메뉴 건너뛰기




Volumn 19, Issue 9, 2002, Pages 1421-1433

Evolution of the sulfide-binding function within the globin multigenic family of the deep-sea hydrothermal vent tubeworm Riftia pachyptila

Author keywords

Duplication; H2S; Hexagonal bilayer hemoglobin; Riftia pachyptila; Selection; Sulfide binding domain

Indexed keywords

COMPLEMENTARY DNA; GLOBIN; HEMOGLOBIN; HEXAGONAL BILAYER HEMOGLOBIN; HYDROGEN SULFIDE; OXYGEN; SULFIDE; UNCLASSIFIED DRUG; CYSTEINE; MESSENGER RNA; SEA WATER;

EID: 0036728906     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.molbev.a004205     Document Type: Article
Times cited : (42)

References (82)
  • 1
    • 0000692741 scopus 로고
    • The sulfide-binding protein in the blood of the vestimentiferan tube-worm Riftia pachyptila, is the extracellular hemoglobin
    • ARP, A. J., J. J. CHILDRESS, and R. D. VETTER. 1987. The sulfide-binding protein in the blood of the vestimentiferan tube-worm Riftia pachyptila, is the extracellular hemoglobin. J. Exp. Biol. 128:139-158.
    • (1987) J. Exp. Biol. , vol.128 , pp. 139-158
    • Arp, A.J.1    Childress, J.J.2    Vetter, R.D.3
  • 2
    • 21844500666 scopus 로고
    • Multiple mechanisms provide tolerance to environmental sulfide in Urechis caupo
    • ARP, A. J., J. G. MENON, and D. JULIAN. 1995. Multiple mechanisms provide tolerance to environmental sulfide in Urechis caupo. Am. Zool. 35:132-144.
    • (1995) Am. Zool. , vol.35 , pp. 132-144
    • Arp, A.J.1    Menon, J.G.2    Julian, D.3
  • 3
    • 0022225471 scopus 로고
    • A fossil hydrothermal worm assemblage from the Tynagh lead-zinc deposit in Ireland
    • BANKS, D. A. 1985. A fossil hydrothermal worm assemblage from the Tynagh lead-zinc deposit in Ireland. Nature 313:128-131.
    • (1985) Nature , vol.313 , pp. 128-131
    • Banks, D.A.1
  • 5
    • 0019888148 scopus 로고
    • Exons and the structure, function and evolution of haemoglobin
    • BLAKE, C. C. 1981. Exons and the structure, function and evolution of haemoglobin. Nature 291:616.
    • (1981) Nature , vol.291 , pp. 616
    • Blake, C.C.1
  • 7
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • CASTRESANA, J. 2000. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol. Biol. Evol. 17:540-552.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 540-552
    • Castresana, J.1
  • 8
    • 0036920345 scopus 로고    scopus 로고
    • Sibling species of eastern Pacific hydrothermal-vent worms (Ampharetidae, Alvinellidae, Vestimentifera) provide new mitochondrial COI clock calibration
    • in press
    • CHEVALDONNÉ, P., D. JOLLIVET, D. DESBRUYERES, R. D. LUTZ, and R. C. VRIJENHOEK. 2002. Sibling species of eastern Pacific hydrothermal-vent worms (Ampharetidae, Alvinellidae, Vestimentifera) provide new mitochondrial COI clock calibration. Cah. Biol. Mar. (in press).
    • (2002) Cah. Biol. Mar.
    • Chevaldonné, P.1    Jollivet, D.2    Desbruyeres, D.3    Lutz, R.D.4    Vrijenhoek, R.C.5
  • 9
    • 0027068701 scopus 로고
    • The biology of hydrothermal vent animals: Physiology, biochemistry and autotrophic symbioses
    • CHILDRESS, J. J., and C. R. FISCHER. 1992. The biology of hydrothermal vent animals: physiology, biochemistry and autotrophic symbioses. Oceanogr. Mar. Biol. Annu. Rev. 30:337-441.
