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Volumn 20, Issue 9, 2003, Pages 1564-1574

Single eubacterial origin of eukaryotic sulfide:quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times

Author keywords

Anaerobiosis; Electron transport chain; Endosymbiosis; Hydrogenosomes; Sulfide quinone reductase

Indexed keywords

ADENOSINE TRIPHOSPHATE; MITOCHONDRIAL ENZYME; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SULFIDE; SULFIDE:QUINONE OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0037787922     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/molbev/msg174     Document Type: Article
Times cited : (148)

References (76)
  • 2
    • 0037119593 scopus 로고    scopus 로고
    • Proterozoic ocean chemistry and evolution: A bioinorganic bridge
    • Anbar, A. D., and A. H. Knoll. 2002. Proterozoic ocean chemistry and evolution: a bioinorganic bridge. Science 297:1137-1142.
    • (2002) Science , vol.297 , pp. 1137-1142
    • Anbar, A.D.1    Knoll, A.H.2
  • 3
    • 0028022988 scopus 로고
    • Purification and characerization of sulfide-quinone reductase, a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limnetica
    • Arieli, B., Y. Shahak, D. Taglicht, G. Hauska, and E. Padan. 1994. Purification and characerization of sulfide-quinone reductase, a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limnetica. J. Biol. Chem. 269:5705-5711.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5705-5711
    • Arieli, B.1    Shahak, Y.2    Taglicht, D.3    Hauska, G.4    Padan, E.5
  • 4
    • 0025605321 scopus 로고
    • Oxidative detoxification of sulfide by mitochondria of the California killifish Fundulus parvipinnis and the speckled sanddab Citharichthys stigmaeus
    • Bagarinao, T., and R. D. Vetter. 1990. Oxidative detoxification of sulfide by mitochondria of the California killifish Fundulus parvipinnis and the speckled sanddab Citharichthys stigmaeus. J. Comp. Physiol. 160B:519-527.
    • (1990) J. Comp. Physiol. , vol.160 B , pp. 519-527
    • Bagarinao, T.1    Vetter, R.D.2
  • 5
    • 18744370234 scopus 로고    scopus 로고
    • Lack of self-averaging in neutral evolution of proteins
    • art. no. 208101
    • Bastolla, U., M. Porto, H. E. Roman, and M. Vendruscolo. 2002. Lack of self-averaging in neutral evolution of proteins. Phys. Rev. Lett. 89: art. no. 208101.
    • (2002) Phys. Rev. Lett. , vol.89
    • Bastolla, U.1    Porto, M.2    Roman, H.E.3    Vendruscolo, M.4
  • 8
    • 0342313681 scopus 로고    scopus 로고
    • Cyanobacterial sulfide-quinone reductase: Cloning and heterologous expression
    • Bronstein, M., M. Schütz, G. Hauska, E. Padan, and Y. Shahak. 2000. Cyanobacterial sulfide-quinone reductase: cloning and heterologous expression. J. Bacteriol. 182:3336-3344.
    • (2000) J. Bacteriol. , vol.182 , pp. 3336-3344
    • Bronstein, M.1    Schütz, M.2    Hauska, G.3    Padan, E.4    Shahak, Y.5
  • 9
    • 0041648334 scopus 로고    scopus 로고
    • NeighborNet: An agglomerative method for the construction of planar phylogenetic networks
    • Bryant, D., and V. Moulton. 2002. NeighborNet: an agglomerative method for the construction of planar phylogenetic networks. Proceedings of the 2nd Workshop in Algorithms for Bioinformatics. (http://www.mcb.mcgill.ca/~bryant/NeighborNet/).
