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Volumn 389, Issue 2, 2005, Pages 497-505

Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis

Author keywords

Autoxidation rate; Body wall myoglobin; Haem distal residue pair; Ophelia bicornis; Oxygen binding; Polychaete annelid

Indexed keywords

ABSORPTION; AMINO ACIDS; DNA; OXIDATION; RATE CONSTANTS;

EID: 22544467448     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050267     Document Type: Article
Times cited : (5)

References (60)
  • 1
    • 0014949443 scopus 로고
    • The function of coelomic cell hemoglobin in the polychaete Glycera dibranchiata
    • Hoffmann, R. J. and Mangum, C. P. (1970) The function of coelomic cell hemoglobin in the polychaete Glycera dibranchiata. Comp. Biochem. Physiol. 36, 211-228
    • (1970) Comp. Biochem. Physiol. , vol.36 , pp. 211-228
    • Hoffmann, R.J.1    Mangum, C.P.2
  • 2
    • 0018830742 scopus 로고
    • Characterization of the hemoglobins and myoglobin of Travisia foetida
    • Terwilliger, R. C., Garlick, R. L. and Terwilliger, N. B. (1980) Characterization of the hemoglobins and myoglobin of Travisia foetida. Comp. Biochem. Physiol. 66B, 261-266
    • (1980) Comp. Biochem. Physiol. , vol.66 B , pp. 261-266
    • Terwilliger, R.C.1    Garlick, R.L.2    Terwilliger, N.B.3
  • 3
    • 0015263189 scopus 로고
    • Molecular and functional heterogeneity in myoglobin from the polychaete Arenicola marina L
    • Weber, R. E. and Pauptit, E. (1972) Molecular and functional heterogeneity in myoglobin from the polychaete Arenicola marina L. Arch. Biochem. Biophys. 148, 322-324
    • (1972) Arch. Biochem. Biophys. , vol.148 , pp. 322-324
    • Weber, R.E.1    Pauptit, E.2
  • 4
    • 0017249269 scopus 로고
    • Hemoglobins of Glycera robusta: Structures of coelomic cell hemoglobin and body wall myoglobin
    • Terwilliger, R. C., Garlick, R. L. and Terwilliger, N. B. (1976) Hemoglobins of Glycera robusta: structures of coelomic cell hemoglobin and body wall myoglobin. Comp. Biochem. Physiol. 54B, 149-153
    • (1976) Comp. Biochem. Physiol. , vol.54 B , pp. 149-153
    • Terwilliger, R.C.1    Garlick, R.L.2    Terwilliger, N.B.3
  • 6
    • 0025875126 scopus 로고
    • Primary structure of myohemerythrin from the annelid Nereis diversicolor
    • Takagi, T. and Cox, J. A. (1991) Primary structure of myohemerythrin from the annelid Nereis diversicolor. FEBS Lett. 285, 25-27
    • (1991) FEBS Lett. , vol.285 , pp. 25-27
    • Takagi, T.1    Cox, J.A.2
  • 7
    • 0016167416 scopus 로고
    • Oxygenational properties of haemerythrin in the blood of Magelona papillicornis Muller (Polychaeta: Magelonidae)
    • Wells, R. M. and Dales, R. P. (1974) Oxygenational properties of haemerythrin in the blood of Magelona papillicornis Muller (Polychaeta: Magelonidae). Comp. Biochem Physiol. 49A, 57-64
    • (1974) Comp. Biochem Physiol. , vol.49 A , pp. 57-64
    • Wells, R.M.1    Dales, R.P.2
  • 9
    • 0000954752 scopus 로고
    • Studies on chlorocruorin. I. The oxygen equilibrium of Spirographis chlorocruorin
    • Antonini, E., Rossi-Fanelli, A. and Caputo, A. (1962) Studies on chlorocruorin. I. The oxygen equilibrium of Spirographis chlorocruorin. Arch. Biochem. Biophys. 97, 336-342
    • (1962) Arch. Biochem. Biophys. , vol.97 , pp. 336-342
    • Antonini, E.1    Rossi-Fanelli, A.2    Caputo, A.3
  • 10
    • 0005434197 scopus 로고
    • The respiratory pigment of the serpulid polychaete, Serpula vermicularis L: Structure of its chlorocruorin and hemoglobin (erythrocruorin)
    • Terwilliger, R. C. (1978) The respiratory pigment of the serpulid polychaete, Serpula vermicularis L: structure of its chlorocruorin and hemoglobin (erythrocruorin). Comp. Biochem. Physiol. 61B, 463-469
