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Volumn 8, Issue 1, 2008, Pages

Enzyme phylogenies as markers for the oxidation state of the environment: The case of respiratory arsenate reductase and related enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ARSENATE REDUCTASE; ARSENIC ACID; ARSENIC TRIOXIDE; MOLYBDOPTERIN; ARSENITE OXIDASE; DIMETHYL SULFOXIDE REDUCTASE; IRON SULFUR PROTEIN; METALLOPROTEIN; MOLYBDENUM COFACTOR; OXIDOREDUCTASE; PTERIDINE DERIVATIVE;

EID: 49249132556     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-8-206     Document Type: Article
Times cited : (98)

References (59)
  • 2
    • 0032828960 scopus 로고    scopus 로고
    • Respiratory chains in the last common ancestor of living organisms
    • 10.1007/PL00006568. 10486003
    • Respiratory chains in the last common ancestor of living organisms. J Castresana M Moreira, J Mol Evol 1999 49 453 460 10.1007/PL00006568 10486003
    • (1999) J Mol Evol , vol.49 , pp. 453-460
    • Castresana, J.1    Moreira, M.2
  • 3
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • 11524134
    • Classification and phylogeny of hydrogenases. PM Vignais B Billoud J Meyer, FEMS Microbiol Rev 2001 25 455 501 11524134
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 5
    • 0036802691 scopus 로고    scopus 로고
    • Arsenate reductase in prokaryotes and eukaryotes
    • 12426124
    • Arsenate reductase in prokaryotes and eukaryotes. R Mukhopadhyay BP Rosen, Environ Health Perspect 2002 110 Suppl 5 745 748 12426124
    • (2002) Environ Health Perspect , vol.110 , Issue.SUPPL. 5 , pp. 745-748
    • Mukhopadhyay, R.1    Rosen, B.P.2
  • 6
    • 12944320850 scopus 로고    scopus 로고
    • Arsenic, microbes and contaminated aquifers
    • 10.1016/j.tim.2004.12.002. 15680760
    • Arsenic, microbes and contaminated aquifers. RS Oremland JF Stolz, Trends Microbiol 2005 13 45 49 10.1016/j.tim.2004.12.002 15680760
    • (2005) Trends Microbiol , vol.13 , pp. 45-49
    • Oremland, R.S.1    Stolz, J.F.2
  • 7
    • 13544263302 scopus 로고    scopus 로고
    • Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic
    • 15691908. 10.1128/AEM.71.2.599-608.2005
    • Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic. S Silver LT Phung, Appl Environ Microbiol 2005 71 599 608 15691908 10.1128/AEM.71.2.599-608.2005
    • (2005) Appl Environ Microbiol , vol.71 , pp. 599-608
    • Silver, S.1    Phung, L.T.2
  • 8
    • 33747353951 scopus 로고    scopus 로고
    • Arsenic and selenium in microbial metabolism
    • 10.1146/annurev.micro.60.080805.142053. 16704340
    • Arsenic and selenium in microbial metabolism. JF Stolz P Basu JM Santini RS Oremland, Annu Rev Microbiol 2006 60 107 130 10.1146/annurev.micro.60.080805. 142053 16704340
    • (2006) Annu Rev Microbiol , vol.60 , pp. 107-130
    • Stolz, J.F.1    Basu, P.2    Santini, J.M.3    Oremland, R.S.4
  • 9
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å
    • 10.1016/S0969-2126(01)00566-4. 11250197
    • Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å PJ Ellis T Conrads R Hille P Kuhn, Structure 2001 9 125 132 10.1016/S0969-2126(01)00566-4 11250197
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.J.1    Conrads, T.2    Hille, R.3    Kuhn, P.4
  • 10
    • 33646894324 scopus 로고    scopus 로고
    • The Rieske protein: A case study on the pitfalls of multiple sequence alignments and phylogenetic reconstruction
    • 10.1093/molbev/msk010. 16569761