    • (1992) Oceanogr. Mar. Biol. Annu. Rev. , vol.30 , pp. 337-441
    • Childress, J.J.1    Fischer, C.R.2
  • 10
    • 0031595785 scopus 로고    scopus 로고
    • Comments on the role of H2S in the chemistry of Earth's early atmosphere and in prebiotic synthesis
    • CLARK, P. D., N. I. DOWLING, and M. HUANG. 1998. Comments on the role of H2S in the chemistry of Earth's early atmosphere and in prebiotic synthesis. J. Mol. Evol. 47:127-132.
    • (1998) J. Mol. Evol. , vol.47 , pp. 127-132
    • Clark, P.D.1    Dowling, N.I.2    Huang, M.3
  • 11
    • 0019732878 scopus 로고
    • 2 binding properties of the product of the central exon of beta-globin gene
    • 2 binding properties of the product of the central exon of beta-globin gene. Nature 291:87-90.
    • (1981) Nature , vol.291 , pp. 87-90
    • Craik, C.S.1    Buchman, S.R.2    Beychok, S.3
  • 12
    • 0000228203 scopus 로고
    • A model of evolutionary change in protein
    • M. O. Dayhoff, ed. National Biomedical Research Foundation, Washington, D.C.
    • DAYHOFF, M. O., R. M. SCHWARTZ, and B. C. ORCUTT. 1978. A model of evolutionary change in protein. Pp. 354-352 in M. O. DAYHOFF, ed. Atlas of protein sequence structure, Vol. 5., Suppl. 3. National Biomedical Research Foundation, Washington, D.C.
    • (1978) Atlas of Protein Sequence Structure , vol.5 , Issue.SUPPL. 3 , pp. 354-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 14
    • 0032085452 scopus 로고    scopus 로고
    • Duplicate genes and the root of angiosperms, with an example using phytochrome sequences
    • DONOGHUE, M. J., and S. MATHEWS. 1998. Duplicate genes and the root of angiosperms, with an example using phytochrome sequences. Mol. Phylogenet. Evol. 9:489-500.
    • (1998) Mol. Phylogenet. Evol. , vol.9 , pp. 489-500
    • Donoghue, M.J.1    Mathews, S.2
  • 15
    • 0014860857 scopus 로고
    • An improved method for determining codon variability in a gene and its application to the rate of fixation of mutations in evolution
    • FITCH, W. M., and E. MARKOWITZ. 1970. An improved method for determining codon variability in a gene and its application to the rate of fixation of mutations in evolution. Biochem. Genet. 4:579-593.
    • (1970) Biochem. Genet. , vol.4 , pp. 579-593
    • Fitch, W.M.1    Markowitz, E.2
  • 16
    • 0024287775 scopus 로고
    • The amino acid sequences of chains a, band c that form the trimer subunit of the extracellular hemoglobin from Lumbricus terrestris terrestris
    • FUSHITANI, K., M. S. MATSUURA, and A. F. RIGGS. 1988. The amino acid sequences of chains a, band c that form the trimer subunit of the extracellular hemoglobin from Lumbricus terrestris terrestris. J. Biol. Chem. 263:6502-6517.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6502-6517
    • Fushitani, K.1    Matsuura, M.S.2    Riggs, A.F.3
  • 17
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny
    • GALTIER, N., M. GOUY, and C. GAUTIER. 1996. SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny. Comput. Appl. Biosci. 12:543-548.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 18
    • 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
  • 19
    • 0019860994 scopus 로고
    • Correlation of DNA exonic regions with protein structural units in haemoglobin
    • Go, M. 1981. Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature 291:90-92.
    • (1981) Nature , vol.291 , pp. 90-92
    • Go, M.1
  • 20
    • 0015244632 scopus 로고
    • Molecular evolution in the descent of man
    • GOODMAN, M., J. BARNABAS, G. MATSUDA, and G. W. MOORE. 1971. Molecular evolution in the descent of man. Nature 233:604-613.