    • (2002) Proceedings of the 2nd Workshop in Algorithms for Bioinformatics
    • Bryant, D.1    Moulton, V.2
  • 10
    • 0030002977 scopus 로고    scopus 로고
    • Genes encoding the same three subunits of respiratory complex II are present in the mitochondrial DNA of two phylogenetically distant eukaryotes
    • Burger, G., B. F. Lang, M. Reith, and M. W. Gray. 1996. Genes encoding the same three subunits of respiratory complex II are present in the mitochondrial DNA of two phylogenetically distant eukaryotes. Proc. Natl. Acad. Sci. USA 93:2328-2332.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2328-2332
    • Burger, G.1    Lang, B.F.2    Reith, M.3    Gray, M.W.4
  • 11
    • 0033784751 scopus 로고    scopus 로고
    • Bangiomorpha pubescens n. gen., n. sp.: Implications for the evolution of sex, multicellularity, and the Mesoproterozoic/Neoproterozoic radiation of eukaryotes
    • Butterfield, N. J. 2000. Bangiomorpha pubescens n. gen., n. sp.: implications for the evolution of sex, multicellularity, and the Mesoproterozoic/Neoproterozoic radiation of eukaryotes. Paleobiology 263:386-404.
    • (2000) Paleobiology , vol.263 , pp. 386-404
    • Butterfield, N.J.1
  • 13
    • 0032480974 scopus 로고    scopus 로고
    • A new model for Proterozoic ocean chemistry
    • Canfield, D. E. 1998. A new model for Proterozoic ocean chemistry. Nature 396:450-453.
    • (1998) Nature , vol.396 , pp. 450-453
    • Canfield, D.E.1
  • 14
  • 17
    • 0032808433 scopus 로고    scopus 로고
    • Chemolithoheterotrophy in a metazoan tissue: Sulfide supports cellular work in ciliated mussel gills
    • Doeller, J. E., B. K. Gaschen, V. Parrino, and D. W. Kraus. 1999. Chemolithoheterotrophy in a metazoan tissue: sulfide supports cellular work in ciliated mussel gills. J. Exp. Biol. 202:1953-1961.
    • (1999) J. Exp. Biol. , vol.202 , pp. 1953-1961
    • Doeller, J.E.1    Gaschen, B.K.2    Parrino, V.3    Kraus, D.W.4
  • 18
    • 0035746153 scopus 로고    scopus 로고
    • Chemolithoheterotrophy in a metazoan tissue: Thiosulfate production matches ATP demand in ciliated mussel gills
    • Doeller, J. E., M. K. Grieshaber, and D. W. Kraus. 2001. Chemolithoheterotrophy in a metazoan tissue: thiosulfate production matches ATP demand in ciliated mussel gills. J. Exp. Biol. 204:3755-3764.
    • (2001) J. Exp. Biol. , vol.204 , pp. 3755-3764
    • Doeller, J.E.1    Grieshaber, M.K.2    Kraus, D.W.3
  • 19
    • 0032404453 scopus 로고    scopus 로고
    • You are what you eat: A gene transfer ratchet could account for bacterial genes in eukaryotic nuclear genomes
    • Doolittle, W. F. 1998. You are what you eat: a gene transfer ratchet could account for bacterial genes in eukaryotic nuclear genomes. Trend. Genet. 14:307-311.
    • (1998) Trend. Genet. , vol.14 , pp. 307-311
    • Doolittle, W.F.1
  • 21
    • 0003437299 scopus 로고    scopus 로고
    • Distributed by the author, Department of Genetics, University of Washington, Seattle
    • Felsenstein, J. 1998. PHYLIP (phylogeny inference package). Distributed by the author, Department of Genetics, University of Washington, Seattle.
    • (1998) PHYLIP (Phylogeny Inference Package)
    • Felsenstein, J.1
  • 22
    • 34250479696 scopus 로고
    • The sulfide system: A new biotic community underneath the oxidized layer of marine sand bottoms
    • Fenchel, T. M., and R. J. Riedl. 1970. The sulfide system: a new biotic community underneath the oxidized layer of marine sand bottoms. Mar. Biol. 7:255-268.
    • (1970) Mar. Biol. , vol.7 , pp. 255-268
    • Fenchel, T.M.1    Riedl, R.J.2
  • 23
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea, and eukarya and its module in common with membrane-bound multisubunit hydrogenases
    • Friedrich T, and D. Schiede. 2000. The respiratory complex I of bacteria, archaea, and eukarya and its module in common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479:1-5.
