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Volumn 93, Issue 8, 2007, Pages 2822-2829

Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder notothenioidei

Author keywords

[No Author keywords available]

Indexed keywords

HEMOPROTEIN; METHEMOGLOBIN;

EID: 35348994296     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.105700     Document Type: Article
Times cited : (42)

References (42)
  • 1
    • 0001023291 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for myoglobin and hemoglobin: A venerable puzzle
    • Shikama, K. 1998. The molecular mechanism of autoxidation for myoglobin and hemoglobin: a venerable puzzle. Chem. Rev. 98:1357-1374.
    • (1998) Chem. Rev , vol.98 , pp. 1357-1374
    • Shikama, K.1
  • 2
    • 0035465476 scopus 로고    scopus 로고
    • Oxygen carriers ("blood substitutes") raison d'être, chemistry, and some physiology
    • Riess, J. 2001. Oxygen carriers ("blood substitutes") raison d'être, chemistry, and some physiology. Chem. Rev. 101:2797-2919.
    • (2001) Chem. Rev , vol.101 , pp. 2797-2919
    • Riess, J.1
  • 3
    • 0028364885 scopus 로고
    • Detection, formation, and relevance of hemichrome and hemochrome
    • Rifkind, J. M., O. Abugo, A. Levy, and J. M. Heim. 1994. Detection, formation, and relevance of hemichrome and hemochrome. Meth. Enzymol. 231:449-480.
    • (1994) Meth. Enzymol , vol.231 , pp. 449-480
    • Rifkind, J.M.1    Abugo, O.2    Levy, A.3    Heim, J.M.4
  • 6
    • 0015239545 scopus 로고
    • Stability of oxyhemoglobin A and its constituent chains and their derivatives
    • Rachmilewitz, E. A., J. Peisach, and W. E. Blumberg. 1971. Stability of oxyhemoglobin A and its constituent chains and their derivatives. J. Biol. Chem. 246:3356-3366.
    • (1971) J. Biol. Chem , vol.246 , pp. 3356-3366
    • Rachmilewitz, E.A.1    Peisach, J.2    Blumberg, W.E.3
  • 7
    • 0033061632 scopus 로고    scopus 로고
    • Molecular dynamics of human methemoglobin: The transmission of conformational information between subunits in an αβ dimer
    • Ramadas, N., and J. M. Rifkind. 1999. Molecular dynamics of human methemoglobin: the transmission of conformational information between subunits in an αβ dimer. Biophys. J. 76:1796-1811.
    • (1999) Biophys. J , vol.76 , pp. 1796-1811
    • Ramadas, N.1    Rifkind, J.M.2
  • 8
    • 0042324524 scopus 로고    scopus 로고
    • A pH-dependent aquo-met-to-hemichrome transition in crystalline horse methemoglobin
    • Robinson, V. L., B. B. Smith, and A. Arnone. 2003. A pH-dependent aquo-met-to-hemichrome transition in crystalline horse methemoglobin. Biochemistry. 42:10113-10125.
    • (2003) Biochemistry , vol.42 , pp. 10113-10125
    • Robinson, V.L.1    Smith, B.B.2    Arnone, A.3
  • 9
    • 17144408393 scopus 로고    scopus 로고
    • Structure-function relationships in the growing hexacoordinate hemoglobin sub-family
    • de Sanctis, D., A. Pesce, M. Nardini, M. Bolognesi, A. Bocedi, and P. Ascenzi. 2004. Structure-function relationships in the growing hexacoordinate hemoglobin sub-family. IUBMB Life. 56:643-651.
    • (2004) IUBMB Life , vol.56 , pp. 643-651
    • de Sanctis, D.1    Pesce, A.2    Nardini, M.3    Bolognesi, M.4    Bocedi, A.5    Ascenzi, P.6
  • 10
    • 17144382480 scopus 로고    scopus 로고
    • Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin
    • Pesce, A., D. De Sanctis, M. Nardini, S. Dewilde, L. Moens, T. Hankeln, T. Burmester, P. Ascenzi, and M. Bolognesi. 2004. Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. IUBMB Life. 56:657-664.
    • (2004) IUBMB Life , vol.56 , pp. 657-664
    • Pesce, A.1    De Sanctis, D.2    Nardini, M.3    Dewilde, S.4    Moens, L.5    Hankeln, T.6    Burmester, T.7    Ascenzi, P.8    Bolognesi, M.9
  • 11
    • 20444445134 scopus 로고    scopus 로고
    • Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem
    • Feng, L., S. Zhou, L. Gu, D. Gell, J. Mackay, M. Weiss, A. Gow, and Y. Shi. 2005. Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem. Nature. 435:697-701.
    • (2005) Nature , vol.435 , pp. 697-701
    • Feng, L.1    Zhou, S.2    Gu, L.3    Gell, D.4    Mackay, J.5    Weiss, M.6    Gow, A.7    Shi, Y.8
