deoxyhemoglobin. Nature 247, 143-145.
    • (1974) Nature , vol.247 , pp. 143-145
    • Arnone, A.1
  • 4
    • 0016345571 scopus 로고
    • Structure of inositol hexaphosphate-human deoxyhaemoglobin complex
    • Arnone, A. & Perutz, M.F. 1974. Structure of inositol hexaphosphate-human deoxyhaemoglobin complex. Nature 49, 34-36.
    • (1974) Nature , vol.49 , pp. 34-36
    • Arnone, A.1    Perutz, M.F.2
  • 5
    • 0027427606 scopus 로고
    • Functional, spectroscopic and structural properties of hemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra bircus ibex)
    • Ascenzi, P., dementi, M.E., Condò, S.G. et al. 1993. Functional, spectroscopic and structural properties of hemoglobin from chamois (Rupicapra rupicapra) and steinbock (Capra bircus ibex). Biocbem J 296, 361-365.
    • (1993) Biocbem J , vol.296 , pp. 361-365
    • Ascenzi, P.1    Dementi, M.E.2    Condò, S.G.3
  • 7
    • 84935023004 scopus 로고
    • Über einen in biologischen beziehung wichtigen einfluss, den die kohlensäurespannung des blutes auf desen sauerstoffbinding übt
    • Bohr, C., Hasselbalch, K.A. & Krogh, A. 1904. Über Einen in Biologischen Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf desen Sauerstoffbinding Übt. Skand Arch Physiol 16, 401-412.
    • (1904) Skand Arch Physiol , vol.16 , pp. 401-412
    • Bohr, C.1    Hasselbalch, K.A.2    Krogh, A.3
  • 8
    • 0017617947 scopus 로고
    • Anion modulation of the negative Bohr effect of hemoglobin, from a primitive amphibian
    • Bonaventura, C., Sullivan, B., Bonaventura, J. & Bourne, S. 1977. Anion modulation of the negative Bohr effect of hemoglobin, from a primitive amphibian. Nature 265, 474-476.
    • (1977) Nature , vol.265 , pp. 474-476
    • Bonaventura, C.1    Sullivan, B.2    Bonaventura, J.3    Bourne, S.4
  • 9
    • 0032168138 scopus 로고    scopus 로고
    • Hydrogen ion titrations of the anodic and cathodic haemoglobin components of the European eel Anguilla anguilla
    • Brauner, C.J. & Weber, R.E. 1998. Hydrogen ion titrations of the anodic and cathodic haemoglobin components of the European eel Anguilla anguilla. J Exp Biol 201, 2507-2514.
    • (1998) J Exp Biol , vol.201 , pp. 2507-2514
    • Brauner, C.J.1    Weber, R.E.2
  • 10
    • 0018673805 scopus 로고
    • The primary structure of the hemoglobin of the greylag goose (Anser anser) and the unequal evolution of the beta-chains
    • Braunitzer, G. & Oberthur, W. 1979. The primary structure of the hemoglobin of the greylag goose (Anser anser) and the unequal evolution of the beta-chains. Hoppe Seylers Z Physiol Chem 360, 679-683.
    • (1979) Hoppe Seylers Z Physiol Chem , vol.360 , pp. 679-683
    • Braunitzer, G.1    Oberthur, W.2
  • 12
    • 0016416337 scopus 로고
    • Molecular adaptation to physiological requirements: The hemoglobin system of trout
    • Brunori, M. 1975. Molecular adaptation to physiological requirements: the hemoglobin system of trout. Curr Top Cell Regul 9, 1-39.
    • (1975) Curr Top Cell Regul , vol.9 , pp. 1-39
    • Brunori, M.1
  • 13
    • 0015902888 scopus 로고
    • Hemoglobin system of trout - Equilibria and kinetics of ligand binding by isolated components
    • Brunori, M., Giardina, B., Binotti, I. & Antonini, E. 1973. Hemoglobin system of trout - equilibria and kinetics of ligand binding by isolated components. Acta Vitaminol Enzymol 27, 29-36.
    • (1973) Acta Vitaminol Enzymol , vol.27 , pp. 29-36
    • Brunori, M.1    Giardina, B.2    Binotti, I.3    Antonini, E.4
  • 14
    • 0016785434 scopus 로고
    • Effect of anions on the oxygen binding properties of the hemoglobin components from trout (Salmo irideus)
    • Brunori, M., Falcioni, G., Fortuna, G. & Giardina, B. 1975. Effect of anions on the oxygen binding properties of the hemoglobin components from trout (Salmo irideus). Arch Biochem Biophys 168, 512-519.