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Schiede, D.2
  • 24
    • 0036898759 scopus 로고    scopus 로고
    • Prokaryotic evolution in light of lateral gene transfer
    • Gogarten, P. J., W. F. Doolittle, and J. G. Lawrence. 2002. Prokaryotic evolution in light of lateral gene transfer. Mol. Biol. Evol. 19:2226-2238.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 2226-2238
    • Gogarten, P.J.1    Doolittle, W.F.2    Lawrence, J.G.3
  • 25
    • 0010494571 scopus 로고    scopus 로고
    • Biological sulfide oxidation: Sulfide-quinone reductase (SQR), the primary reaction
    • S. G. Pandalai, ed. Research Signpost, Trivadrum, India
    • Griesbeck, C., G. Hauska, and M. Schütz. 2000. Biological sulfide oxidation: sulfide-quinone reductase (SQR), the primary reaction. Pp. 179-203 in S. G. Pandalai, ed. Recent research developments in microbiology, Vol 4. Research Signpost, Trivadrum, India.
    • (2000) Recent Research Developments in Microbiology , vol.4 , pp. 179-203
    • Griesbeck, C.1    Hauska, G.2    Schütz, M.3
  • 27
    • 0031942895 scopus 로고    scopus 로고
    • Animal adaptations for tolerance and exploitation of poisonous sulfide
    • Grieshaber, M. K., and S. Völkel. 1998. Animal adaptations for tolerance and exploitation of poisonous sulfide. Ann. Rev. Physiol. 60:30-53.
    • (1998) Ann. Rev. Physiol. , vol.60 , pp. 30-53
    • Grieshaber, M.K.1    Völkel, S.2
  • 28
    • 0033947724 scopus 로고    scopus 로고
    • Enolase from Trypanosoma brucei, from the amitochondriate protist Mastigamoeba balamuthi, and from the chloroplast and cytosol of Euglena gracilis: Pieces in the evolutionary puzzle of the eukaryotic glycolytic pathway
    • Hannaert, V., H. Brinkmann, U. Nowitzki, J. A. Lee, M. A. Albert, C. W. Sensen, T. Gaasterland, M. Muller, P. Michels, and W. Martin. 2000. Enolase from Trypanosoma brucei, from the amitochondriate protist Mastigamoeba balamuthi, and from the chloroplast and cytosol of Euglena gracilis: pieces in the evolutionary puzzle of the eukaryotic glycolytic pathway. Mol. Biol. Evol. 17:989-1000.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 989-1000
    • Hannaert, V.1    Brinkmann, H.2    Nowitzki, U.3    Lee, J.A.4    Albert, M.A.5    Sensen, C.W.6    Gaasterland, T.7    Muller, M.8    Michels, P.9    Martin, W.10
  • 29
    • 0033736055 scopus 로고    scopus 로고
    • Iron hydrogenase and the evolution of anaerobic eukaryotes
    • Horner, D. S., P. D. Foster, and T. M. Embley. 2000. Iron hydrogenase and the evolution of anaerobic eukaryotes. Mol. Biol. Evol. 17:1695-1709.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1695-1709
    • Horner, D.S.1    Foster, P.D.2    Embley, T.M.3
  • 30
    • 0036495241 scopus 로고    scopus 로고
    • Iron hydrogenases - Ancient enzymes in modern eukaryotes
    • Horner, D. S., B. Heil, T. Happe, and T. M. Embley. 2002. Iron hydrogenases-ancient enzymes in modern eukaryotes. Trends Biochem. Sci. 27:148-153.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 148-153
    • Horner, D.S.1    Heil, B.2    Happe, T.3    Embley, T.M.4
  • 31
    • 0032819619 scopus 로고    scopus 로고
    • A single eubacterial origin of eukaryotic pyruvate: Ferredoxin oxidoreductase genes: Implications for the evolution of anaerobic eukaryotes
    • Horner, D. S., R. P. Hirt, and T. M. Embley. 1999. A single eubacterial origin of eukaryotic pyruvate: ferredoxin oxidoreductase genes: implications for the evolution of anaerobic eukaryotes. Mol. Biol. Evol. 16:1280-1291.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 1280-1291
    • Horner, D.S.1    Hirt, R.P.2    Embley, T.M.3
  • 32
    • 0035811487 scopus 로고    scopus 로고
    • Morphological and ecological complexity in early eukaryotic ecosystems
    • Javaux, E. J., A. H. Knoll, and M. R. Walter. 2001. Morphological and ecological complexity in early eukaryotic ecosystems. Nature 412:66-69.