    • The Rieske protein: A case study on the pitfalls of multiple sequence alignments and phylogenetic reconstruction. E Lebrun JM Santini M Brugna AL Ducluzeau S Ouchane B Schoepp-Cothenet F Baymann W Nitschke, Mol Biol Evol 2006 23 1180 1191 10.1093/molbev/msk010 16569761
    • (2006) Mol Biol Evol , vol.23 , pp. 1180-1191
    • Lebrun, E.1    Santini, J.M.2    Brugna, M.3    Ducluzeau, A.L.4    Ouchane, S.5    Schoepp-Cothenet, B.6    Baymann, F.7    Nitschke, W.8
  • 11
    • 0027944529 scopus 로고
    • Microbe grows by reducing arsenic
    • 10.1038/371750a0. 7935832
    • Microbe grows by reducing arsenic. D Ahmann AL Roberts LR Krumholz FM Morel, Nature 1994 371 750 10.1038/371750a0 7935832
    • (1994) Nature , vol.371 , pp. 750
    • Ahmann, D.1    Roberts, A.L.2    Krumholz, L.R.3    Morel, F.M.4
  • 13
    • 0141591471 scopus 로고    scopus 로고
    • Genetic identification of a respiratory arsenate reductase
    • 12939408. 10.1073/pnas.1834303100
    • Genetic identification of a respiratory arsenate reductase. CW Saltikov DK Newman, Proc Nat Acad Sci USA 2003 100 10983 10988 12939408 10.1073/pnas.1834303100
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 10983-10988
    • Saltikov, C.W.1    Newman, D.K.2
  • 14
    • 0032456229 scopus 로고    scopus 로고
    • A brief review of microbial arsenate reductase
    • A brief review of microbial arsenate reductase. DK Newman D Ahmann FM Morel, Geomicrobiology 1998 15 255 268
    • (1998) Geomicrobiology , vol.15 , pp. 255-268
    • Newman, D.K.1    Ahmann, D.2    Morel, F.M.3
  • 15
    • 0032145466 scopus 로고    scopus 로고
    • Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis
    • 10.1046/j.1432-1327.1998.2550647.x. 9738904
    • Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. T Krafft JM Macy, Eur J Biochem 1998 255 647 653 10.1046/j.1432-1327.1998.2550647.x 9738904
    • (1998) Eur J Biochem , vol.255 , pp. 647-653
    • Krafft, T.1    MacY, J.M.2
  • 16
    • 0642308250 scopus 로고    scopus 로고
    • The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10
    • 10.1016/S0378-1097(03)00609-8. 13129615
    • The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10. E Afkar J Lisak C Saltikov P Basu RS Oremland JF Stolz, FEMS Microbiol Lett 2003 226 107 112 10.1016/S0378-1097(03)00609-8 13129615
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 107-112
    • Afkar, E.1    Lisak, J.2    Saltikov, C.3    Basu, P.4    Oremland, R.S.5    Stolz, J.F.6
  • 17
    • 9744286923 scopus 로고    scopus 로고
    • Bacillus macyae sp. nov., an arsenate-respiring bacterium isolated from an Australian gold mine
    • 10.1099/ijs.0.63059-0. 15545465
    • Bacillus macyae sp. nov., an arsenate-respiring bacterium isolated from an Australian gold mine. JM Santini IC Streimann RN vanden Hoven, Int J Syst Evol Microbiol 2004 54 2241 2244 10.1099/ijs.0.63059-0 15545465
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 2241-2244
    • Santini, J.M.1    Streimann, I.C.2    Vanden, N.H.R.3
  • 19
    • 0036190355 scopus 로고    scopus 로고
    • The DMSO reductase family of microbial molybdenum enzymes; Molecular properties and role in the dissimilatory reduction of toxic elements
    • 10.1080/014904502317246138
    • The DMSO reductase family of microbial molybdenum enzymes; molecular properties and role in the dissimilatory reduction of toxic elements. AG McEwan JP Ridge CA McDevitt P Hugenholtz, Geomicrobiol J 2002 19 3 21 10.1080/014904502317246138
    • (2002) Geomicrobiol J , vol.19 , pp. 3-21
    • McEwan, A.G.1    Ridge, J.P.2    McDevitt, C.A.3    Hugenholtz, P.4