    • (1975) Arch Biochem Biophys , vol.168 , pp. 512-519
    • Brunori, M.1    Falcioni, G.2    Fortuna, G.3    Giardina, B.4
  • 15
    • 0016830466 scopus 로고
    • The interaction of organic phosphates with human and chicken hemoglobin
    • Brygier, J., De Bruin, S.H., Van Hoof, M.K. & Rollema, H.S. 1975. The interaction of organic phosphates with human and chicken hemoglobin. Eur J Biochem 60, 379-383.
    • (1975) Eur J Biochem , vol.60 , pp. 379-383
    • Brygier, J.1    De Bruin, S.H.2    Van Hoof, M.K.3    Rollema, H.S.4
  • 16
    • 0015210116 scopus 로고
    • Differences in the interaction of 2,3-diphosphoglycerate with certain mammalian hemoglobins
    • Bunn, H.F. 1971. Differences in the interaction of 2,3-diphosphoglycerate with certain mammalian hemoglobins. Science 172, 1049-1050.
    • (1971) Science , vol.172 , pp. 1049-1050
    • Bunn, H.F.1
  • 17
    • 7944236840 scopus 로고
    • Les hemoglobines des amphibiens: Separation et caracterisation preliminaire des chaines d'une hemoglobine du crapaud Bufo bufo
    • Caffin, J.P., Chauvet, J.P. & Acher, R. 1969. Les hemoglobines des amphibiens: separation et caracterisation preliminaire des chaines d'une hemoglobine du crapaud Bufo bufo. FEBS Lett 5, 196-198.
    • (1969) FEBS Lett , vol.5 , pp. 196-198
    • Caffin, J.P.1    Chauvet, J.P.2    Acher, R.3
  • 19
    • 0026579114 scopus 로고
    • A comparative study of the temperature dependence of the oxygen-binding properties of mammalian hemoglobins
    • Coletta, M., Clementi, M.E., Ascenzi, P., Petruzzelli, R., Condò, S.G. & Giardina, B. 1992. A comparative study of the temperature dependence of the oxygen-binding properties of mammalian hemoglobins. Eur J Biochem 204, 1155-1157.
    • (1992) Eur J Biochem , vol.204 , pp. 1155-1157
    • Coletta, M.1    Clementi, M.E.2    Ascenzi, P.3    Petruzzelli, R.4    Condò, S.G.5    Giardina, B.6
  • 21
    • 0030838805 scopus 로고    scopus 로고
    • A comparative study on the functional properties of the wild European mouflon and domestic sheep hemoglobins
    • Corda, M., Giardina, B., Pellegrini, M. et al. 1997. A comparative study on the functional properties of the wild European mouflon and domestic sheep hemoglobins. Comp Biochem Physiol B Biochem Mol Biol 117, 417-420.
    • (1997) Comp Biochem Physiol B Biochem Mol Biol , vol.117 , pp. 417-420
    • Corda, M.1    Giardina, B.2    Pellegrini, M.3
  • 22
    • 0014211650 scopus 로고
    • Acetylated peptide chains in bullfrog hemoglobins
    • De Wirt, W. & Ingram, V.M. 1967. Acetylated peptide chains in bullfrog hemoglobins. Biochem Biophys Res Commun 27, 236-241.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 236-241
    • De Wirt, W.1    Ingram, V.M.2
  • 23
    • 0029163616 scopus 로고
    • The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity
    • Fago, A., Carratore, V., di Frisco, G., Feuerlein, R.J., Sottrup-Jensen, L. & Weber, R.E. 1995. The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity. J Biol Chem 270, 18897-18902.
    • (1995) J Biol Chem , vol.270 , pp. 18897-18902
    • Fago, A.1    Carratore, V.2    Di Frisco, G.3    Feuerlein, R.J.4    Sottrup-Jensen, L.5    Weber, R.E.6
  • 24
    • 0030905324 scopus 로고    scopus 로고
    • The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a root-effect hemoglobin
    • Fago, A., Bendixen, E., Malte, H. & Weber, R.E. 1997. The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a root-effect hemoglobin. J Biol Chem 272, 15628-15635.
    • (1997) J Biol Chem , vol.272 , pp. 15628-15635
    • Fago, A.1    Bendixen, E.2    Malte, H.3    Weber, R.E.4
  • 25
    • 0023656180 scopus 로고
    • Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X-ray studies of carboxymethylated hemoglobin and X-ray studies of carbamino hemoglobin
    • Fantl, W.J., DiDonato, A., Manning, J.M., Rogers, P.H. & Arnone, A. 1987. Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X-ray studies of carboxymethylated hemoglobin and X-ray studies of carbamino hemoglobin. J Biol Chem 262, 12700-12713.
