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Volumn 2, Issue 1, 2009, Pages 67-73

Hemoproteins in the cold

Author keywords

Bacterium; Cold adaptation; Fish; Hemoglobin; Hexacoordination; Neuroglobin

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 67349271018     PISSN: 18747787     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.margen.2009.03.004     Document Type: Review
Times cited : (3)

References (76)
  • 1
    • 0035929255 scopus 로고    scopus 로고
    • Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis
    • Awenius C., Hanken T., and Burmester T. Neuroglobins from the zebrafish Danio rerio and the pufferfish Tetraodon nigroviridis. Biochem. Biophys. Res. Commun. 287 (2001) 418-421
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 418-421
    • Awenius, C.1    Hanken, T.2    Burmester, T.3
  • 2
    • 34249031561 scopus 로고    scopus 로고
    • Neuroglobin, seven years after
    • Brunori M., and Vallone B. Neuroglobin, seven years after. Cell. Mol. Life Sci. 64 (2007) 1259-1268
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1259-1268
    • Brunori, M.1    Vallone, B.2
  • 4
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • Burmester T., Weich B., Reinhardt S., and Hankeln T. A vertebrate globin expressed in the brain. Nature 407 (2000) 520-523
    • (2000) Nature , vol.407 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 5
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T., Ebner B., Weich B., and Hankeln T. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol. Biol. Evol. 19 (2002) 416-421
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 7
    • 63449084083 scopus 로고    scopus 로고
    • The "icefish paradox". Which is the task of neuroglobin in Antarctic hemoglobin-less icefish?
    • Cheng C.H., di Prisco G., and Verde C. The "icefish paradox". Which is the task of neuroglobin in Antarctic hemoglobin-less icefish?. IUBMB Life 61 (2009) 184-188
    • (2009) IUBMB Life , vol.61 , pp. 184-188
    • Cheng, C.H.1    di Prisco, G.2    Verde, C.3
  • 14
    • 0001294439 scopus 로고
    • A study of hemoglobin in Antarctic fishes: purification and characterization of hemoglobins from four species
    • di Prisco G. A study of hemoglobin in Antarctic fishes: purification and characterization of hemoglobins from four species. Comp. Biochem. Physiol. B 90B (1988) 631-637
    • (1988) Comp. Biochem. Physiol. B , vol.90 B , pp. 631-637
    • di Prisco, G.1
  • 15
    • 34447504390 scopus 로고    scopus 로고
    • Biogeography and adaptation of Notothenioid fish: hemoglobin function and globin-gene evolution
    • di Prisco G., Eastman J.T., Giordano D., Parisi E., and Verde C. Biogeography and adaptation of Notothenioid fish: hemoglobin function and globin-gene evolution. Gene 398 (2007) 143-155
    • (2007) Gene , vol.398 , pp. 143-155
    • di Prisco, G.1    Eastman, J.T.2    Giordano, D.3    Parisi, E.4    Verde, C.5
  • 17
    • 0037073478 scopus 로고    scopus 로고
    • The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state
    • Falzone C.J., Christie Vu B., Scott N.L., and Lecomte J.T. The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state. J. Mol. Biol. 324 (2002) 1015-1029
    • (2002) J. Mol. Biol. , vol.324 , pp. 1015-1029
    • Falzone, C.J.1    Christie Vu, B.2    Scott, N.L.3    Lecomte, J.T.4
  • 18
    • 20444445134 scopus 로고    scopus 로고
    • Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for heme
    • Feng L., Zhou S., Gu L., Gell D., Mackay J., Weiss M., Gow A., and Shi Y. Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for heme. Nature 435 (2005) 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
  • 24
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: evolution of different patterns of gene expression
    • Hardison R. Hemoglobins from bacteria to man: evolution of different patterns of gene expression. J. Exp. Biol. 201 (1998) 1099-1117
    • (1998) J. Exp. Biol. , vol.201 , pp. 1099-1117
