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Volumn 22, Issue 2-3, 2008, Pages 143-152

Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase

Author keywords

Antarctic fish; Hemicrome; Hemoglobins; Roman crystallography

Indexed keywords

ABSORPTION; CRYSTAL STRUCTURE; CRYSTALLINE MATERIALS; CRYSTALLOGRAPHY; CRYSTALS; HEMOGLOBIN; IRON; MAMMALS; PH; PH EFFECTS; POWDERS;

EID: 47849092863     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.3233/SPE-2008-0332     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0032921026 scopus 로고    scopus 로고
    • Is cooperative oxygen binding by hemoglobin really understood?
    • W.A. Eaton, E.R. Henry, J. Hofrichter and A. Mozzarelli, Is cooperative oxygen binding by hemoglobin really understood?, Nat. Struct. Biol. 6(4) (1999), 351-358.
    • (1999) Nat. Struct. Biol , vol.6 , Issue.4 , pp. 351-358
    • Eaton, W.A.1    Henry, E.R.2    Hofrichter, J.3    Mozzarelli, A.4
  • 2
    • 33645127489 scopus 로고    scopus 로고
    • The allosteric properties of hemoglobin: Insights from natural and site directed mutants
    • A. Bellelli, M. Brunori, A.E. Miele, G. Panetta and B. Vallone, The allosteric properties of hemoglobin: insights from natural and site directed mutants, Curr. Protein Pept. Sci. 7(1) (2006), 17-45.
    • (2006) Curr. Protein Pept. Sci , vol.7 , Issue.1 , pp. 17-45
    • Bellelli, A.1    Brunori, M.2    Miele, A.E.3    Panetta, G.4    Vallone, B.5
  • 3
    • 0141717848 scopus 로고    scopus 로고
    • The global allostery model of hemoglobin: An allosteric mechanism involving homotropic and heterotropic interactions
    • T. Yonetani and A. Tsuneshige, The global allostery model of hemoglobin: an allosteric mechanism involving homotropic and heterotropic interactions, C. R. Biol. 326(6) (2003), 523-532.
    • (2003) C. R. Biol , vol.326 , Issue.6 , pp. 523-532
    • Yonetani, T.1    Tsuneshige, A.2
  • 4
    • 0031033020 scopus 로고    scopus 로고
    • D. Barrick, N.T. Ho, V. Simplaceanu, F.W. Dahlquist and C. Ho, A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin, Nat. Struct. Biol. 4(1) (1997), 78-83.
    • D. Barrick, N.T. Ho, V. Simplaceanu, F.W. Dahlquist and C. Ho, A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin, Nat. Struct. Biol. 4(1) (1997), 78-83.
  • 6
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • M.F. Perutz, Stereochemistry of cooperative effects in haemoglobin, Nature 228(273) (1970), 726-739.
    • (1970) Nature , vol.228 , Issue.273 , pp. 726-739
    • Perutz, M.F.1
  • 7
    • 20444417111 scopus 로고    scopus 로고
    • The enigma of the liganded hemoglobin end state: A novel quaternary structure of human carbonmonoxy hemoglobin
    • M.K. Safo and D.J. Abraham, The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin, Biochemistry 44(23) (2005), 8347-8359.
    • (2005) Biochemistry , vol.44 , Issue.23 , pp. 8347-8359
    • Safo, M.K.1    Abraham, D.J.2
  • 8
    • 0033214516 scopus 로고    scopus 로고
    • What is the true structure of liganded haemoglobin?
    • J.R. Tame, What is the true structure of liganded haemoglobin?, Trends Biochem. Sci. 24(10) (1999), 372-377.
    • (1999) Trends Biochem. Sci , vol.24 , Issue.10 , pp. 372-377
    • Tame, J.R.1
  • 9
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin A at 1.7-A resolution
    • M.M. Silva, P.H. Rogers and A. Arnone, A third quaternary structure of human hemoglobin A at 1.7-A resolution, J. Biol. Chem. 267(24) (1992), 17248-17256.
    • (1992) J. Biol. Chem , vol.267 , Issue.24 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 10
    • 0027988868 scopus 로고
    • The T-to-R transformation in hemoglobin: A reevaluation