    • (1987) J Biol Chem , vol.262 , pp. 12700-12713
    • Fantl, W.J.1    DiDonato, A.2    Manning, J.M.3    Rogers, P.H.4    Arnone, A.5
  • 26
    • 0030037572 scopus 로고    scopus 로고
    • Oxygen equilibria of cathodic eel hemoglobin analysed in terms of the MWC model and Adair's successive oxygenation theory
    • Feuerlein, R.J. & Weber, R.E. 1996. Oxygen equilibria of cathodic eel hemoglobin analysed in terms of the MWC model and Adair's successive oxygenation theory. J Comp Physiol B 165, 597-606.
    • (1996) J Comp Physiol B , vol.165 , pp. 597-606
    • Feuerlein, R.J.1    Weber, R.E.2
  • 27
    • 0024507074 scopus 로고
    • Arctic adaptation in reindeer. The energy saving of a hemoglobin
    • Giardina, B., Brix, O., Nuutinen, M. et al. 1989. Arctic adaptation in reindeer. The energy saving of a hemoglobin. FEBS Lett 247, 135-138.
    • (1989) FEBS Lett , vol.247 , pp. 135-138
    • Giardina, B.1    Brix, O.2    Nuutinen, M.3
  • 28
    • 0025250645 scopus 로고
    • Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach
    • Giardina, B., Brix, O., Colosimo, A., Petruzzelli, R., Cerroni, L. & Condò, S.G. 1990a. Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach. Eur J Biochem 194, 61-65.
    • (1990) Eur J Biochem , vol.194 , pp. 61-65
    • Giardina, B.1    Brix, O.2    Colosimo, A.3    Petruzzelli, R.4    Cerroni, L.5    Condò, S.G.6
  • 29
    • 0025126281 scopus 로고
    • Flight and heat dissipation in birds. A possible molecular mechanism
    • Giardina, B., Corda, M., Pellegrini, M.G. et al. 1990b. Flight and heat dissipation in birds. A possible molecular mechanism. FEBS Lett 270, 173-176.
    • (1990) FEBS Lett , vol.270 , pp. 173-176
    • Giardina, B.1    Corda, M.2    Pellegrini, M.G.3
  • 30
    • 0015935317 scopus 로고
    • Structure and function of the isolated hemoglobins of the American eel. Anguilla rostrata
    • Gillen, R.G. & Riggs, A. 1973. Structure and function of the isolated hemoglobins of the American eel, Anguilla rostrata. J Biol Chem 248, 1961-1969.
    • (1973) J Biol Chem , vol.248 , pp. 1961-1969
    • Gillen, R.G.1    Riggs, A.2
  • 31
    • 84886639405 scopus 로고
    • Stereochemistry of ATP and GTP bound to fish hemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study
    • Gronenborn, A.M., Clore, G.M., Brunori, M., Giardina, B., Falcioni, G. & Perutz, M.F. 1984. Stereochemistry of ATP and GTP bound to fish hemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study. J Mol Biol 178, 731-742.
    • (1984) J Mol Biol , vol.178 , pp. 731-742
    • Gronenborn, A.M.1    Clore, G.M.2    Brunori, M.3    Giardina, B.4    Falcioni, G.5    Perutz, M.F.6
  • 32
    • 0014146844 scopus 로고
    • Temperature regulation during flight in pigeons
    • Hart, J.S. & Roy, O.Z. 1967. Temperature regulation during flight in pigeons. Am J Physiol 213, 1311-1316.
    • (1967) Am J Physiol , vol.213 , pp. 1311-1316
    • Hart, J.S.1    Roy, O.Z.2
  • 33
    • 17444441893 scopus 로고
    • On the phylogeny of the hemoglobin molecule. On the polymorphism and the N-terminal amino acids of carp hemoglobin
    • Hilse, K., Sorger, U. & Braunitzer, G. 1966. On the phylogeny of the hemoglobin molecule. On the polymorphism and the N-terminal amino acids of carp hemoglobin. Hoppe Seylers Z Physiol Chem 344, 166-168.