  • 12
    • 0026545367 scopus 로고
    • Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative
    • Camardella, L., C. Caruso, R. D'Avino, G. di Prisco, B. Rutigliano, M. Tamburrini, G. Fermi, and M. F. Perutz. 1992. Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. J. Mol. Biol. 224:449-460.
    • (1992) J. Mol. Biol , vol.224 , pp. 449-460
    • Camardella, L.1    Caruso, C.2    D'Avino, R.3    di Prisco, G.4    Rutigliano, B.5    Tamburrini, M.6    Fermi, G.7    Perutz, M.F.8
  • 14
    • 0026586178 scopus 로고    scopus 로고
    • Tamburini, M., A. Brancaccio, R. Ippoliti, and G. di Prisco. 1992. The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps. Arch. Biochem. Biophys. 292:295-302.
    • Tamburini, M., A. Brancaccio, R. Ippoliti, and G. di Prisco. 1992. The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps. Arch. Biochem. Biophys. 292:295-302.
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of x-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276:307-326.
    • (1997) Meth. Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 30144435515 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjedgaard. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. D. 56:714-721.
    • (1991) Acta Crystallogr. D , vol.56 , pp. 714-721
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjedgaard, M.4
  • 19
    • 0029146246 scopus 로고
    • Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola
    • Mitchell, D. T., G. B. Kitto, and M. L. Hackert. 1995. Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola. J. Mol. Biol. 251:421-431.
    • (1995) J. Mol. Biol , vol.251 , pp. 421-431
    • Mitchell, D.T.1    Kitto, G.B.2    Hackert, M.L.3
  • 22
    • 1942533441 scopus 로고    scopus 로고
    • The crystal structure of Synechocystis hemoglobin with a covalent heme linkage
    • Hoy, J. A., S. Kundu, J. T. Trent, S. Ramaswamy, and M. S. Hargrove. 2004. The crystal structure of Synechocystis hemoglobin with a covalent heme linkage. J. Biol. Chem. 279:16535-16542.
    • (2004) J. Biol. Chem , vol.279 , pp. 16535-16542
    • Hoy, J.A.1    Kundu, S.2    Trent, J.T.3    Ramaswamy, S.4    Hargrove, M.S.5
  • 26
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr. 1:760-763.
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr. 1:760-763.
  • 27
    • 0035800031 scopus 로고    scopus 로고
    • Factors determining the orientation of axially coordinated imidazoles in heme proteins
    • Zaric, S., D. Popovic, and E. Knapp. 2001. Factors determining the orientation of axially coordinated imidazoles in heme proteins. Biochemistry. 40:7914-7928.
    • (2001) Biochemistry , vol.40 , pp. 7914-7928
    • Zaric, S.1    Popovic, D.2    Knapp, E.3
  • 28
    • 0015239511 scopus 로고
    • The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance
    • Peisach, J., W. E. Blumberg, S. Ogawa, E. A. Rachmilewitz, and R. Oltzik. 1971. The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance. J. Biol. Chem. 246:3342-3355.
    • (1971) J. Biol. Chem , vol.246 , pp. 3342-3355
    • Peisach, J.1    Blumberg, W.E.2    Ogawa, S.3    Rachmilewitz, E.A.4    Oltzik, R.5
  • 31
    • 0027368854 scopus 로고
    • High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
    • Quillin, M., R. Arduini, J. Olson, and G. J. Phillips. 1993. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. Mol. Biol. 234:140-155.
    • (1993) J. Mol. Biol , vol.234 , pp. 140-155
    • Quillin, M.1    Arduini, R.2    Olson, J.3    Phillips, G.J.4
  • 32
    • 20444466524 scopus 로고    scopus 로고
    • Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: What have we learned?
    • Smulevich, G., A. Feis, and B. D. Howes. 2005. Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned? Acc. Chem. Res. 38:433-440.
    • (2005) Acc. Chem. Res , vol.38 , pp. 433-440
    • Smulevich, G.1    Feis, A.2    Howes, B.D.3
  • 33
    • 0037189541 scopus 로고    scopus 로고
    • The x-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket
    • Ilari, A., A. Bonamore, A. Farina, K. Johnson, and A. Boffi. 2002. The x-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket. J. Biol. Chem. 26:23725-23732.