    • (1971) Nature , vol.233 , pp. 604-613
    • Goodman, M.1    Barnabas, J.2    Matsuda, G.3    Moore, G.W.4
  • 21
    • 0016436505 scopus 로고
    • Darwinian evolution in the genealogy of hemoglobin
    • GOODMAN, M., G. W. MOORE, and G. MATSUDA. 1975. Darwinian evolution in the genealogy of hemoglobin. Nature 253:603-608.
    • (1975) Nature , vol.253 , pp. 603-608
    • Goodman, M.1    Moore, G.W.2    Matsuda, G.3
  • 24
    • 0022180868 scopus 로고
    • Amino acid composition and the evolutionary rates of protein-coding genes
    • GRAUR, D. 1985. Amino acid composition and the evolutionary rates of protein-coding genes. J. Mol. Evol. 22:53-62.
    • (1985) J. Mol. Evol. , vol.22 , pp. 53-62
    • Graur, D.1
  • 25
    • 0031942895 scopus 로고    scopus 로고
    • Animal adaptations for tolerance and exploitation of poisonous sulfide
    • GRIESHABER, M. K., and S. VOLKEL. 1998. Animal adaptations for tolerance and exploitation of poisonous sulfide. Annu. Rev. Physiol. 60:33-53.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 33-53
    • Grieshaber, M.K.1    Volkel, S.2
  • 26
    • 0034052855 scopus 로고    scopus 로고
    • Sulfide detoxification in Hediste diversicolor and Marenzelleria viridis, two dominant polychaete worms within the shallow coastal waters of the southern Baltic Sea
    • HAHLBECK, E., C. ARNDT, and D. SCHIEDEK. 2000. Sulfide detoxification in Hediste diversicolor and Marenzelleria viridis, two dominant polychaete worms within the shallow coastal waters of the southern Baltic Sea. Comp. Biochem. Physiol. B 125:457-471.
    • (2000) Comp. Biochem. Physiol. B , vol.125 , pp. 457-471
    • Hahlbeck, E.1    Arndt, C.2    Schiedek, D.3
  • 27
    • 0032462723 scopus 로고    scopus 로고
    • Evolutionary origins and age of vestimentiferan tubeworms
    • HALANYCH, K. M., R. A. LUTZ, and R. C. VRIJENHOEK. 1998. Evolutionary origins and age of vestimentiferan tubeworms. Cah. Biol. Mar. 39:355-358.
    • (1998) Cah. Biol. Mar. , vol.39 , pp. 355-358
    • Halanych, K.M.1    Lutz, R.A.2    Vrijenhoek, R.C.3
  • 28
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • HARDISON, R. 1998. Hemoglobins from bacteria to man: evolution of different patterns of gene expression. J. Exp. Biol. 201:1099-1117.
    • (1998) J. Exp. Biol. , vol.201 , pp. 1099-1117
    • Hardison, R.1
  • 29
    • 0021619724 scopus 로고
    • Fossils of hydrothermal vent worms from cretaceous sulfide ores of the Samail Ophiolites, Oman
    • HAYMON, R. M., R. A. KOSKI, and C. SINCLAIR. 1984. Fossils of hydrothermal vent worms from cretaceous sulfide ores of the Samail Ophiolites, Oman. Science 223:1407-1409.
    • (1984) Science , vol.223 , pp. 1407-1409
    • Haymon, R.M.1    Koski, R.A.2    Sinclair, C.3
  • 30
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • HILL, R. E., and N. D. HASTIE. 1987. Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature 326:96-99.
    • (1987) Nature , vol.326 , pp. 96-99
    • Hill, R.E.1    Hastie, N.D.2
  • 31
    • 0006378890 scopus 로고
    • Gene volution and the haemoglobin
    • INGRAM, V. 1961. Gene volution and the haemoglobin. Nature 189:704-708.