    • (2001) Nature , vol.412 , pp. 66-69
    • Javaux, E.J.1    Knoll, A.H.2    Walter, M.R.3
  • 33
    • 0016837549 scopus 로고
    • Paracoccus denitrificans and the evolutionary origin of the mitochondrion
    • John, P., and F. R. Whatley. 1975. Paracoccus denitrificans and the evolutionary origin of the mitochondrion. Nature 254:495-498.
    • (1975) Nature , vol.254 , pp. 495-498
    • John, P.1    Whatley, F.R.2
  • 35
    • 0035504444 scopus 로고    scopus 로고
    • The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
    • Huynen M. A., B. Snel, P. Bork and T. J. Gibson. 2001. The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly. Hum. Mol. Genet. 10:2463-2468.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2463-2468
    • Huynen, M.A.1    Snel, B.2    Bork, P.3    Gibson, T.J.4
  • 36
    • 0035936144 scopus 로고    scopus 로고
    • The genome of the intracellular parasite, Encephalithozoon cuniculi
    • Katinka, M.D., S. Duprat, E. Cornillot et al. (17 co-authors). 2001. The genome of the intracellular parasite, Encephalithozoon cuniculi. Nature 414:450-453.
    • (2001) Nature , vol.414 , pp. 450-453
    • Katinka, M.D.1    Duprat, S.2    Cornillot, E.3
  • 37
    • 0034443285 scopus 로고    scopus 로고
    • Origin and evolution of the mitochondrial proteome
    • Kurland, C. G., and S. G. Andersson. 2000. Origin and evolution of the mitochondrial proteome. Microbiol. Mol. Biol. Rev. 64:786-820.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 786-820
    • Kurland, C.G.1    Andersson, S.G.2
  • 38
    • 0037115872 scopus 로고    scopus 로고
    • Comparative analysis of ribosomal proteins in complete genomes: An example of reductive evolution at the domain scale
    • Lecompte, O., R. Ripp, J. C. Thierry, D. Moras, and O. Poch. 2002. Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale. Nucleic Acids Res. 30:5382-5390.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5382-5390
    • Lecompte, O.1    Ripp, R.2    Thierry, J.C.3    Moras, D.4    Poch, O.5
  • 39
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill, R., and G. Kispal. 2000. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trend. Biochem. Sci. 25:352-356.
    • (2000) Trend. Biochem. Sci. , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 40
    • 0035197418 scopus 로고    scopus 로고
    • An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle
    • Martin, W., M. Hoffmeister, C. Rotte, and K. Henze. 2001. An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle. Biol. Chem. 382:1521-1539.
    • (2001) Biol. Chem. , vol.382 , pp. 1521-1539
    • Martin, W.1    Hoffmeister, M.2    Rotte, C.3    Henze, K.4
  • 41
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis for the first eukaryote
    • Martin, W., and M. Müller. 1998. The hydrogen hypothesis for the first eukaryote. Nature 392:37-41.
    • (1998) Nature , vol.392 , pp. 37-41
    • Martin, W.1    Müller, M.2
  • 42
    • 0037126071 scopus 로고    scopus 로고
    • Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus
    • Martin, W., T. Rujan, E. Richly, A. Hansen, S. Cornelsen, T. Lins, D. Leister, B. Stoebe, M. Hasegawa, and D. Penny. 2002. Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus. Proc. Natl. Acad. Sci. USA 99:12246-12251.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12246-12251
    • Martin, W.1    Rujan, T.2    Richly, E.3    Hansen, A.4    Cornelsen, S.5    Lins, T.6    Leister, D.7    Stoebe, B.8    Hasegawa, M.9    Penny, D.10
  • 43
    • 0004056086 scopus 로고
    • University Park Press, Baltimore
    • National Research Council. 1979. Hydrogen sulfide. University Park Press, Baltimore.
    • (1979) Hydrogen Sulfide
  • 44
    • 0030458552 scopus 로고    scopus 로고
    • Phylogenetic analysis in molecular evolutionary genetics
    • Nei, M. 1996. Phylogenetic analysis in molecular evolutionary genetics. Ann. Rev. Genet. 30:371-403.