    • Hardison, R.1
  • 26
    • 33747790905 scopus 로고    scopus 로고
    • The oxygenation of the atmosphere and oceans
    • Holland H.D. The oxygenation of the atmosphere and oceans. Philos. Trans. R. Soc. B361 (2006) 903-916
    • (2006) Philos. Trans. R. Soc. , vol.B361 , pp. 903-916
    • Holland, H.D.1
  • 27
    • 1942533441 scopus 로고    scopus 로고
    • The crystal structure of Synechocystis hemoglobin with a covalent heme linkage
    • Hoy J.A., Kundu S., Trent III J.T., Ramaswamy S., and Hargrove M.S. The crystal structure of Synechocystis hemoglobin with a covalent heme linkage. J. Biol. Chem. 279 (2004) 16535-16542
    • (2004) J. Biol. Chem. , vol.279 , pp. 16535-16542
    • Hoy, J.A.1    Kundu, S.2    Trent III, J.T.3    Ramaswamy, S.4    Hargrove, M.S.5
  • 28
    • 0001266102 scopus 로고
    • A three-dimensional model of the myoglobin molecule obtained by X-ray analysis
    • Kendrew J.C., Bodo G., Dintzis H.M., Parrish R.G., Wyckoff H., and Phillips D.C. A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181 (1958) 662-666
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3    Parrish, R.G.4    Wyckoff, H.5    Phillips, D.C.6
  • 33
    • 47849092863 scopus 로고    scopus 로고
    • Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase
    • Merlino A., Verde C., di Prisco G., Mazzarella L., and Vergara A. Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase. Spectroscopy: Biomed. Appl. 22 2-3 (2008) 143-152
    • (2008) Spectroscopy: Biomed. Appl. , vol.22 , Issue.2-3 , pp. 143-152
    • Merlino, A.1    Verde, C.2    di Prisco, G.3    Mazzarella, L.4    Vergara, A.5
  • 36
    • 0029146246 scopus 로고
    • Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola
    • Mitchell D.T., Kitto G.B., and Hackert M.L. Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola. J. Mol. Biol. 251 (1995) 421-431
    • (1995) J. Mol. Biol. , vol.251 , pp. 421-431
    • Mitchell, D.T.1    Kitto, G.B.2    Hackert, M.L.3
  • 37
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and 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
  • 38
    • 34447530237 scopus 로고    scopus 로고
    • Protein fold and structure in the truncated (2/2) globin family
    • Nardini M., Pesce A., Milani M., and Bolognesi M. Protein fold and structure in the truncated (2/2) globin family. Gene 398 (2007) 2-11
    • (2007) Gene , vol.398 , pp. 2-11
    • Nardini, M.1    Pesce, A.2    Milani, M.3    Bolognesi, M.4
  • 39
    • 0021004799 scopus 로고
    • Species adaptation in a protein molecule
    • Perutz M.F. Species adaptation in a protein molecule. Mol. Biol. Evol. 1 (1983) 1-28
    • (1983) Mol. Biol. Evol. , vol.1 , pp. 1-28
    • Perutz, M.F.1
  • 40
    • 85021467943 scopus 로고
    • Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence
    • Perutz M.F., Kendrew J.C., and Watson H.C. Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence. J. Mol. Biol. 13 (1965) 669-678
    • (1965) J. Mol. Biol. , vol.13 , pp. 669-678
    • Perutz, M.F.1    Kendrew, J.C.2    Watson, H.C.3
  • 42
  • 45
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • Poole R.K. Nitric oxide and nitrosative stress tolerance in bacteria. Biochem. Soc. Trans. 33 (2005) 176-180
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 176-180
    • Poole, R.K.1
  • 48
    • 0028364885 scopus 로고
    • Detection, formation, and relevance of hemichrome and hemochrome
    • Rifkind J.M., Abugo O., Levy A., and Heim J.M. Detection, formation, and relevance of hemichrome and hemochrome. Methods Enzymol. 231 (1994) 449-480
    • (1994) Methods Enzymol. , vol.231 , pp. 449-480
    • Rifkind, J.M.1    Abugo, O.2    Levy, A.3    Heim, J.M.4
  • 49
    • 0042324524 scopus 로고    scopus 로고
    • A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin
    • Robinson V.L., Smith B.B., and Arnone A. A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin. Biochemistry 42 (2003) 10113-10125