    • (1966) Hoppe Seylers Z Physiol Chem , vol.344 , pp. 166-168
    • Hilse, K.1    Sorger, U.2    Braunitzer, G.3
  • 34
    • 0017377947 scopus 로고
    • Studies on avian erythrocyte metabolism. Inositol tetrakisphosphate: The major phosphate compound in the erythrocytes of the ostrich (Struthio camelus camelus)
    • Isaacks, R., Harkness, D., Sampsell, R. et al. 1977a. Studies on avian erythrocyte metabolism. Inositol tetrakisphosphate: the major phosphate compound in the erythrocytes of the ostrich (Struthio camelus camelus). Eur J Biochem 77, 567-574.
    • (1977) Eur J Biochem , vol.77 , pp. 567-574
    • Isaacks, R.1    Harkness, D.2    Sampsell, R.3
  • 35
    • 0017622249 scopus 로고
    • Studies on avian erythrocyte metabolism. VII. Effect of inositol pentaphosphate and other organic phosphates on oxygen affinity of the embryonic and adult-type hemoglobins of the turkey embryo
    • Isaacks, R.E., Harkness, D.R., Goldman, P.H., Adler, J.L. & Kim, C.Y. 1977b. Studies on avian erythrocyte metabolism. VII. Effect of inositol pentaphosphate and other organic phosphates on oxygen affinity of the embryonic and adult-type hemoglobins of the turkey embryo. Hemoglobin 1, 577-593.
    • (1977) Hemoglobin , vol.1 , pp. 577-593
    • Isaacks, R.E.1    Harkness, D.R.2    Goldman, P.H.3    Adler, J.L.4    Kim, C.Y.5
  • 36
    • 0028981025 scopus 로고
    • Structure of deoxyhemoglobin of the antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded hemoglobin structures
    • Ito, N., Komiyama, N.H. & Fermi, G. 1995. Structure of deoxyhemoglobin of the antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded hemoglobin structures. J Mol Biol 250, 648-658.
    • (1995) J Mol Biol , vol.250 , pp. 648-658
    • Ito, N.1    Komiyama, N.H.2    Fermi, G.3
  • 37
    • 0026095651 scopus 로고
    • Adaptation of bird hemoglobins to high altitudes: Demonstration of molecular mechanism by protein engineering
    • Jessen, T.H., Weber, R.E., Fermi, G., Tame, J. & Braunitzer, G. 1991. Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering. Proc Natl Acad Sci USA 88, 6519-6522.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6519-6522
    • Jessen, T.H.1    Weber, R.E.2    Fermi, G.3    Tame, J.4    Braunitzer, G.5
  • 38
    • 0023788207 scopus 로고
    • Functional properties of hemoglobin in human red cells: II. Determination of the Bohr effect
    • Kister, J., Marden, M.C., Bohn, B. & Poyart, C. 1988. Functional properties of hemoglobin in human red cells: II. Determination of the Bohr effect. Respir Physiol 73, 363-378.
    • (1988) Respir Physiol , vol.73 , pp. 363-378
    • Kister, J.1    Marden, M.C.2    Bohn, B.3    Poyart, C.4
  • 39
    • 0023411854 scopus 로고
    • The primary structure of the pallid bat (Antrozous pallidus, Chiroptera) hemoglobin
    • Kleinschmidt, T., Koop, B.F. & Braunitzer, G. 1987. The primary structure of the pallid bat (Antrozous pallidus, Chiroptera) hemoglobin. Biol Chem Hoppe Seyler 368, 1197-2202.
    • (1987) Biol Chem Hoppe Seyler , vol.368 , pp. 1197-2202
    • Kleinschmidt, T.1    Koop, B.F.2    Braunitzer, G.3
  • 40
    • 0028852689 scopus 로고
    • Transplanting a unique allosteric effect from crocodile into human haemoglobin
    • Komiyama, N.H., Miyazaki, G., Tame, J. & Nagai, K. 1995. Transplanting a unique allosteric effect from crocodile into human haemoglobin. Nature 373, 244-246.
    • (1995) Nature , vol.373 , pp. 244-246
    • Komiyama, N.H.1    Miyazaki, G.2    Tame, J.3    Nagai, K.4
  • 41
    • 0035850791 scopus 로고    scopus 로고
    • The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity
    • Liang, Y., Hua, Z., Liang, X., Xu, Q. & Lu, G. 2001. The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity. J Mol Biol 313, 123-137.