    • (1961) Nature , vol.189 , pp. 704-708
    • Ingram, V.1
  • 32
    • 0024358140 scopus 로고
    • Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes
    • IWABE, N., K. KUMA, M. HASEGAWA, S. OSAWA, and T MIYATA. 1989. Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc. Natl. Acad. Sci. USA 86:9355-9359.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9355-9359
    • Iwabe, N.1    Kuma, K.2    Hasegawa, M.3    Osawa, S.4    Miyata, T.5
  • 33
    • 0024287524 scopus 로고
    • Exonintron organization in genes of earthworm and vertebrate globins
    • JHIANG, M. S., J. R. GAREY, and A. F. RIGGS. 1988. Exonintron organization in genes of earthworm and vertebrate globins. Science 240:334-336.
    • (1988) Science , vol.240 , pp. 334-336
    • Jhiang, M.S.1    Garey, J.R.2    Riggs, A.F.3
  • 34
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • JONES, D. T., W. R. TAYLOR, and J. M. TXORNTON. 1992. The rapid generation of mutation data matrices from protein sequences. CABIOS 8:275-282.
    • (1992) CABIOS , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Txornton, J.M.3
  • 35
    • 0001308009 scopus 로고
    • Riftia pachyptila Jones: Observations on the vestimentiferan worm from the Galapagos Rift
    • JONES, M. L. 1981. Riftia pachyptila Jones: observations on the vestimentiferan worm from the Galapagos Rift. Science 213:333-336.
    • (1981) Science , vol.213 , pp. 333-336
    • Jones, M.L.1
  • 36
    • 0028843842 scopus 로고
    • Alignment of 700 globin sequences: Extent of amino acid substitution and its correlation with variation in volume
    • KAPP, O. H., L. MOENS, J. VANFLETEREN, C. N. A. TROTMAN, T. SUZUKI, and S. N. VINOGRADOV. 1995. Alignment of 700 globin sequences: extent of amino acid substitution and its correlation with variation in volume. Protein Sci. 4:2179-2190.
    • (1995) Protein Sci. , vol.4 , pp. 2179-2190
    • Kapp, O.H.1    Moens, L.2    Vanfleteren, J.3    Trotman, C.N.A.4    Suzuki, T.5    Vinogradov, S.N.6
  • 38
    • 0019446947 scopus 로고
    • Was globin evolution very rapid in its early stages? A dubious case against the rate-constancy hypothesis
    • KIMURA, M. 1981. Was globin evolution very rapid in its early stages? A dubious case against the rate-constancy hypothesis. J. Mol. Evol. 17:110-113.
    • (1981) J. Mol. Evol. , vol.17 , pp. 110-113
    • Kimura, M.1
  • 39
    • 0032953625 scopus 로고    scopus 로고
    • Accelerated evolution and molecular surface of venom phospholipase A2 enzymes
    • KINI, R. M., and Y. M. CHAN. 1999. Accelerated evolution and molecular surface of venom phospholipase A2 enzymes. J. Mol. Evol. 48:125-132.
    • (1999) J. Mol. Evol. , vol.48 , pp. 125-132
    • Kini, R.M.1    Chan, Y.M.2
  • 41
    • 0033676221 scopus 로고    scopus 로고
    • Molecular phylogeny of the Annelida
    • MCHUGH, D. 2000. Molecular phylogeny of the Annelida. Can. J. Zool. 78:1873-1884.
    • (2000) Can. J. Zool. , vol.78 , pp. 1873-1884
    • Mchugh, D.1
  • 42
    • 0028922906 scopus 로고
    • Testing the covarion hypothesis of molecular evolution
    • MIYAMOTO, M. M., and W. M. FITC. 1995. Testing the covarion hypothesis of molecular evolution. Mol. Biol. Evol. 12:503-513.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 503-513
    • Miyamoto, M.M.1    Fitc, W.M.2
  • 44
    • 0032540246 scopus 로고    scopus 로고
    • Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata
    • NGUYEN, B. D., X. ZHAO, K. VYAS, G. N. LA MAR, R. A. LILE, E. A. BRUCKER, G. N. PHILLIPS JR., J. S. OLSON, J. B. WITTENBERG. 1998. Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata. J. Biol. Chem. 273(16):9517-9526.