    • (1978) Comp. Biochem. Physiol. , vol.61 B , pp. 463-469
    • Terwilliger, R.C.1
  • 11
    • 0041647718 scopus 로고
    • A contribution to the knowledge of haemoglobin
    • Lankester, E. R. (1872) A contribution to the knowledge of haemoglobin. Proc. R. Soc. London Ser. B 21, 70-80
    • (1872) Proc. R. Soc. London Ser. B , vol.21 , pp. 70-80
    • Lankester, E.R.1
  • 12
    • 0017388869 scopus 로고
    • Structure and oxygen equilibrium of hemoglobin and myoglobin from the pacific lugworm Abarenicola pacifica
    • Garlick, R. L. and Terwilliger, R. C. (1977) Structure and oxygen equilibrium of hemoglobin and myoglobin from the pacific lugworm Abarenicola pacifica. Comp. Biochem. Physiol. 57B, 177-184
    • (1977) Comp. Biochem. Physiol. , vol.57 B , pp. 177-184
    • Garlick, R.L.1    Terwilliger, R.C.2
  • 13
    • 22544445653 scopus 로고
    • Chlorocruorin and haemoglobin
    • Fox, H. M. (1947) Chlorocruorin and haemoglobin. Nature (London) 160, 825
    • (1947) Nature (London) , vol.160 , pp. 825
    • Fox, H.M.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli, L. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, L.K.1
  • 17
    • 22544453680 scopus 로고
    • Pure native globin from human hemoglobin: Preparation and some physico-chemical properties
    • Rossi-Fanelli, A., Antonini, E. and Caputo, A. (1958) Pure native globin from human hemoglobin: preparation and some physico-chemical properties. Biochim. Biophys. Acta 28, 221
    • (1958) Biochim. Biophys. Acta , vol.28 , pp. 221
    • Rossi-Fanelli, A.1    Antonini, E.2    Caputo, A.3
  • 18
    • 0032010153 scopus 로고    scopus 로고
    • A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
    • Zhang, Z. and Marshall, A. G. (1998) A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 9, 225-233
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 225-233
    • Zhang, Z.1    Marshall, A.G.2
  • 19
    • 0019751816 scopus 로고
    • Measurement of binding of gaseous and nongaseous ligands to hemoglobin by conventional spectrophotometric procedures
    • Giardina, B. and Amiconi, G. (1981) Measurement of binding of gaseous and nongaseous ligands to hemoglobin by conventional spectrophotometric procedures. Methods Enzymol. 76, 417-427
    • (1981) Methods Enzymol. , vol.76 , pp. 417-427
    • Giardina, B.1    Amiconi, G.2
  • 20
    • 0018117288 scopus 로고
    • Membrane-covered thin layer optical cell for gas-reaction studies of hemoglobin
    • Dolman, D. and Gill, S. J. (1978) Membrane-covered thin layer optical cell for gas-reaction studies of hemoglobin. Anal. Biochem. 87, 127-134
    • (1978) Anal. Biochem. , vol.87 , pp. 127-134
    • Dolman, D.1    Gill, S.J.2
  • 21
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, J. (1964) Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19, 223-286
    • (1964) Adv. Protein Chem. , vol.19 , pp. 223-286
    • Wyman, J.1
  • 23
    • 0030027631 scopus 로고    scopus 로고
    • Globins in nonvertebrate species: Dispersal by horizontal gene transfer and evolution of the structure-function relationships
    • Moens, L., Vanfleteren, J., Van de Peer, Y., Kapp, O., Czeluzniak, J., Goodman, M., Blaxter, M. and Vinogradov, S. (1996) Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships. Mol. Biol. Evol. 13, 324-333
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 324-333
    • Moens, L.1    Vanfleteren, J.2    Van De Peer, Y.3    Kapp, O.4    Czeluzniak, J.5    Goodman, M.6    Blaxter, M.7    Vinogradov, S.8
  • 24
    • 0023176681 scopus 로고
    • Determinants of a protein fold: Unique features of the globin amino acid sequences