    • (1996) Ann. Rev. Genet. , vol.30 , pp. 371-403
    • Nei, M.1
  • 46
    • 0036549786 scopus 로고    scopus 로고
    • Evidence for lateral transfer of genes encoding ferredoxins, nitroreductases, NADH oxidase, and alcohol dehydrogenase 3 from anaerobic prokaryotes to Giardia lamblia and Entamoeba histolytica
    • Nixon, J. E. J., A. Wang, J. Field, H. G. Morrison, A. G. McArthur, M. L. Sogin, B. J. Loftus, and J. Samuelson. 2002. Evidence for lateral transfer of genes encoding ferredoxins, nitroreductases, NADH oxidase, and alcohol dehydrogenase 3 from anaerobic prokaryotes to Giardia lamblia and Entamoeba histolytica. Euk. Cell 1:181-190.
    • (2002) Euk. Cell , vol.1 , pp. 181-190
    • Nixon, J.E.J.1    Wang, A.2    Field, J.3    Morrison, H.G.4    McArthur, A.G.5    Sogin, M.L.6    Loftus, B.J.7    Samuelson, J.8
  • 47
    • 0034039158 scopus 로고    scopus 로고
    • Sulfide:quinone oxidoreductase in membranes of the hyperthermophilic bacterium Aquifex aeolicus (VF5)
    • Nübel, T., C. Klughammer, R. Huber, G. Hauska, and M. Schütz. 2000. Sulfide:quinone oxidoreductase in membranes of the hyperthermophilic bacterium Aquifex aeolicus (VF5) Arch. Microbiol. 173:233-244.
    • (2000) Arch. Microbiol. , vol.173 , pp. 233-244
    • Nübel, T.1    Klughammer, C.2    Huber, R.3    Hauska, G.4    Schütz, M.5
  • 48
    • 0025284319 scopus 로고
    • Production of thiosulfate during sulphide oxidation by mitochondria of the symbiont-containing bivalve Solemya reidi
    • O'Brien, J., and R. D. Vetter. 1990. Production of thiosulfate during sulphide oxidation by mitochondria of the symbiont-containing bivalve Solemya reidi. J. Exp. Biol. 149:133-148.
    • (1990) J. Exp. Biol. , vol.149 , pp. 133-148
    • O'Brien, J.1    Vetter, R.D.2
  • 49
    • 0028252105 scopus 로고
    • Sulphide tolerance in Heteromastus filiformis (Polychaeta): Mitochondrial adaptations
    • Oeschger, R., and B. Vismann. 1994. Sulphide tolerance in Heteromastus filiformis (Polychaeta): mitochondrial adaptations. Ophelia 40:147-158.
    • (1994) Ophelia , vol.40 , pp. 147-158
    • Oeschger, R.1    Vismann, B.2
  • 50
    • 0014409302 scopus 로고
    • Roles of ubiquinone-10 and rhodoquinone in photosynthetic formation of adenosine triphosphate by chromatophores from Rhodospirillum rubrum
    • Okayama, S., N. Yamamoto, K. Nishikawa, and T. Horio. 1968. Roles of ubiquinone-10 and rhodoquinone in photosynthetic formation of adenosine triphosphate by chromatophores from Rhodospirillum rubrum. J. Biol. Chem. 243:2995-2999.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2995-2999
    • Okayama, S.1    Yamamoto, N.2    Nishikawa, K.3    Horio, T.4
  • 51
    • 0033867969 scopus 로고    scopus 로고
    • ATP production from the oxidation of sulfide in gill mitochondria of the ribbed mussel Geukensia demissa
    • Parrino, V., D. W. Kraus, and J. E. Doeller. 2000. ATP Production from the oxidation of sulfide in gill mitochondria of the ribbed mussel Geukensia demissa. J. Exp. Biol. 202:2209-2218.
    • (2000) J. Exp. Biol. , vol.202 , pp. 2209-2218
    • Parrino, V.1    Kraus, D.W.2    Doeller, J.E.3
  • 52
    • 0032804337 scopus 로고    scopus 로고
    • Structure and mechanism of iron-only hydrogenases
    • Peters, J. W. 1999 Structure and mechanism of iron-only hydrogenases. Curr. Opin. Struct. Biol. 9:670-676.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 670-676
    • Peters, J.W.1
  • 53
    • 0038575389 scopus 로고    scopus 로고
    • Archaeal chromatin and transcription
    • Reeve, J. 2003. Archaeal chromatin and transcription. Mol. Microbiol. 48:587-598.