    • (2001) J Mol Biol , vol.313 , pp. 123-137
    • Liang, Y.1    Hua, Z.2    Liang, X.3    Xu, Q.4    Lu, G.5
  • 42
    • 0021193127 scopus 로고
    • Quantitative evaluation for the role of beta βHis and β143 His residues in the Bohr effect of human hemoglobin in the presence of 0.1 M chloride ion
    • Matsukawa, S., Itatani, Y., Mawatari, K., Shimokawa, Y. & Yoneyama, Y. 1984. Quantitative evaluation for the role of beta βHis and β143 His residues in the Bohr effect of human hemoglobin in the presence of 0.1 M chloride ion. J Biol Chem 259, 11479-11486,
    • (1984) J Biol Chem , vol.259 , pp. 11479-11486
    • Matsukawa, S.1    Itatani, Y.2    Mawatari, K.3    Shimokawa, Y.4    Yoneyama, Y.5
  • 43
    • 0028081486 scopus 로고
    • The effect of inositol hexaphosphate in the high-affinity hemoglobin of the Andean chicken (Gallus gallus)
    • Mejia, O., Leon-Velarde, F. & Monge, C. 1994. The effect of inositol hexaphosphate in the high-affinity hemoglobin of the Andean chicken (Gallus gallus). Comp Biochem Physiol B Biochem Mol Biol 109, 437-441.
    • (1994) Comp Biochem Physiol B Biochem Mol Biol , vol.109 , pp. 437-441
    • Mejia, O.1    Leon-Velarde, F.2    Monge, C.3
  • 44
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. & Changeaux, 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    Changeaux, J.P.3
  • 45
    • 0033574669 scopus 로고    scopus 로고
    • Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question
    • Mazzarella, L., D'Avino, R., di Frisco, G. et al. 1999. Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question. J Mol Biol 287, 897-906.
    • (1999) J Mol Biol , vol.287 , pp. 897-906
    • Mazzarella, L.1    D'Avino, R.2    Di Frisco, G.3
  • 46
    • 0030901801 scopus 로고    scopus 로고
    • Oxygen and carbon dioxide transport in vertebrate erythrocytes: An evolutionary change in the role of membrane transport
    • Nikinmaa, M. 1997. Oxygen and carbon dioxide transport in vertebrate erythrocytes: an evolutionary change in the role of membrane transport. J Exp Biol 200, 369-380.
    • (1997) J Exp Biol , vol.200 , pp. 369-380
    • Nikinmaa, M.1
  • 47
    • 0018572809 scopus 로고
    • X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1α
    • O'Donnell, S., Mandaro, R., Schuster, T.M. & Arnone, A. 1979. X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1α. J Biol Chem 254, 12204-12208.
    • (1979) J Biol Chem , vol.254 , pp. 12204-12208
    • O'Donnell, S.1    Mandaro, R.2    Schuster, T.M.3    Arnone, A.4
  • 48
    • 0019211691 scopus 로고
    • Changes in pKa values of individual histidine residues of human hemoglobin upon reaction with carbon monoxide
    • Ohe, M. & Kajita, A. 1980. Changes in pKa values of individual histidine residues of human hemoglobin upon reaction with carbon monoxide. Biochemistry 19, 4443-4450.
    • (1980) Biochemistry , vol.19 , pp. 4443-4450
    • Ohe, M.1    Kajita, A.2
  • 49
    • 0028886065 scopus 로고
    • Structure/function relationships in the hemoglobin components from moray (Muraena helena)
    • Pellegrini, M., Giardina, B., Olianas, A. et al. 1995. Structure/ function relationships in the hemoglobin components from moray (Muraena helena). Eur J Biochem 234, 431-436.
    • (1995) Eur J Biochem , vol.234 , pp. 431-436
    • Pellegrini, M.1    Giardina, B.2    Olianas, A.3
  • 50
    • 0033559631 scopus 로고    scopus 로고
    • Low-temperature sensitivity and enhanced Bohr effect in red deer (Cervus elaphus) hemoglobin: A molecular adaptive strategy to life at high altitude and low temperature
    • Pellegrini, M., Giardina, B., Cartagnola, M. et al. 1999. Low-temperature sensitivity and enhanced Bohr effect in red deer (Cervus elaphus) hemoglobin: a molecular adaptive strategy to life at high altitude and low temperature. Eur J Biochem 260, 667-671.
    • (1999) Eur J Biochem , vol.260 , pp. 667-671
    • Pellegrini, M.1    Giardina, B.2    Cartagnola, M.3
  • 51
    • 0037591730 scopus 로고    scopus 로고
    • Structural-functional characterization of the cathodic hemoglobin of the conger eel Conger conger: Molecular modelling study of an additional phosphate-binding site
    • Pellegrini, M., Giardina, B., Verde, C. et al. 2003. Structural- functional characterization of the cathodic hemoglobin of the conger eel Conger conger: molecular modelling study of an additional phosphate-binding site. Biochem J 372, 679-686.