    • Bashford, D., Chlothia, C. and Lesk, A. A. (1987) Determinants of a protein fold: unique features of the globin amino acid sequences. J. Mol. Biol. 196, 199-216
    • (1987) J. Mol. Biol. , vol.196 , pp. 199-216
    • Bashford, D.1    Chlothia, C.2    Lesk, A.A.3
  • 25
    • 0030056291 scopus 로고    scopus 로고
    • Aplysia limacina myoglobin cDNA cloning: An alternative mechanism of oxygen stabilization as studied by active-site mutagenesis
    • Cutruzzolà, F., Travaglini-Allocatelli, C., Brancaccio, A. and Brunori, M. (1996) Aplysia limacina myoglobin cDNA cloning: an alternative mechanism of oxygen stabilization as studied by active-site mutagenesis. Biochem. J. 314, 83-90
    • (1996) Biochem. J. , vol.314 , pp. 83-90
    • Cutruzzolà, F.1    Travaglini-Allocatelli, C.2    Brancaccio, A.3    Brunori, M.4
  • 26
    • 0017398707 scopus 로고
    • Cooperative, low-molecular-weight dimeric myoglobins from the radular muscle of the gastropod mollusc Nassa mutabilis L
    • Geraci, G., Sada, A. and Cirotto, C. (1977) Cooperative, low-molecular-weight dimeric myoglobins from the radular muscle of the gastropod mollusc Nassa mutabilis L. Eur. J. Biochem. 77, 555-560
    • (1977) Eur. J. Biochem. , vol.77 , pp. 555-560
    • Geraci, G.1    Sada, A.2    Cirotto, C.3
  • 27
    • 0014873826 scopus 로고
    • Studies on erythrocruorin. I. Physicochemical properties of earthworm erythrocruorin
    • Rossi Fanelli, M. R., Chiancone, E., Vecchini, P. and Antonini, E. (1970) Studies on erythrocruorin. I. Physicochemical properties of earthworm erythrocruorin. Arch. Biochem. Biophys. 141, 278-283
    • (1970) Arch. Biochem. Biophys. , vol.141 , pp. 278-283
    • Rossi Fanelli, M.R.1    Chiancone, E.2    Vecchini, P.3    Antonini, E.4
  • 28
    • 0024962496 scopus 로고
    • Spectral properties unique to the myoglobins lacking the usual distal histidine residue
    • Shikama, K. and Matsuoka, A. (1989) Spectral properties unique to the myoglobins lacking the usual distal histidine residue. J. Mol. Biol. 209, 489-491
    • (1989) J. Mol. Biol. , vol.209 , pp. 489-491
    • Shikama, K.1    Matsuoka, A.2
  • 29
    • 0034736304 scopus 로고    scopus 로고
    • A primitive myoglobin from Tetrahymena pyriformis: Its heme environment, autoxidizability, and genomic DNA structure
    • Korenaga, S., Igarashi, J., Matsuoka, A. and Shikama, K. (2000) A primitive myoglobin from Tetrahymena pyriformis: its heme environment, autoxidizability, and genomic DNA structure. Biochim. Biophys. Acta 1543, 131-145
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 131-145
    • Korenaga, S.1    Igarashi, J.2    Matsuoka, A.3    Shikama, K.4
  • 30
    • 0021099098 scopus 로고
    • Interaction of ligands with the distal glutamine in elephant myoglobin
    • Bartnicki, D. E., Mizukami, H. and Romero-Herrera, A. E. (1983) Interaction of ligands with the distal glutamine in elephant myoglobin. J. Biol. Chem. 258, 1599-1602
    • (1983) J. Biol. Chem. , vol.258 , pp. 1599-1602
    • Bartnicki, D.E.1    Mizukami, H.2    Romero-Herrera, A.E.3
  • 31
    • 0002331134 scopus 로고
    • The derivatives of ferric hemoglobin and myoglobin
    • (Neuberger, A. and Tatum, E. L., eds.), North-Holland Publishing, Amsterdam
    • Antonini, E. and Brunori, M. (1971) The derivatives of ferric hemoglobin and myoglobin. In Hemoglobin and Myoglobin in their Reactions with Ligands (Neuberger, A. and Tatum, E. L., eds.), pp. 40-54, North-Holland Publishing, Amsterdam
    • (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands , pp. 40-54
    • Antonini, E.1    Brunori, M.2
  • 32
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber, R. E. and Vinogradov, S. N. (2001) Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol. Rev. 81, 569-628