    • (2003) Biochemistry , vol.42 , pp. 10113-10125
    • Robinson, V.L.1    Smith, B.B.2    Arnone, A.3
  • 50
    • 10344243985 scopus 로고    scopus 로고
    • A globin gene of ancient evolutionary origin in lower vertebrates: evidence for two distinct globin families in animals
    • Roesner A., Fuchs C., Hankeln T., and Burmester T. A globin gene of ancient evolutionary origin in lower vertebrates: evidence for two distinct globin families in animals. Mol. Biol. Evol. 22 (2005) 12-20
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 12-20
    • Roesner, A.1    Fuchs, C.2    Hankeln, T.3    Burmester, T.4
  • 51
    • 0001063415 scopus 로고
    • Vertebrates without erythrocytes and blood pigment
    • Ruud J.T. Vertebrates without erythrocytes and blood pigment. Nature 173 (1954) 848-850
    • (1954) Nature , vol.173 , pp. 848-850
    • Ruud, J.T.1
  • 52
    • 0037018935 scopus 로고    scopus 로고
    • Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein
    • Scott N.L., Falzone C.J., Vuletich D.A., Zhao J., Bryant D.A., and Lecomte J.T. Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein. Biochemistry 41 (2002) 6902-6910
    • (2002) Biochemistry , vol.41 , pp. 6902-6910
    • Scott, N.L.1    Falzone, C.J.2    Vuletich, D.A.3    Zhao, J.4    Bryant, D.A.5    Lecomte, J.T.6
  • 53
    • 33745651826 scopus 로고    scopus 로고
    • When bad things happen to good fish: the loss of hemoglobin and myoglobin expression in Antarctic icefishes
    • Sidell B.D., and O'Brien K.M. When bad things happen to good fish: the loss of hemoglobin and myoglobin expression in Antarctic icefishes. J. Exp. Biol. 209 (2006) 1791-1802
    • (2006) J. Exp. Biol. , vol.209 , pp. 1791-1802
    • Sidell, B.D.1    O'Brien, K.M.2
  • 54
    • 44349180793 scopus 로고    scopus 로고
    • NO dioxygenase activity in hemoglobins is ubiquitos in vitro, but limited by reduction in vivo
    • Smagghe B.J., Trent III J.T., and Hargrove M.S. NO dioxygenase activity in hemoglobins is ubiquitos in vitro, but limited by reduction in vivo. PloS ONE 3 (2008) e2039
    • (2008) PloS ONE , vol.3
    • Smagghe, B.J.1    Trent III, J.T.2    Hargrove, M.S.3
  • 56
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is upregulated by and protects neurons from hypoxic-ischemic injury
    • Sun Y., Jin K., Mao X.O., Zhu Y., and Greenberg D.A. Neuroglobin is upregulated by and protects neurons from hypoxic-ischemic injury. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 15306-15311
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, Y.4    Greenberg, D.A.5
  • 58
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate haemoglobin
    • Trent III J.T., and Hargrove M.S. A ubiquitously expressed human hexacoordinate haemoglobin. J. Biol. Chem. 277 (2002) 19538-19545
    • (2002) J. Biol. Chem. , vol.277 , pp. 19538-19545
    • Trent III, J.T.1    Hargrove, M.S.2
  • 60
    • 10644251786 scopus 로고    scopus 로고
    • The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity
    • Vallone B., Nienhaus K., Matthes A., Brunori M., and Nienhaus G.U. The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 17351-17356
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17351-17356
    • Vallone, B.1    Nienhaus, K.2    Matthes, A.3    Brunori, M.4    Nienhaus, G.U.5
  • 61
    • 33845206135 scopus 로고    scopus 로고
    • The evolution of thermal adaptation in polar fish
    • Verde C., Parisi E., and di Prisco G. The evolution of thermal adaptation in polar fish. Gene 385 (2006) 137-145
    • (2006) Gene , vol.385 , pp. 137-145
    • Verde, C.1    Parisi, E.2    di Prisco, G.3
  • 62
    • 65549097257 scopus 로고    scopus 로고
    • The hemoglobins of fishes living at polar latitudes - current knowledge on structural adaptations in a changing environment
    • Verde C., Vergara A., Mazzarella L., and di Prisco G. The hemoglobins of fishes living at polar latitudes - current knowledge on structural adaptations in a changing environment. Curr. Protein Pept. Sci. 9 (2008) 578-590