    • (2003) Mol. Microbiol. , vol.48 , pp. 587-598
    • Reeve, J.1
  • 55
    • 0030627901 scopus 로고    scopus 로고
    • Protein structures sustain evolutionary drift
    • Rost, B. 1997. Protein structures sustain evolutionary drift. Fold. Des. 2:S19-S24.
    • (1997) Fold. Des. , vol.2
    • Rost, B.1
  • 56
    • 0035029530 scopus 로고    scopus 로고
    • + oxidoreductase from the mitochondrion of Euglena gracilis and from the apicomplexan Cryptosporidium parvum: A fusion of pyruvate: Ferredoxin oxidoreductase and NADPH-cytochrome P450 reductase
    • + oxidoreductase from the mitochondrion of Euglena gracilis and from the apicomplexan Cryptosporidium parvum: a fusion of pyruvate: ferredoxin oxidoreductase and NADPH-cytochrome P450 reductase. Mol. Biol. Evol. 18:710-720.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 710-720
    • Rotte, C.1    Stejskal, F.2    Zhu, G.3    Keithly, J.S.4    Martin, W.5
  • 57
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 58
    • 0034697992 scopus 로고    scopus 로고
    • Early evolution of cytochrome bc complexes
    • Schütz, M., M. Brugna, E. Lebrun et al. (12 co-authors). 2000. Early evolution of cytochrome bc complexes. J. Mol. Biol. 300:663-675.
    • (2000) J. Mol. Biol. , vol.300 , pp. 663-675
    • Schütz, M.1    Brugna, M.2    Lebrun, E.3
  • 59
    • 0031670477 scopus 로고    scopus 로고
    • Sulfide-quinone reductase activity in membranes of the chemotrophic bacterium Paracoccus denitrificans GB17
    • Schütz, M., C. Klughammer, C. Griesbeck, A. Quentmeier, C. G. Friedrich, and G. Hauska. 1998. Sulfide-quinone reductase activity in membranes of the chemotrophic bacterium Paracoccus denitrificans GB17. Arch. Microbiol. 170:353-360.
    • (1998) Arch. Microbiol. , vol.170 , pp. 353-360
    • Schütz, M.1    Klughammer, C.2    Griesbeck, C.3    Quentmeier, A.4    Friedrich, C.G.5    Hauska, G.6
  • 60
    • 1842375039 scopus 로고    scopus 로고
    • Sulfide-quinone reductase from Rhodobacter capsulatus
    • Schütz, M., Y. Shahak, E. Padan, and G. Hauska. 1997. Sulfide-quinone reductase from Rhodobacter capsulatus. J. Biol. Chem. 272:9890-9894.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9890-9894
    • Schütz, M.1    Shahak, Y.2    Padan, E.3    Hauska, G.4
  • 61
    • 0026521170 scopus 로고
    • Sulfide quinone reductase (SQR) activity in Chlorobium
    • Shahak, Y., B. Arieli, E. Padan, and G. Hauska. 1992. Sulfide quinone reductase (SQR) activity in Chlorobium. FEBS Lett. 299:127-130.
    • (1992) FEBS Lett. , vol.299 , pp. 127-130
    • Shahak, Y.1    Arieli, B.2    Padan, E.3    Hauska, G.4
  • 63
    • 0035282466 scopus 로고    scopus 로고
    • Isotopic evidence for microbial sulphate reduction in the early Archaean era
    • Shen, Y., R. Buick, and D. E. Canfield. 2001. Isotopic evidence for microbial sulphate reduction in the early Archaean era. Nature 410:77-81.
    • (2001) Nature , vol.410 , pp. 77-81
    • Shen, Y.1    Buick, R.2    Canfield, D.E.3
  • 64
    • 0037025197 scopus 로고    scopus 로고
    • Rooting the eukaryote tree by using a derived gene fusion
    • Stechmann, A. and T. Cavalier-Smith. 2002. Rooting the eukaryote tree by using a derived gene fusion. Science 297:89-91.