    • (1998) J. Biol. Chem. , vol.273 , Issue.16 , pp. 9517-9526
    • Nguyen, B.D.1    Zhao, X.2    Vyas, K.3    La Mar, G.N.4    Lile, R.A.5    Brucker, E.A.6    Phillips G.N., Jr.7    Olson, J.S.8    Wittenberg, J.B.9
  • 45
    • 0016742498 scopus 로고
    • The effect of sulfide on cytochrome aa3. Isosteric and allosteric shifts of the reduced alpha-peak
    • NICHOLLS, P. 1975. The effect of sulfide on cytochrome aa3. Isosteric and allosteric shifts of the reduced alpha-peak. Biochim. Biophys. Acta 396:24-35.
    • (1975) Biochim. Biophys. Acta , vol.396 , pp. 24-35
    • Nicholls, P.1
  • 46
    • 0034731009 scopus 로고    scopus 로고
    • Mechanisms of molecular evolution
    • OHTA, T. 2000. Mechanisms of molecular evolution. Philos. Trans. R. Soc. Lond. B 355:1623-1626.
    • (2000) Philos. Trans. R. Soc. Lond. B , vol.355 , pp. 1623-1626
    • Ohta, T.1
  • 49
    • 0038221110 scopus 로고
    • Amino-acid composition of human crystallized myoglobin and haemoglobin
    • ROSSI-FANELLI, A., D. CAVALLINI, and C. DE MARCO. 1955. Amino-acid composition of human crystallized myoglobin and haemoglobin. Nature 17:377-381.
    • (1955) Nature , vol.17 , pp. 377-381
    • Rossi-Fanelli, A.1    Cavallini, D.2    De Marco, C.3
  • 50
    • 0035535003 scopus 로고    scopus 로고
    • A cladistic analysis of Siboglinidae Caullrey, 1914 (Polychaeta, Annelida): Formerly the phyla Pogonophora and Vestimentifera
    • ROUSE, G. W. 2001. A cladistic analysis of Siboglinidae Caullrey, 1914 (Polychaeta, Annelida): formerly the phyla Pogonophora and Vestimentifera. Zool. J. Linn. Soc. 132:55-80.
    • (2001) Zool. J. Linn. Soc. , vol.132 , pp. 55-80
    • Rouse, G.W.1
  • 51
    • 18844450291 scopus 로고
    • The articulation of annelids
    • ROUSE, G. W., and K. FAUCHALD. 1995. The articulation of annelids. Zool. Scripta 24:269-301.
    • (1995) Zool. Scripta , vol.24 , pp. 269-301
    • Rouse, G.W.1    Fauchald, K.2
  • 52
    • 0031284707 scopus 로고    scopus 로고
    • Cladistics and polychaetes
    • -. 1997. Cladistics and polychaetes. Zool. Scripta 26:139-204.
    • (1997) Zool. Scripta , vol.26 , pp. 139-204
  • 53
    • 0015927177 scopus 로고
    • Generation time and genomic evolution in primates
    • SARICH, V. M., and A. C. WILSON. 1973. Generation time and genomic evolution in primates. Science 179:1144-1147.
    • (1973) Science , vol.179 , pp. 1144-1147
    • Sarich, V.M.1    Wilson, A.C.2
  • 54
    • 0023644671 scopus 로고
    • Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris terrestris
    • SHISHIKURA, F., J. W. SNOW, T GOTOH, S. M. VINOGRADOV, and D. A. WALTZ. 1987. Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris terrestris. J. Biol. Chem. 262:3123-3131.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3123-3131
    • Shishikura, F.1    Snow, J.W.2    Gotoh, T.3    Vinogradov, S.M.4    Waltz, D.A.5
  • 55
    • 0029836454 scopus 로고    scopus 로고
    • Quartet Puzzling: A quartet maximum-likelihood method for reconstructing tree topologies
    • STRIMMER, K., and A. VON HAESELER. 1996. Quartet Puzzling: a quartet maximum-likelihood method for reconstructing tree topologies. Mol. Biol. Evol. 13:964-969.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 56
    • 0022982174 scopus 로고
    • The complete amino acid sequence of giant multisubunit hemoglobin from the polychaete Tylorrhynchus heterochaetus
    • SUZUKI, T, and T GOTOH. 1986. The complete amino acid sequence of giant multisubunit hemoglobin from the polychaete Tylorrhynchus heterochaetus. J. Biol. Chem. 261:9257-9267.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9257-9267
    • Suzuki, T.1    Gotoh, T.2
  • 57
    • 0028811397 scopus 로고
    • Primary structure of a constituent polypeptide chain of the chlorocruorin from Sabellastarte indica
    • SUZUKI, T., Y. HIRAO, and S. N. VINOGRADOV. 1995. Primary structure of a constituent polypeptide chain of the chlorocruorin from Sabellastarte indica. Biochim. Biophys. Acta 1252:189-193.