    • R. Srinivasan and G.D. Rose, The T-to-R transformation in hemoglobin: a reevaluation, Proc. Natl. Acad. Sci. USA 91(23) (1994), 11113-11117.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.23 , pp. 11113-11117
    • Srinivasan, R.1    Rose, G.D.2
  • 11
    • 0032540854 scopus 로고    scopus 로고
    • Crystal structure of a human embryonic haemoglobin: The carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution
    • A.J. Sutherland-Smith, H.M. Baker, O.M. Hofmann, T. Brittain and E.N. Baker, Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution, J. Mol. Biol. 280(3) (1998), 475-484.
    • (1998) J. Mol. Biol , vol.280 , Issue.3 , pp. 475-484
    • Sutherland-Smith, A.J.1    Baker, H.M.2    Hofmann, O.M.3    Brittain, T.4    Baker, E.N.5
  • 12
    • 0035006227 scopus 로고    scopus 로고
    • The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 Å resolution and its relationship to the quaternary structures of other hemoglobin crystal forms
    • M.K. Safo and D.J. Abraham, The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 Å resolution and its relationship to the quaternary structures of other hemoglobin crystal forms, Protein Sci. 10(6) (2001), 1091-1099.
    • (2001) Protein Sci , vol.10 , Issue.6 , pp. 1091-1099
    • Safo, M.K.1    Abraham, D.J.2
  • 13
    • 0034687668 scopus 로고    scopus 로고
    • Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin
    • T.C. Mueser, P.H. Rogers and A. Arnone, Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin, Biochemistry 39(50) (2000), 15353-15364.
    • (2000) Biochemistry , vol.39 , Issue.50 , pp. 15353-15364
    • Mueser, T.C.1    Rogers, P.H.2    Arnone, A.3
  • 15
    • 0033574669 scopus 로고    scopus 로고
    • Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question
    • L. Mazzarella, R. D'Avino, G. di Prisco et al., Crystal structure of Trematomus newnesi hemoglobin re-opens the Root effect question, J. Mol. Biol. 287(5) (1999), 897-906.
    • (1999) J. Mol. Biol , vol.287 , Issue.5 , pp. 897-906
    • Mazzarella, L.1    D'Avino, R.2    di Prisco, G.3
  • 16
    • 33748996221 scopus 로고    scopus 로고
    • High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the Root effect
    • L. Mazzarella, A. Vergara, L. Vitagliano et al., High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: the role of histidine residues in modulating the strength of the Root effect, Proteins Struct. Funct. Bioinf. 65 (2006), 490-498.
    • (2006) Proteins Struct. Funct. Bioinf , vol.65 , pp. 490-498
    • Mazzarella, L.1    Vergara, A.2    Vitagliano, L.3
  • 17
    • 30144436769 scopus 로고    scopus 로고
    • L. Mazzarella, G. Bonomi, M.C. Lubrano et al., Minimal structural requirement of Root effect: crystal structure of the cathodic hemoglobin isolated from Trematomus newnesi, Proteins Struct. Funct. Bioinf. 62(2) (2006), 316-321.
    • L. Mazzarella, G. Bonomi, M.C. Lubrano et al., Minimal structural requirement of Root effect: crystal structure of the cathodic hemoglobin isolated from Trematomus newnesi, Proteins Struct. Funct. Bioinf. 62(2) (2006), 316-321.
  • 20
    • 35348994296 scopus 로고    scopus 로고
    • Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder Notothenioidei
    • A. Vergara, M. Franzese, A. Merlino et al., Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder Notothenioidei, Biophys. J. 93 (2007), 2822-2829.
    • (2007) Biophys. J , vol.93 , pp. 2822-2829
    • Vergara, A.1    Franzese, M.2    Merlino, A.3
  • 21
    • 36749064392 scopus 로고    scopus 로고
    • Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus, Gene
    • 1,2