    • (2002) Science , vol.297 , pp. 89-91
    • Stechmann, A.1    Cavalier-Smith, T.2
  • 65
    • 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
  • 66
    • 0034804608 scopus 로고    scopus 로고
    • Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
    • Tachezy, J., L. B. Sanchez, and M. Müller. 2001. Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS. Mol. Biol. Evol. 18:1919-1928.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1919-1928
    • Tachezy, J.1    Sanchez, L.B.2    Müller, M.3
  • 67
    • 0027968068 scopus 로고
    • ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. ClustalW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 69
    • 0034646401 scopus 로고    scopus 로고
    • Insights into DNA replication from the third domain of life
    • Tye, B. K. 2000. Insights into DNA replication from the third domain of life. Proc. Natl. Acad. Sci. USA 97:2399-2401.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2399-2401
    • Tye, B.K.1
  • 70
    • 0033532082 scopus 로고    scopus 로고
    • A fission yeast gene for mitochondrial sulfide oxidation
    • Vande Weghe, J. G., and D. W. Ow. 1999. A fission yeast gene for mitochondrial sulfide oxidation. J. Biol. Chem. 274:13250-13257.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13250-13257
    • Vande Weghe, J.G.1    Ow, D.W.2
  • 71
    • 0000576377 scopus 로고
    • Mechanisms of sulphide tolerance in the peanut worm, Sipunculus nudus (Sipunculidae) and in the lugworm, Arenicola marina (Polychaeta)
    • Völkel, S., and M. K. Grieshaber. 1992. Mechanisms of sulphide tolerance in the peanut worm, Sipunculus nudus (Sipunculidae) and in the lugworm, Arenicola marina (Polychaeta). J. Comp. Physiol. B Biochem. Syst. Environ. Physiol. 162:469-477.
    • (1992) J. Comp. Physiol. B Biochem. Syst. Environ. Physiol. , vol.162 , pp. 469-477
    • Völkel, S.1    Grieshaber, M.K.2
  • 72
    • 0030068577 scopus 로고    scopus 로고
    • Mitochondrial sulfide oxidation in Arenicola marina: Evidence for alternative electron pathways
    • -. 1996a. Mitochondrial sulfide oxidation in Arenicola marina: evidence for alternative electron pathways. Eur. J. Biochem. 235:231-237.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 231-237
  • 73
    • 1842365519 scopus 로고    scopus 로고
    • Sulphide oxidation and oxidative phosphorylation in the mitochondria of the lugworm Arenicola marina
    • -. 1996b. Sulphide oxidation and oxidative phosphorylation in the mitochondria of the lugworm Arenicola marina. J. Exp. Biol. 200:83-92.
    • (1996) J. Exp. Biol. , vol.200 , pp. 83-92
  • 74
    • 0028983706 scopus 로고
    • Sulfide stress and tolerance in the lugworm Arenicola marina during low tide
    • Völkel, S., K. Hauschild, and M. K. Grieshaber. 1995. Sulfide stress and tolerance in the lugworm Arenicola marina during low tide. Mar. Ecol. Prog. Ser. 122:205-215.
    • (1995) Mar. Ecol. Prog. Ser. , vol.122 , pp. 205-215
    • Völkel, S.1    Hauschild, K.2    Grieshaber, M.K.3
  • 75
    • 0037158721 scopus 로고    scopus 로고
    • A mitochondrial remnant in the microsporidian Trachipleistophora hominis
    • Williams, B.A., R. P. Hirt, J. M. Lucocq, and T. M. Embley. 2002 A mitochondrial remnant in the microsporidian Trachipleistophora hominis. Nature 418:865-869.
    • (2002) Nature , vol.418 , pp. 865-869
    • Williams, B.A.1    Hirt, R.P.2    Lucocq, J.M.3    Embley, T.M.4
  • 76
    • 0035030625 scopus 로고    scopus 로고
    • Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria
    • Yong, R., and D. G. Searcy. 2001. Sulfide oxidation coupled to ATP synthesis in chicken liver mitochondria. Comp. Biochem. Physiol. B 129:129-137.
    • (2001) Comp. Biochem. Physiol. B , vol.129 , pp. 129-137
    • Yong, R.1    Searcy, D.G.2


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