    • (2003) Biochem J , vol.372 , pp. 679-686
    • Pellegrini, M.1    Giardina, B.2    Verde, C.3
  • 52
    • 0016712736 scopus 로고
    • Structural states and transitions of carp hemoglobin
    • Pennelly, R.R., Tan-Wilson, A.L. & Noble, R.W. 1975. Structural states and transitions of carp hemoglobin. J Biol Chem 250, 7239-7244.
    • (1975) J Biol Chem , vol.250 , pp. 7239-7244
    • Pennelly, R.R.1    Tan-Wilson, A.L.2    Noble, R.W.3
  • 53
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in hemoglobin
    • Perutz, M.F. 1970. Stereochemistry of cooperative effects in hemoglobin. Nature 228, 726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 54
    • 0021004799 scopus 로고
    • Species adaptation in a protein molecule
    • Perutz, M.F. 1983. Species adaptation in a protein molecule. Mol Biol Evol 1, 1-28.
    • (1983) Mol Biol Evol , vol.1 , pp. 1-28
    • Perutz, M.F.1
  • 55
    • 0029881314 scopus 로고    scopus 로고
    • Cause of the Root effect in fish hemoglobins
    • Perutz, M.F. 1996. Cause of the Root effect in fish hemoglobins. Nat Struct Biol 3, 211-212.
    • (1996) Nat Struct Biol , vol.3 , pp. 211-212
    • Perutz, M.F.1
  • 56
    • 0019964409 scopus 로고
    • Stereochemistry of cooperative effects in fish an amphibian hemoglobins
    • Perutz, M.F. & Brunori, M. 1982. Stereochemistry of cooperative effects in fish an amphibian hemoglobins. Nature 299, 421-426.
    • (1982) Nature , vol.299 , pp. 421-426
    • Perutz, M.F.1    Brunori, M.2
  • 57
    • 0018860147 scopus 로고
    • Regulation of oxygen affinity of mammalian hemoglobins
    • Perutz, M.F. & Imai, K. 1980. Regulation of oxygen affinity of mammalian hemoglobins. J Mol Biol 136, 183-191.
    • (1980) J Mol Biol , vol.136 , pp. 183-191
    • Perutz, M.F.1    Imai, K.2
  • 58
    • 0019797209 scopus 로고
    • Allosteric regulation of crocodilian hemoglobin
    • Perutz, M.F., Bauer, C., Gros, G. et al. 1981. Allosteric regulation of crocodilian hemoglobin. Nature 291, 682-684.
    • (1981) Nature , vol.291 , pp. 682-684
    • Perutz, M.F.1    Bauer, C.2    Gros, G.3
  • 59
    • 0029780026 scopus 로고    scopus 로고
    • Diving behaviour and hemoglobin function: The primary structure of the α- and β-chains of the sea turtle (Caretta caretta) and its functional implications
    • Petruzzelli, R., Aureli, G., Lania, A., Galtieri, A., Desideri, A. & Giardina, B. 1996. Diving behaviour and hemoglobin function: the primary structure of the α- and β-chains of the sea turtle (Caretta caretta) and its functional implications. Biochem J 316, 959-965.
    • (1996) Biochem J , vol.316 , pp. 959-965
    • Petruzzelli, R.1    Aureli, G.2    Lania, A.3    Galtieri, A.4    Desideri, A.5    Giardina, B.6
  • 61
    • 0020669007 scopus 로고
    • Erythrocytic phosphates and flying activity in birds
    • Riera, M., Palomeque, J. & Planas, J. 1983. Erythrocytic phosphates and flying activity in birds. Comp Biochem Physiol A 74, 849-854.
    • (1983) Comp Biochem Physiol A , vol.74 , pp. 849-854
    • Riera, M.1    Palomeque, J.2    Planas, J.3
  • 62
    • 0023836405 scopus 로고
    • The Bohr effect
    • Riggs, A.F. 1988. The Bohr effect. Annu Rev Physiol 50, 181-204.
    • (1988) Annu Rev Physiol , vol.50 , pp. 181-204
    • Riggs, A.F.1
  • 63
    • 0021441888 scopus 로고
    • Primary structure, biochemical and physiological aspects of hemoglobin from South American lungfish (Lepidosiren paradoxus, Dipnoi)
    • Rodewald, K., Stangl, A. & Braunitzer, G. 1984. Primary structure, biochemical and physiological aspects of hemoglobin from South American lungfish (Lepidosiren paradoxus, Dipnoi). Hoppe Seylers Z Physiol Chem 365, 639-649.