    • D. Giordano, A. Vergara, H.C. Lee et al., Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus, Gene 406(1,2) (2007), 48-58.
    • (2007) , vol.406 , pp. 48-58
    • Giordano, D.1    Vergara, A.2    Lee, H.C.3
  • 22
    • 4644346825 scopus 로고    scopus 로고
    • Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes
    • C. Verde, B.D. Howes, M.C. de Rosa et al., Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes, Prot. Sci. 13(10) (2004), 2766-2781.
    • (2004) Prot. Sci , vol.13 , Issue.10 , pp. 2766-2781
    • Verde, C.1    Howes, B.D.2    de Rosa, M.C.3
  • 23
    • 42949162118 scopus 로고    scopus 로고
    • Spectroscopic and crystallographic characterization of hemichromes in tetrameric hemoglobins
    • A. Vergara, L. Vitagliano, G. di Prisco, C. Verde and L. Mazzarella, Spectroscopic and crystallographic characterization of hemichromes in tetrameric hemoglobins, Meth. Enz. 436A (2008), 421-440.
    • (2008) Meth. Enz , vol.436 A , pp. 421-440
    • Vergara, A.1    Vitagliano, L.2    di Prisco, G.3    Verde, C.4    Mazzarella, L.5
  • 25
    • 0037178126 scopus 로고    scopus 로고
    • Trehalose glass-facilitated thermal reduction of metmyoglobin and methemoglobin
    • A. Ray, B.A. Friedman and J.M. Friedman, Trehalose glass-facilitated thermal reduction of metmyoglobin and methemoglobin, J. Am. Chem. Soc. 124(25) (2002), 7270-7271.
    • (2002) J. Am. Chem. Soc , vol.124 , Issue.25 , pp. 7270-7271
    • Ray, A.1    Friedman, B.A.2    Friedman, J.M.3
  • 26
    • 0035824117 scopus 로고    scopus 로고
    • Acetylphenylhydrazine induced haemoglobin oxidation in erythrocytes studied by Mossbauer spectroscopy
    • S. Croci, G. Pedrazzi, G. Passeri, P. Piccolo and I. Ortalli, Acetylphenylhydrazine induced haemoglobin oxidation in erythrocytes studied by Mossbauer spectroscopy, Biochim. Biophys. Acta 1568(1) (2001), 99-104.
    • (2001) Biochim. Biophys. Acta , vol.1568 , Issue.1 , pp. 99-104
    • Croci, S.1    Pedrazzi, G.2    Passeri, G.3    Piccolo, P.4    Ortalli, I.5
  • 27
    • 0028364885 scopus 로고
    • Detection, formation, and relevance of hemichrome and hemochrome
    • J.M. Rifkind, O. Abugo, A. Levy and J.M. Heim, Detection, formation, and relevance of hemichrome and hemochrome, Meth. Enz. 231 (1994), 449-480.
    • (1994) Meth. Enz , vol.231 , pp. 449-480
    • Rifkind, J.M.1    Abugo, O.2    Levy, A.3    Heim, J.M.4
  • 28
    • 17144408393 scopus 로고    scopus 로고
    • Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
    • D. de Sanctis, A. Pesce, M. Nardini, M. Bolognesi, A. Bocedi and P. Ascenzi, Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family, IUBMB Life 56(11/12) (2004), 643-651.
    • (2004) IUBMB Life , vol.56 , Issue.11-12 , pp. 643-651
    • de Sanctis, D.1    Pesce, A.2    Nardini, M.3    Bolognesi, M.4    Bocedi, A.5    Ascenzi, P.6
  • 29
    • 17144382480 scopus 로고    scopus 로고
    • Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin
    • A. Pesce, D. De Sanctis, M. Nardini et al., Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin, IUBMB Life 56(11/12) (2004), 657-664.
    • (2004) IUBMB Life , vol.56 , Issue.11-12 , pp. 657-664
    • Pesce, A.1    De Sanctis, D.2    Nardini, M.3
  • 30
    • 33846013259 scopus 로고    scopus 로고
    • Sugar-derived glasses support thermal and photo-initiated electron transfer processes over macroscopic distances
    • M. Navati and J.M. Friedman, Sugar-derived glasses support thermal and photo-initiated electron transfer processes over macroscopic distances, J. Biol. Chem. 281 (2006), 36021-36028.
    • (2006) J. Biol. Chem , vol.281 , pp. 36021-36028
    • Navati, M.1    Friedman, J.M.2
  • 31
    • 0026545367 scopus 로고
    • Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative
    • L. Camardella, C. Caruso, R. D'Avino et al., Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative, J. Mol. Biol. 224 (1992), 449-460.
    • (1992) J. Mol. Biol , vol.224 , pp. 449-460
    • Camardella, L.1    Caruso, C.2    D'Avino, R.3
  • 32
    • 3543012707 scopus 로고    scopus 로고
    • A new software suite for macromolecular structure determination
    • Crystallography & NMR system
    • A.T. Brunger, P.D. Adams, G.M. Clore et al., Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr. D - Biol. Crystallogr. 54 (1998), 905-921.
    • (1998) Acta Crystallogr. D - Biol. Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3
  • 33
    • 30144435515 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan and M. Kjedgaard, Improved methods for binding protein models in electron density maps and the location of errors in these models, Acta Crystallogr. D - Biol. Crystallogr. 56 (1991), 714-721.
    • (1991) Acta Crystallogr. D - Biol. Crystallogr , vol.56 , pp. 714-721
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjedgaard, M.4
  • 34
    • 33646727439 scopus 로고    scopus 로고
    • Raman crystallography and other biochemical applications of Raman microscopy
    • P.R. Carey, Raman crystallography and other biochemical applications of Raman microscopy, Annu. Rev. Phys. Chem. 57 (2006), 527-554.
    • (2006) Annu. Rev. Phys. Chem , vol.57 , pp. 527-554
    • Carey, P.R.1
  • 35
    • 2842546487 scopus 로고
    • Structural correlation and vinyl influences in resonance Raman spectra of protoheme complexes and protein
    • S. Choi, T.G. Spiro, K.C. Langry, K.M. Smith, D.L. Budd and G.N. La Mar, Structural correlation and vinyl influences in resonance Raman spectra of protoheme complexes and protein, J. Am. Chem. Soc. 104 (1982), 4345-4351.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langry, K.C.3    Smith, K.M.4    Budd, D.L.5    La Mar, G.N.6
  • 36
    • 0003969504 scopus 로고
    • A. Lever and H. Gray, eds, Addison-Wesley, Reading, MA
    • T.G. Spiro, Iron Porphyrins, Vol. II, A. Lever and H. Gray, eds, Addison-Wesley, Reading, MA, 1983.
    • (1983) Iron Porphyrins , vol.2
    • Spiro, T.G.1
  • 37
    • 0027497088 scopus 로고
    • Single-crystal micro-Raman spectroscopy
    • G. Smulevich and T.G. Spiro, Single-crystal micro-Raman spectroscopy, Meth. Enzymol. 226 (1993), 397-408.
    • (1993) Meth. Enzymol , vol.226 , pp. 397-408
    • Smulevich, G.1    Spiro, T.G.2
  • 38
    • 0033548078 scopus 로고    scopus 로고
    • The heme environment in barley hemoglobin
    • T.K. Das, H.C. Lee, S.M.G. Duff et al., The heme environment in barley hemoglobin, J. Biol. Chem. 274(7) (1999), 4207-4212.
    • (1999) J. Biol. Chem , vol.274 , Issue.7 , pp. 4207-4212
    • Das, T.K.1    Lee, H.C.2    Duff, S.M.G.3
  • 39
    • 0033548681 scopus 로고    scopus 로고
    • Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands
    • M. Couture, T.K. Das, H.C. Lee et al., Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands, J. Biol. Chem. 274(11) (1999), 6898-6910.
    • (1999) J. Biol. Chem , vol.274 , Issue.11 , pp. 6898-6910
    • Couture, M.1    Das, T.K.2    Lee, H.C.3
  • 40
    • 0022966966 scopus 로고
    • Resonance Raman charcaterization of the 7-ns photoproduct of (carbomonoxy)hemoglobin: Implication for hemoglobin dynamics
    • S. Dasgupta and T.G. Spiro, Resonance Raman charcaterization of the 7-ns photoproduct of (carbomonoxy)hemoglobin: implication for hemoglobin dynamics, Biochemistry 25 (1986), 5941-5948.
    • (1986) Biochemistry , vol.25 , pp. 5941-5948
    • Dasgupta, S.1    Spiro, T.G.2


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