    • (2001) Physiol. Rev. , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 34
    • 50849148366 scopus 로고
    • Studies on the oxygen and carbon monoxide equilibria of human myoglobin
    • Rossi-Fanelli, A. and Antonini, E. (1958) Studies on the oxygen and carbon monoxide equilibria of human myoglobin. Arch. Biochem. Biophys. 77, 478-492
    • (1958) Arch. Biochem. Biophys. , vol.77 , pp. 478-492
    • Rossi-Fanelli, A.1    Antonini, E.2
  • 35
    • 4544387529 scopus 로고    scopus 로고
    • Morphological and genetic evidence supports the existence of two species in the genus Ophelia (Annelida, Polychaeta) from the Western Mediterranean
    • Maltagliati, F., Casu, M. and Castelli, A. (2004) Morphological and genetic evidence supports the existence of two species in the genus Ophelia (Annelida, Polychaeta) from the Western Mediterranean. Biol. J. Linn. Soc. 83, 101-113
    • (2004) Biol. J. Linn. Soc. , vol.83 , pp. 101-113
    • Maltagliati, F.1    Casu, M.2    Castelli, A.3
  • 39
    • 0019827532 scopus 로고
    • Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin
    • Phillips, S. E. and Schoenborn, B. P. (1981) Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature (London) 292, 81-82
    • (1981) Nature (London) , vol.292 , pp. 81-82
    • Phillips, S.E.1    Schoenborn, B.P.2
  • 40
    • 0032479053 scopus 로고    scopus 로고
    • The mini-hemoglobins in neural and body wall tissue of the nemertean worm Cerebratulus lacteus
    • Vandergon, T. L., Riggs, C. K., Gorr, T. A., Colacino, J. M. and Riggs, A. F. (1998) The mini-hemoglobins in neural and body wall tissue of the nemertean worm Cerebratulus lacteus. J. Biol. Chem. 273, 16998-17011
    • (1998) J. Biol. Chem. , vol.273 , pp. 16998-17011
    • Vandergon, T.L.1    Riggs, C.K.2    Gorr, T.A.3    Colacino, J.M.4    Riggs, A.F.5
  • 42
    • 0034673683 scopus 로고    scopus 로고
    • Isolation and cDNA-derived amino acid sequences of hemoglobin and myoglobin from the deep-sea clam Calyptogena kaikoi
    • Suzuki, T., Kawamichi, H., Ohtsuki, R., Iwai, M. and Fujikura, K. (2000) Isolation and cDNA-derived amino acid sequences of hemoglobin and myoglobin from the deep-sea clam Calyptogena kaikoi. Biochem. Biophys. Acta 1478, 152-158
    • (2000) Biochem. Biophys. Acta , vol.1478 , pp. 152-158
    • Suzuki, T.1    Kawamichi, H.2    Ohtsuki, R.3    Iwai, M.4    Fujikura, K.5
  • 43
    • 0022897256 scopus 로고
    • The hemoglobin of Urechis caupo: The cDNA-derived amino acid sequence
    • Garey, J. R. and Riggs, A. F. (1986) The hemoglobin of Urechis caupo: the cDNA-derived amino acid sequence. J. Biol. Chem. 261, 16446-16450
    • (1986) J. Biol. Chem. , vol.261 , pp. 16446-16450
    • Garey, J.R.1    Riggs, A.F.2
  • 44
    • 0024519403 scopus 로고
    • Discrimination between oxygen and carbon monoxide and inhibition of autoxidation by myoglobin
    • Springer, B. A., Egerberg, K. D., Sligar, S. G., Rohlfs, R. J., Mathews, A. J. and Olson, J. S. (1989) Discrimination between oxygen and carbon monoxide and inhibition of autoxidation by myoglobin. J. Biol. Chem. 264, 3057-3060
    • (1989) J. Biol. Chem. , vol.264 , pp. 3057-3060
    • Springer, B.A.1    Egerberg, K.D.2    Sligar, S.G.3    Rohlfs, R.J.4    Mathews, A.J.5    Olson, J.S.6
  • 45
    • 0027958149 scopus 로고
    • Formation of the two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin
    • De Baere, I., Perutz, M., Kiger, L., Marden, M. C. and Poyart, C. (1994) Formation of the two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 91, 1594-1597
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1594-1597
    • De Baere, I.1    Perutz, M.2    Kiger, L.3    Marden, M.C.4    Poyart, C.5