    • (2002) J. Biol. Chem , vol.26 , pp. 23725-23732
    • Ilari, A.1    Bonamore, A.2    Farina, A.3    Johnson, K.4    Boffi, A.5
  • 34
    • 33749528323 scopus 로고    scopus 로고
    • Pentacoordinate and hexacoordinate ferric hemes in acid medium: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus
    • Marmo Moreira, L., A. Lima Poli, A. J. Costa-Filho, and H. Imasato. 2006. Pentacoordinate and hexacoordinate ferric hemes in acid medium: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus. Biophys. Chem. 124:62-72.
    • (2006) Biophys. Chem , vol.124 , pp. 62-72
    • Marmo Moreira, L.1    Lima Poli, A.2    Costa-Filho, A.J.3    Imasato, H.4
  • 35
    • 0028096564 scopus 로고
    • Structural characterization of oxidized dimeric Scapharca inaequivalvis hemoglobin by resonance Raman spectroscopy
    • Boffi, A., S. Takahashi, C. Spagnuolo, D. L. Rousseau, and E. Chiancone. 1994. Structural characterization of oxidized dimeric Scapharca inaequivalvis hemoglobin by resonance Raman spectroscopy. J. Biol. Chem. 269:20437-20440.
    • (1994) J. Biol. Chem , vol.269 , pp. 20437-20440
    • Boffi, A.1    Takahashi, S.2    Spagnuolo, C.3    Rousseau, D.L.4    Chiancone, E.5
  • 36
    • 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
    • Mazzarella, L., A. Vergara, L. Vitagliano, A. Merlino, G. Bonomi, S. Scala, C. Verde, and G. di Prisco. 2006. 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. 65:490-498.
    • (2006) Proteins , vol.65 , pp. 490-498
    • Mazzarella, L.1    Vergara, A.2    Vitagliano, L.3    Merlino, A.4    Bonomi, G.5    Scala, S.6    Verde, C.7    di Prisco, G.8
  • 37
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin A at 1.7-Å resolution
    • Silva, M. M., P. H. Rogers, and A. Arnone. 1992. A third quaternary structure of human hemoglobin A at 1.7-Å resolution. J. Biol. Chem. 267:17248-17256.
    • (1992) J. Biol. Chem , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 38
    • 33845470157 scopus 로고
    • Models of the cytochromes b. 5. EPR studies of low-spin iron(III) tetraphenylporphyrins
    • Walker, F. A., D. Reis, and V. L. Balke. 1984. Models of the cytochromes b. 5. EPR studies of low-spin iron(III) tetraphenylporphyrins. J. Am. Chem. Soc. 106:6888-6898.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 6888-6898
    • Walker, F.A.1    Reis, D.2    Balke, V.L.3
  • 40
    • 0035852972 scopus 로고    scopus 로고
    • Hemoglobin of the Antarctic fishes Trematomus bernacchii and Trematomus newnesi: Structural basis for the increased stability of the liganded tetramer relative to human hemoglobin
    • Giangiacomo, L., R. D'Avino, G. di Prisco, and E. Chiancone. 2001. Hemoglobin of the Antarctic fishes Trematomus bernacchii and Trematomus newnesi: structural basis for the increased stability of the liganded tetramer relative to human hemoglobin. Biochemistry. 40:3062-3068.
    • (2001) Biochemistry , vol.40 , pp. 3062-3068
    • Giangiacomo, L.1    D'Avino, R.2    di Prisco, G.3    Chiancone, E.4
  • 41
    • 30144436769 scopus 로고    scopus 로고
    • Minimal structural requirement of root effect: Crystal structure of the cathodic hemoglobin isolated from Trematomus newnesi
    • Mazzarella, L., G. Bonomi, M. C. Lubrano, A. Merlino, A. Vergara, L. Vitagliano, C. Verde, and G. di Prisco. 2006. Minimal structural requirement of root effect: crystal structure of the cathodic hemoglobin isolated from Trematomus newnesi. Proteins. 62:316-321.
    • (2006) Proteins , vol.62 , pp. 316-321
    • Mazzarella, L.1    Bonomi, G.2    Lubrano, M.C.3    Merlino, A.4    Vergara, A.5    Vitagliano, L.6    Verde, C.7    di Prisco, G.8
  • 42
    • 1842637797 scopus 로고    scopus 로고
    • Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin
    • Vinck, E., S. Van Doorslaer, S. Dewilde, and L. Moens. 2004. Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin. J. Am. Chem. Soc. 126:4516-4517.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 4516-4517
    • Vinck, E.1    Van Doorslaer, S.2    Dewilde, S.3    Moens, L.4


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