    • (1984) Hoppe Seylers Z Physiol Chem , vol.365 , pp. 639-649
    • Rodewald, K.1    Stangl, A.2    Braunitzer, G.3
  • 64
    • 0018572254 scopus 로고
    • The interaction of inositol pentaphosphate with the hemoglobins of highland and lowland geese
    • Rollema, H.S. & Bauer, C. 1979. The interaction of inositol pentaphosphate with the hemoglobins of highland and lowland geese. J Biol Chem 254, 12038-12043.
    • (1979) J Biol Chem , vol.254 , pp. 12038-12043
    • Rollema, H.S.1    Bauer, C.2
  • 65
    • 0022558891 scopus 로고
    • Assessment of role of beta β-histidyl and other histidyl residues in the Bohr effect of human normal adult hemoglobin
    • Russu, I.M. & Ho, C. 1986. Assessment of role of beta β-histidyl and other histidyl residues in the Bohr effect of human normal adult hemoglobin. Biochemistry 25, 1706-1716.
    • (1986) Biochemistry , vol.25 , pp. 1706-1716
    • Russu, I.M.1    Ho, C.2
  • 66
    • 0018868084 scopus 로고
    • Role of the β146 histidyl residue in the alkaline Bohr effect of hemoglobin
    • Russu, I.M., Ho, N.T. & Ho, C. 1980. Role of the β146 histidyl residue in the alkaline Bohr effect of hemoglobin. Biochemistry 19, 1043-1052.
    • (1980) Biochemistry , vol.19 , pp. 1043-1052
    • Russu, I.M.1    Ho, N.T.2    Ho, C.3
  • 67
    • 0028284553 scopus 로고
    • Adaptation to extreme environments: Structure-function relationships in Emperor penguin hemoglobin
    • Tamburrini, M., Condò, S.G., di Prisco, G. & Giardina, B. 1994. Adaptation to extreme environments: structure-function relationships in Emperor penguin hemoglobin. J Mol Biol 237, 615-621.
    • (1994) J Mol Biol , vol.237 , pp. 615-621
    • Tamburrini, M.1    Condò, S.G.2    Di Prisco, G.3    Giardina, B.4
  • 68
    • 0033807219 scopus 로고    scopus 로고
    • Structural and functional analysis of the two hemoglobins of the Antarctic seabird Catharacta maccormicki characterization of an additional phosphate binding site by molecular modelling
    • Tamburrini, M., Riccio, A., Romano, M., Giardina, B. & di Prisco, G. 2000. Structural and functional analysis of the two hemoglobins of the Antarctic seabird Catharacta maccormicki characterization of an additional phosphate binding site by molecular modelling. Eur J Biochem 267, 6089-6098.
    • (2000) Eur J Biochem , vol.267 , pp. 6089-6098
    • Tamburrini, M.1    Riccio, A.2    Romano, M.3    Giardina, B.4    Di Prisco, G.5
  • 69
    • 0034828648 scopus 로고    scopus 로고
    • The hemoglobin system of the brown moray Gymnothorax unicolor: Structure/function relationships
    • Tamburrini, M., Verde, C., Olianas, A. et al. 2001. The hemoglobin system of the brown moray Gymnothorax unicolor: structure/function relationships. Eur J Biochem 268, 4104-4111.
    • (2001) Eur J Biochem , vol.268 , pp. 4104-4111
    • Tamburrini, M.1    Verde, C.2    Olianas, A.3
  • 70
    • 0030596491 scopus 로고    scopus 로고
    • The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms
    • Tame, J.R., Wilson, J.C. & Weber, R.E. 1996. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. J Mol Biol 259, 749-760.
    • (1996) J Mol Biol , vol.259 , pp. 749-760
    • Tame, J.R.1    Wilson, J.C.2    Weber, R.E.3
  • 71
    • 0015804663 scopus 로고
    • The effect of inositol hexaphosphate on the allosteric properties of carp hemoglobin
    • Tan, A.L. & Noble, R.W. 1973. The effect of inositol hexaphosphate on the allosteric properties of carp hemoglobin. J Biol Chem 248, 7412-7416.
    • (1973) J Biol Chem , vol.248 , pp. 7412-7416
    • Tan, A.L.1    Noble, R.W.2
  • 72
    • 0015217131 scopus 로고
    • Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant
    • Tomita, S. & Riggs, A. 1971. Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant. J Biol Chem 246, 547-554.