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 189-193
    • Suzuki, T.1    Hirao, Y.2    Vinogradov, S.N.3
  • 58
    • 0031689710 scopus 로고    scopus 로고
    • Evolution of myoglobin
    • SUZUKI, T, and K. IMAI. 1998. Evolution of myoglobin. Cell Mol. Life Sci. 54:979-1004.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 979-1004
    • Suzuki, T.1    Imai, K.2
  • 59
    • 0025174729 scopus 로고
    • Primary structure of a constituent polypeptide chain (AIII) of the giant haemoglobin from the deep-sea tube worm Lamellibrachiasp. A possible H2S-binding site
    • SUZUKI, T., T. TAKAGI, and S. OHTA. 1990. Primary structure of a constituent polypeptide chain (AIII) of the giant haemoglobin from the deep-sea tube worm Lamellibrachiasp. A possible H2S-binding site. Biochem. J. 266:221-225.
    • (1990) Biochem. J. , vol.266 , pp. 221-225
    • Suzuki, T.1    Takagi, T.2    Ohta, S.3
  • 60
    • 0027549041 scopus 로고
    • N-terminal amino acid sequence of 440 kDa haemoglobins of deep-sea tube worms, Lamellibrachia sp. 1, Lamellibrachia sp.2 and slender vestimentifera gen.sp. 1. Evolutionary relationship with annelid hemoglobins
    • -. 1993. N-terminal amino acid sequence of 440 kDa haemoglobins of deep-sea tube worms, Lamellibrachia sp. 1, Lamellibrachia sp.2 and slender vestimentifera gen.sp. 1. Evolutionary relationship with annelid hemoglobins. Zool. Sci. 10:141-146.
    • (1993) Zool. Sci. , vol.10 , pp. 141-146
  • 61
    • 0000574480 scopus 로고
    • The deep-sea tube worm hemoglobin: Subunit structure and phylogenetic relationship with annelid hemoglobin
    • SUZUKI, T., T. TAKAGI, K. OKUDA, T. FURUKOHRI, and S. OHTA. 1989. The deep-sea tube worm hemoglobin: subunit structure and phylogenetic relationship with annelid hemoglobin. Zool. Sci. 6:915-926.
    • (1989) Zool. Sci. , vol.6 , pp. 915-926
    • Suzuki, T.1    Takagi, T.2    Okuda, K.3    Furukohri, T.4    Ohta, S.5
  • 63
    • 0038158587 scopus 로고
    • Primary structure of 440 kDa hemoglobin from the deep sea tubeworm Lamellibrachia
    • S. N. Vinogradov and O. H. Kapp, eds. Springer, New York
    • TAKAGI, T., H. IWAASA, S. OHTA, and T SUZUKI. 1991. Primary structure of 440 kDa hemoglobin from the deep sea tubeworm Lamellibrachia. Pp. 245-249 in S. N. VINOGRADOV and O. H. KAPP, eds. Structure and function of invertebrate oxygen carriers. Springer, New York.
    • (1991) Structure and Function of Invertebrate Oxygen Carriers , pp. 245-249
    • Takagi, T.1    Iwaasa, H.2    Ohta, S.3    Suzuki, T.4
  • 64
    • 0018859945 scopus 로고
    • The structure of hemoglobin from an unusual deep sea worm (Vestimentifera)
    • TERWILLIGER, R. C., N. B. TERWlLLIGER, and E. SCHABTACH. 1980. The structure of hemoglobin from an unusual deep sea worm (Vestimentifera). Comp. Biochem. Physiol. 65B:531-535.