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 578-590
    • Verde, C.1    Vergara, A.2    Mazzarella, L.3    di Prisco, G.4
  • 64
    • 42949162118 scopus 로고    scopus 로고
    • Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins
    • Vergara A., Vitagliano L., Verde C., di Prisco G., and Mazzarella L. Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins. Methods Enzymol. 436 (2008) 425-444
    • (2008) Methods Enzymol. , vol.436 , pp. 425-444
    • Vergara, A.1    Vitagliano, L.2    Verde, C.3    di Prisco, G.4    Mazzarella, L.5
  • 65
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: enzymatic, transport, storage, and sensing
    • Vinogradov S., and Moens L. Diversity of globin function: enzymatic, transport, storage, and sensing. J. Biol. Chem. 283 (2008) 8773-8777
    • (2008) J. Biol. Chem. , vol.283 , pp. 8773-8777
    • Vinogradov, S.1    Moens, L.2
  • 69
    • 49449107745 scopus 로고    scopus 로고
    • Spectroscopic and crystallographic analysis of a tetrameric hemoglobin oxidation pathway reveals features of an intermediate R/T state
    • Vitagliano L., Vergara A., Bonomi G., Merlino A., Smulevich G., Howes B., di Prisco G., Verde C., and Mazzarella L. Spectroscopic and crystallographic analysis of a tetrameric hemoglobin oxidation pathway reveals features of an intermediate R/T state. J. Am. Chem. Soc. 130 (2008) 10527-10535
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10527-10535
    • Vitagliano, L.1    Vergara, A.2    Bonomi, G.3    Merlino, A.4    Smulevich, G.5    Howes, B.6    di Prisco, G.7    Verde, C.8    Mazzarella, L.9
  • 70
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich D.A., and Lecomte J.T. A phylogenetic and structural analysis of truncated hemoglobins. J. Mol. Evol. 62 (2006) 196-210
    • (2006) J. Mol. Evol. , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.2
  • 71
    • 0036915028 scopus 로고    scopus 로고
    • Hemoglobin, from microorganisms to man: a single structural motif, multiple functions
    • (Article in French)
    • Wajcman H., and Kiger L. Hemoglobin, from microorganisms to man: a single structural motif, multiple functions. C. R. Biol. 325 (2002) 1159-1174 (Article in French)
    • (2002) C. R. Biol. , vol.325 , pp. 1159-1174
    • Wajcman, H.1    Kiger, L.2
  • 72
    • 0141704224 scopus 로고    scopus 로고
    • Oxidized human neuroglobin acts as a heterotrimeric Gα protein guanine nucleotide dissociation inhibitor
    • Wakasugi K., Nakano T., and Morishima I. Oxidized human neuroglobin acts as a heterotrimeric Gα protein guanine nucleotide dissociation inhibitor. J. Biol. Chem. 278 (2003) 36505-36512
    • (2003) J. Biol. Chem. , vol.278 , pp. 36505-36512
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 73
    • 43249104256 scopus 로고    scopus 로고
    • Zebrafish neuroglobin is a cell-membrane-penetrating globin
    • Watanabe S., and Wakasugi K. Zebrafish neuroglobin is a cell-membrane-penetrating globin. Biochemistry 47 (2008) 5266-5270
    • (2008) Biochemistry , vol.47 , pp. 5266-5270
    • Watanabe, S.1    Wakasugi, K.2
  • 75
    • 4644261106 scopus 로고    scopus 로고
    • Bis-Histidyl Hexacoordination in hemoglobins facilitates heme reduction kinetics
    • Weiland T.R., Kundu S., Trent III J.T., Hoy J.A., and Hargrove M.S. Bis-Histidyl Hexacoordination in hemoglobins facilitates heme reduction kinetics. J. Am. Chem. Soc. 126 (2004) 11930-11935
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 11930-11935
    • Weiland, T.R.1    Kundu, S.2    Trent III, J.T.3    Hoy, J.A.4    Hargrove, M.S.5
  • 76
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg J.B., Bolognesi M., Wittenberg B.A., and Guertin M. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 277 (2002) 871-874
    • (2002) J. Biol. Chem. , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4


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