  • 51
    • 0032497416 scopus 로고    scopus 로고
    • African elephant myoglobin with an unusual autoxidation behaviour: Comparison with the H64Q mutant of sperm whale myoglobin
    • Tada, T., Watanabe, Y., Matsuoka, A., Ikeda-Saito, M., Imai, K., Ni-hei, Y. and Shikama, K. (1998) African elephant myoglobin with an unusual autoxidation behaviour: comparison with the H64Q mutant of sperm whale myoglobin. Biochim. Biophys. Acta 1387, 165-176
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 165-176
    • Tada, T.1    Watanabe, Y.2    Matsuoka, A.3    Ikeda-Saito, M.4    Imai, K.5    Ni-hei, Y.6    Shikama, K.7
  • 52
    • 0019348428 scopus 로고
    • An exceptional amino acid replacement on the distal side of the iron atom in proboscidean myoglobin
    • Romero-Herrera, A. E., Goodman, M., Dene, H., Bartnicki, D. E. and Mizukami, K. (1981) An exceptional amino acid replacement on the distal side of the iron atom in proboscidean myoglobin. J. Mol. Evol. 17, 140-147
    • (1981) J. Mol. Evol. , vol.17 , pp. 140-147
    • Romero-Herrera, A.E.1    Goodman, M.2    Dene, H.3    Bartnicki, D.E.4    Mizukami, K.5
  • 53
  • 54
    • 0000675667 scopus 로고
    • The oxidation of haemoglobin to methaemoglobin by oxygen. II. The relation between the rate of oxidation and the partial pressure of oxygen
    • Brooks, J. (1935) The oxidation of haemoglobin to methaemoglobin by oxygen. II. The relation between the rate of oxidation and the partial pressure of oxygen. Proc. R. Soc. London Ser. B 118, 560-577
    • (1935) Proc. R. Soc. London Ser. B , vol.118 , pp. 560-577
    • Brooks, J.1
  • 55
    • 0001388027 scopus 로고
    • Aplysia oxymyoglobin with an unusual stability property: Kinetic analysis of the pH dependence
    • Shikama, K. and Matsuoka, A. (1986) Aplysia oxymyoglobin with an unusual stability property: kinetic analysis of the pH dependence. Biochemistry 25, 3898-3903
    • (1986) Biochemistry , vol.25 , pp. 3898-3903
    • Shikama, K.1    Matsuoka, A.2
  • 56
    • 0023049205 scopus 로고
    • Amino acid sequence of myoglobin from the mollusc Dolabella auricularia
    • Suzuki, T. (1986) Amino acid sequence of myoglobin from the mollusc Dolabella auricularia. J. Biol. Chem. 261, 3692-3699
    • (1986) J. Biol. Chem. , vol.261 , pp. 3692-3699
    • Suzuki, T.1
  • 57
    • 0033775922 scopus 로고    scopus 로고
    • Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin
    • Suzuki, T., Watanabe, Y., Nagasawa, M., Matsuoka, A. and Shikama, K. (2000) Dual nature of the distal histidine residue in the autoxidation reaction of myoglobin and hemoglobin. Eur. J. Biochem. 267, 6166-6174
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6166-6174
    • Suzuki, T.1    Watanabe, Y.2    Nagasawa, M.3    Matsuoka, A.4    Shikama, K.5
  • 58
    • 0032478044 scopus 로고    scopus 로고
    • Primary structures of Arenicola marina isomyoglobins: Molecular basis for functional heterogeneity
    • Kleinschmidt, T. and Weber, R. E. (1998) Primary structures of Arenicola marina isomyoglobins: molecular basis for functional heterogeneity. Biochim. Biophys. Acta 1383, 55-62
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 55-62
    • Kleinschmidt, T.1    Weber, R.E.2
  • 60
    • 0023886498 scopus 로고
    • Mini-myoglobin: The structural significance of haem-ligand interactions
    • De Sanctis, G., Falcioni, G., Giardina, B., Ascoli, F. and Brunori, M. (1988) Mini-myoglobin: the structural significance of haem-ligand interactions. J. Mol. Biol. 200, 725-733
    • (1988) J. Mol. Biol. , vol.200 , pp. 725-733
    • De Sanctis, G.1    Falcioni, G.2    Giardina, B.3    Ascoli, F.4    Brunori, M.5


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