    • (1980) Comp. Biochem. Physiol. , vol.65 B , pp. 531-535
    • Terwilliger, R.C.1    Terwllliger, N.B.2    Schabtach, E.3
  • 65
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • THOMPSON, J. D., T. J. GIBSON, E PLEWNIAK, E JEANMOUGIN, and D. G. HIGGINS. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, E.3    Jeanmougin, E.4    Higgins, D.G.5
  • 66
    • 0027075371 scopus 로고
    • The nature and origin of the modern hydrothermal vent fauna
    • TUNNICLIFFE, V. 1992. The nature and origin of the modern hydrothermal vent fauna. Palaios 7:338-350.
    • (1992) Palaios , vol.7 , pp. 338-350
    • Tunnicliffe, V.1
  • 67
    • 0029668305 scopus 로고    scopus 로고
    • Influence of sea-floor spreading on the global hydrothermal vent fauna
    • TUNNICLIFFE, V., and C. M. R. FOWLER. 1996. Influence of sea-floor spreading on the global hydrothermal vent fauna. Nature 379:531-533.
    • (1996) Nature , vol.379 , pp. 531-533
    • Tunnicliffe, V.1    Fowler, C.M.R.2
  • 68
    • 0001937695 scopus 로고
    • Metazoan adaptation to hydrogen sulfide
    • C. Bryant, ed. Chapman and Hall, London
    • VETTER, R. D., and G. N. POWELL. 1991. Metazoan adaptation to hydrogen sulfide. Pp. 109-128 in C. BRYANT, ed. Metazoan life without oxygen. Chapman and Hall, London.
    • (1991) Metazoan Life Without Oxygen , pp. 109-128
    • Vetter, R.D.1    Powell, G.N.2
  • 70
    • 84895356722 scopus 로고
    • Sulfide tolerance: Physiological mechanisms and ecological implications
    • VISMANN, B. 1991. Sulfide tolerance: physiological mechanisms and ecological implications, Ophelia 34:1-27.
    • (1991) Ophelia , vol.34 , pp. 1-27
    • Vismann, B.1
  • 71
    • 21844494452 scopus 로고
    • Sulfide tolerance and detoxification in Arenicola marina and Siptmculus nudus
    • VOLKEL, S. 1995. Sulfide tolerance and detoxification in Arenicola marina and Siptmculus nudus. Am. Zool. 35:145-153.
    • (1995) Am. Zool. , vol.35 , pp. 145-153
    • Volkel, S.1
  • 72
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • WEBER, R. E., and S. N. VINOGRADOV. 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
  • 73
    • 0042844884 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometic composition of the 400 kDa hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary structures of the three major globin chain
    • YUASA, H. J., B. N. GREEN, and T TAKAGI. 1996. Electrospray ionization mass spectrometic composition of the 400 kDa hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary structures of the three major globin chain. Biochim. Biophys. Acta 1296:235-244.