    • (1971) J Biol Chem , vol.246 , pp. 547-554
    • Tomita, S.1    Riggs, A.2
  • 73
    • 0014253759 scopus 로고
    • Respiratory physiology of house sparrows in relation to high-altitude flight
    • Tucker, V.A. 1968. Respiratory physiology of house sparrows in relation to high-altitude flight. J Exp Biol 48, 55-66.
    • (1968) J Exp Biol , vol.48 , pp. 55-66
    • Tucker, V.A.1
  • 74
    • 0034067349 scopus 로고    scopus 로고
    • Organic phosphates in the red blood cells of fish
    • Val, A.L. 2000. Organic phosphates in the red blood cells of fish. Comp Biochem Physiol A Mol Integr Physiol 125, 417-435.
    • (2000) Comp Biochem Physiol A Mol Integr Physiol , vol.125 , pp. 417-435
    • Val, A.L.1
  • 75
    • 0019311408 scopus 로고
    • Identification of the residues involved in the oxygen-linked chloride-ion binding sites in human deoxyhemoglobin and oxyhemoglobin
    • Van Beek, G.G. & De Bruin, S.H. 1980. Identification of the residues involved in the oxygen-linked chloride-ion binding sites in human deoxyhemoglobin and oxyhemoglobin. Eur J Biochem 105, 353-360.
    • (1980) Eur J Biochem , vol.105 , pp. 353-360
    • Van Beek, G.G.1    De Bruin, S.H.2
  • 76
    • 0018720275 scopus 로고
    • The binding of chloride ions to ligated and unligated human hemoglobin and its influence on the Bohr effect
    • Van Beek, G.G., Zuiderweg, E.R. & De Bruin, S.H. 1979. The binding of chloride ions to ligated and unligated human hemoglobin and its influence on the Bohr effect. Eur J Biochem 99, 379-383.
    • (1979) Eur J Biochem , vol.99 , pp. 379-383
    • Van Beek, G.G.1    Zuiderweg, E.R.2    De Bruin, S.H.3
  • 77
    • 0033823827 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic studies of bar-headed goose fluoromethaemoglobin with inositol hexaphosphate
    • Wang, H.C., Liang, Y.H., Zhu, J.P. & Lu, G.Y. 2000. Crystallization and preliminary crystallographic studies of bar-headed goose fluoromethaemoglobin with inositol hexaphosphate. Acta Crystallogr D Biol Crystallogr 56, 1183-1184.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 1183-1184
    • Wang, H.C.1    Liang, Y.H.2    Zhu, J.P.3    Lu, G.Y.4
  • 78
    • 0023866302 scopus 로고
    • Functional adaptations in hemoglobins from ectothermic vertebrates
    • Weber, R.E. & Jensen, F.B. 1988. Functional adaptations in hemoglobins from ectothermic vertebrates. Annu Rev Physiol 50, 161-179.
    • (1988) Annu Rev Physiol , vol.50 , pp. 161-179
    • Weber, R.E.1    Jensen, F.B.2
  • 79
    • 0022982116 scopus 로고
    • Oxygen binding in alligator blood related to temperature, diving, and 'alkaline tide'
    • Weber, R.E. & White, F.N. 1986. Oxygen binding in alligator blood related to temperature, diving, and 'alkaline tide'. Am J Physiol 251, R901-R908.
    • (1986) Am J Physiol , vol.251
    • Weber, R.E.1    White, F.N.2
  • 80
    • 0036839292 scopus 로고    scopus 로고
    • Novel mechanism for high-altitude adaptation in hemoglobin of the Andean frog Telmatobius peruvianus
    • Weber, R.E., Ostojic, H., Fago, A. et al. 2002. Novel mechanism for high-altitude adaptation in hemoglobin of the Andean frog Telmatobius peruvianus. Am J Physiol Regul Integr Comp Physiol 283, R1052-R1060.
    • (2002) Am J Physiol Regul Integr Comp Physiol , vol.283
    • Weber, R.E.1    Ostojic, H.2    Fago, A.3
  • 81
    • 0014280659 scopus 로고
    • Regulation in macromolecules as illustrated by hemoglobin
    • Wyman, J. 1968. Regulation in macromolecules as illustrated by hemoglobin. Q Rev Biopbys 1, 35-80.
    • (1968) Q Rev Biopbys , vol.1 , pp. 35-80
    • Wyman, J.1
  • 82
    • 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. et al. 2004. Novel mechanisms of pH sensitivity in Tuna hemoglobin: a structural explanation of the Root effect. J Biol Chem 279, 28632-28640.
    • (2004) J Biol Chem , vol.279 , pp. 28632-28640
    • Yokoyama, T.1    Chong, K.T.2    Miyazaki, G.3


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