    • (1996) Biochim. Biophys. Acta , vol.1296 , pp. 235-244
    • Yuasa, H.J.1    Green, B.N.2    Takagi, T.3
  • 75
    • 0031020865 scopus 로고    scopus 로고
    • Quaternary structure of the extracellular haemoglobin of the lugworm Arenicola marina: A multi-angle-laser-light-scattering and electrospray-ionisation-mass-spectrometry analysis
    • ZAL, F., B. N. GREEN, F. H. LALLIER, S. N. VINOGRADOV, and A. TOULMOND. 1997a. Quaternary structure of the extracellular haemoglobin of the lugworm Arenicola marina: a multi-angle-laser-light-scattering and electrospray-ionisation-mass-spectrometry analysis. Eur. J. Biochem. 243:85-92.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 85-92
    • Zal, F.1    Green, B.N.2    Lallier, F.H.3    Vinogradov, S.N.4    Toulmond, A.5
  • 76
    • 0029882788 scopus 로고    scopus 로고
    • The multi-hemoglobin system of hydrothermal vent tube worm Riftia pachyptila: II - Complete polypeptide chain composition investigated by Maximum Entropy analysis of mass spectra
    • ZAL, E, F. H. LALLIER, B. N. GREEN, S. N. VINOGRADOV, and A. TOULMOND. 1996a. The multi-hemoglobin system of hydrothermal vent tube worm Riftia pachyptila: II - Complete polypeptide chain composition investigated by Maximum Entropy analysis of mass spectra. J. Biol. Chem. 271:8875-8881.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8875-8881
    • Zal, E.1    Lallier, F.H.2    Green, B.N.3    Vinogradov, S.N.4    Toulmond, A.5
  • 77
    • 0029945982 scopus 로고    scopus 로고
    • The multi-hemoglobin system of hydrothermal vent tube worm Riftia pachyptila: I - Reexamination of the number and masses of its constituents
    • ZAL, F., F. H. LALLIER, J. S. WALL, S. N. VINOGRADOV, and A. TOULMOND. 1996b. The multi-hemoglobin system of hydrothermal vent tube worm Riftia pachyptila: I - Reexamination of the number and masses of its constituents. J. Biol. Chem. 271:8869-8874.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8869-8874
    • Zal, F.1    Lallier, F.H.2    Wall, J.S.3    Vinogradov, S.N.4    Toulmond, A.5
  • 78
    • 0032555212 scopus 로고    scopus 로고
    • S-sulfohemoglobin and disulfide exchange: The mechanisms of sulfide binding by Riftia pachyptila hemoglobins
    • ZAL, F., E. LEIZE, F. H. LALLIER, A. TOULMOND, A. VAN DORSSELAER, and J. J. CHILDRESS. 1998. S-sulfohemoglobin and disulfide exchange: the mechanisms of sulfide binding by Riftia pachyptila hemoglobins. Proc. Natl. Acad. Sci. USA 95:8997-9002.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8997-9002
    • Zal, F.1    Leize, E.2    Lallier, F.H.3    Toulmond, A.4    Van Dorsselaer, A.5    Childress, J.J.6
  • 79
    • 0030701984 scopus 로고    scopus 로고
    • Primary structure of the common polypeptide chain b from the multi-haemoglobin system of the hydrothermal vent tube worm Riftia pachyptila: An insight on the sulfide binding-site
    • ZAL, E, T SUZUKI, Y. KAWASAKI, J. J. CHILDRESS, F. H. LALUER, and A. TOULMOND. 1997b. Primary structure of the common polypeptide chain b from the multi-haemoglobin system of the hydrothermal vent tube worm Riftia pachyptila: an insight on the sulfide binding-site. Proteins Struct. Funct. Genet. 29:562-574.
    • (1997) Proteins Struct. Funct. Genet. , vol.29 , pp. 562-574
    • Zal, E.1    Suzuki, T.2    Kawasaki, Y.3    Childress, J.J.4    Laluer, F.H.5    Toulmond, A.6
  • 80
    • 0032584099 scopus 로고    scopus 로고
    • Positive Darwinian selection after gene duplication in primate ribonuclease genes
    • ZHANG, J.,H. F. ROSENBERG, and M. NEI. 1998. Positive Darwinian selection after gene duplication in primate ribonuclease genes. Proc. Natl. Acad. Sci. USA 95:3708-3713.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3708-3713
    • Zhang, J.1    Rosenberg, H.F.2    Nei, M.3
  • 82
    • 0001133499 scopus 로고
    • A comparison of animal hemoglobin by triptic peptide pattern analysis
    • ZUCKERKANDL, E., R. T. JONES, and L. PAULING. 1960. A comparison of animal hemoglobin by triptic peptide pattern analysis. Proc. Natl. Acad. Sci. USA 46:1349-1360.
    • (1960) Proc. Natl. Acad. Sci. USA , vol.46 , pp. 1349-1360
    • Zuckerkandl, E.1    Jones, R.T.2    Pauling, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.