  • 21
    • 27744451137 scopus 로고    scopus 로고
    • Arsenate respiratory reductase gene (arrA) for Desulfosporosinus sp. strain Y5
    • 10.1016/j.bbrc.2005.10.011. 16242665
    • Arsenate respiratory reductase gene (arrA) for Desulfosporosinus sp. strain Y5. JR Pérez-Jiménez C DeFraia LY Young, Biochem Biophys Res Commun 2005 338 825 829 10.1016/j.bbrc.2005.10.011 16242665
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 825-829
    • Pérez-Jiménez, J.R.1    Defraia, C.2    Young, L.Y.3
  • 22
    • 0026550359 scopus 로고
    • Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulfide reductase
    • 10.1111/j.1432-1033.1992.tb16953.x. 1597189
    • Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulfide reductase. T Krafft M Bokranz O Klimmek I Schröder F Fahrenholz E Kojro A Kröger, Eur J Biochem 1992 206 503 510 10.1111/j.1432-1033.1992.tb16953.x 1597189
    • (1992) Eur J Biochem , vol.206 , pp. 503-510
    • Krafft, T.1    Bokranz, M.2    Klimmek, O.3    Schröder, I.4    Fahrenholz, F.5    Kojro, E.6    Kröger, A.7
  • 23
    • 0032923401 scopus 로고    scopus 로고
    • The genetic basis of tetrathionate respiration in Salmonella typhimurium
    • 10.1046/j.1365-2958.1999.01345.x. 10231485
    • The genetic basis of tetrathionate respiration in Salmonella typhimurium. M Hensel AP Hinsley T Nikolaus G Sawers BC Berks, Mol Microbiol 1999 32 275 287 10.1046/j.1365-2958.1999.01345.x 10231485
    • (1999) Mol Microbiol , vol.32 , pp. 275-287
    • Hensel, M.1    Hinsley, A.P.2    Nikolaus, T.3    Sawers, G.4    Berks, B.C.5
  • 25
    • 0036854448 scopus 로고    scopus 로고
    • Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica
    • 12427953
    • Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica. AP Hinsley BC Berks, Microbiology 2002 148 Pt 11 3631 3638 12427953
    • (2002) Microbiology , vol.148 , Issue.PART 11 , pp. 3631-3638
    • Hinsley, A.P.1    Berks, B.C.2
  • 26
    • 0035907063 scopus 로고    scopus 로고
    • A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif
    • 10.1016/S0014-5793(01)02428-0. 11376660
    • A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif. AP Hinsley NR Standley T Palmer BC Berks, FEBS Lett 2001 497 45 49 10.1016/S0014-5793(01) 02428-0 11376660
    • (2001) FEBS Lett , vol.497 , pp. 45-49
    • Hinsley, A.P.1    Standley, N.R.2    Palmer, T.3    Berks, B.C.4
  • 27
    • 33947168706 scopus 로고    scopus 로고
    • Detection, diversity and expression of aerobic bacterial arsenite oxidase genes
    • 10.1111/j.1462-2920.2006.01215.x. 17359265
    • Detection, diversity and expression of aerobic bacterial arsenite oxidase genes. WP Inskeep RE Macur N Hamamura TP Warelow SA Ward JM Santini, Environ Microbiol 2007 9 934 943 10.1111/j.1462-2920.2006.01215.x 17359265
    • (2007) Environ Microbiol , vol.9 , pp. 934-943
    • Inskeep, W.P.1    MacUr, R.E.2    Hamamura, N.3    Warelow, T.P.4    Ward, S.A.5    Santini, J.M.6
  • 28
    • 0042430577 scopus 로고    scopus 로고
    • Formate dehydrogenase - a versatile enzyme in changing environments
    • 10.1016/S0959-440X(03)00098-8. 12948771
    • Formate dehydrogenase - a versatile enzyme in changing environments. M Jormakka B Byrne S Iwata, Curr Opin Struct Biol 2003 13 4 418 423 10.1016/S0959-440X(03)00098-8 12948771
    • (2003) Curr Opin Struct Biol , vol.13 , Issue.4 , pp. 418-423
    • Jormakka, M.1    Byrne, B.2    Iwata, S.3
  • 29
    • 0025788382 scopus 로고
    • Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine
    • 1834669
    • Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine. BL Berg J Li J Heider V Stewart, J Biol Chem 1991 266 22380 22385 1834669
    • (1991) J Biol Chem , vol.266 , pp. 22380-22385
    • Berg, B.L.1    Li, J.2    Heider, J.3    Stewart, V.4
  • 30
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
    • 10.1111/j.1365-2958.1988.tb00090.x. 3062312
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. PT Bilous ST Cole WF Anderson JH Weiner, Mol Microbiol 1988 2 785 795 10.1111/j.1365-2958.1988.tb00090.x 3062312
    • (1988) Mol Microbiol , vol.2 , pp. 785-795
    • Bilous, P.T.1    Cole, S.T.2    Anderson, W.F.3    Weiner, J.H.4
  • 31
    • 35648954491 scopus 로고    scopus 로고
    • Nitrate reductase: Structure, functions, and effect of stress factors
    • 10.1134/S0006297907100124. 18021072
    • Nitrate reductase: structure, functions, and effect of stress factors. EV Morozkina RA Zvyagilskaya, Biochemistry (mosc.) 2007 72 1151 1160 10.1134/S0006297907100124 18021072
    • (2007) Biochemistry (Mosc.) , vol.72 , pp. 1151-1160
    • Morozkina, E.V.1    Zvyagilskaya, R.A.2
  • 32
    • 0036523461 scopus 로고    scopus 로고
    • Evolution of nitrate reductase: Molecular and structural variations on a common function
    • 10.1002/1439-7633(20020301)3:2/3<198::AID-CBIC198>3.0.CO;2-C. 11921398
    • Evolution of nitrate reductase: molecular and structural variations on a common function. JF Stolz P Basu, Chembiochem 2002 3 198 206 10.1002/1439-7633(20020301)3:2/3<198::AID-CBIC198>3.0.CO;2-C 11921398
    • (2002) Chembiochem , vol.3 , pp. 198-206
    • Stolz, J.F.1    Basu, P.2
  • 33
    • 0031061532 scopus 로고    scopus 로고
    • A fosmid-based genomic map and identification of 474 genes of the hyperthermophilic archaeon Pyrobaculum aerophilum
    • 10.1007/s007920050013. 9680335
    • A fosmid-based genomic map and identification of 474 genes of the hyperthermophilic archaeon Pyrobaculum aerophilum. S Fitz-Gibbon AJ Choi JH Miller KO Stetter MI Simon R Swanson UJ Kim, Extremophiles 1997 1 36 51 10.1007/s007920050013 9680335
    • (1997) Extremophiles , vol.1 , pp. 36-51
    • Fitz-Gibbon, S.1    Choi, A.J.2    Miller, J.H.3    Stetter, K.O.4    Simon, M.I.5    Swanson, R.6    Kim, U.J.7
  • 34
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • erratum in: Nature 1998 394: 101. 10.1038/37052. 9389475
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. HP Klenk RA Clayton JF Tomb & co-authors, Nature 1997 390 364 370 erratum in: Nature 1998 394: 101 10.1038/37052 9389475
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2
  • 35
    • 0036179831 scopus 로고    scopus 로고
    • The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes
    • 10.1046/j.0014-2956.2001.02662.x. 11856339
    • The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes. W Dietrich O Klimmek, Eur J Biochem 2002 269 1086 1095 10.1046/j.0014-2956.2001.02662.x 11856339
    • (2002) Eur J Biochem , vol.269 , pp. 1086-1095
    • Dietrich, W.1    Klimmek, O.2
  • 36
    • 0029078973 scopus 로고
    • Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism
    • 7751291
    • Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism. NK Heinzinger SY Fujimoto MA Clark MS Moreno EL Barrett, J Bacteriol 1995 177 2813 2820 7751291
    • (1995) J Bacteriol , vol.177 , pp. 2813-2820
    • Heinzinger, N.K.1    Fujimoto, S.Y.2    Clark, M.A.3    Moreno, M.S.4    Barrett, E.L.5
  • 37
    • 0025368948 scopus 로고
    • Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon
    • 2233673
    • Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon. F Blasco C Iobbi J Ratouchniak V Bonnefoy M Chippaux, Mol Gen Genet 1990 222 104 111 2233673
    • (1990) Mol Gen Genet , vol.222 , pp. 104-111
    • Blasco, F.1    Iobbi, C.2    Ratouchniak, J.3    Bonnefoy, V.4    Chippaux, M.5
  • 38
    • 0025912548 scopus 로고
    • Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes
    • 10.1007/BF00290984. 1781728
    • Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes. M Bokranz M Gutmann C Krötner E Kojro F Fahrenholz F Lauterbach A Kröger, Arch Microbiol 1991 156 119 128 10.1007/BF00290984 1781728
    • (1991) Arch Microbiol , vol.156 , pp. 119-128
    • Bokranz, M.1    Gutmann, M.2    Krötner, C.3    Kojro, E.4    Fahrenholz, F.5    Lauterbach, F.6    Kröger, A.7
  • 39
    • 0023988313 scopus 로고
    • NarI region of the Escherichia coli nitrate reductase (nar) operon contains two genes
    • 2832376
    • NarI region of the Escherichia coli nitrate reductase (nar) operon contains two genes. EJ Sodergren JA DeMoss, J Bacteriol 1988 170 1721 1729 2832376
    • (1988) J Bacteriol , vol.170 , pp. 1721-1729
    • Sodergren, E.J.1    Demoss, J.A.2
  • 40
    • 0032582701 scopus 로고    scopus 로고
    • Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport
    • 10.1074/jbc.273.44.28785. 9786877
    • Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport. MD Roldán HJ Sears MR Cheesman SJ Ferguson AJ Thomson BC Berks DJ Richardson, J Biol Chem 1998 273 28785 28790 10.1074/jbc.273.44.28785 9786877
    • (1998) J Biol Chem , vol.273 , pp. 28785-28790
    • Roldán, M.D.1    Sears, H.J.2    Cheesman, M.R.3    Ferguson, S.J.4    Thomson, A.J.5    Berks, B.C.6    Richardson, D.J.7
  • 41
    • 28644437016 scopus 로고    scopus 로고
    • A bacterial view of the periodic table: Genes and proteins for toxic inorganic ions
    • 10.1007/s10295-005-0019-6. 16133099
    • A bacterial view of the periodic table: genes and proteins for toxic inorganic ions. S Silver T Phung le, J Ind Microbiol Biotechnol 2005 32 11-12 587 605 10.1007/s10295-005-0019-6 16133099
    • (2005) J Ind Microbiol Biotechnol , vol.32 , Issue.11-12 , pp. 587-605
    • Silver, S.1    Le Phung, T.2
  • 42
    • 0027104536 scopus 로고
    • The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase
    • 1331097
    • The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase. GL Anderson J Williams R Hille, J Biol Chem 1992 267 23674 23682 1331097
    • (1992) J Biol Chem , vol.267 , pp. 23674-23682
    • Anderson, G.L.1    Williams, J.2    Hille, R.3
  • 43
    • 2642547186 scopus 로고    scopus 로고
    • Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: The arsenite oxidase and its physiological electron acceptor
    • 10.1016/j.bbabio.2004.03.001. 15178476
    • Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor. RN vanden Hoven JM Santini, Biochim Biophys Acta 2004 1656 148 155 10.1016/j.bbabio.2004.03.001 15178476
    • (2004) Biochim Biophys Acta , vol.1656 , pp. 148-155
    • Vanden, N.H.R.1    Santini, J.M.2
  • 45
    • 0023281247 scopus 로고
    • Thiosulfate reductase as a chlorate reductase in Salmonella typhimurium
    • Thiosulfate reductase as a chlorate reductase in Salmonella typhimurium. DL Riggs JS Tang EL Barret, FEMS Microbiol 1987 159 491 497
    • (1987) FEMS Microbiol , vol.159 , pp. 491-497
    • Riggs, D.L.1    Tang, J.S.2    Barret, E.L.3
  • 46
    • 33747790905 scopus 로고    scopus 로고
    • The oxygenation of the atmosphere and oceans
    • 16754606. 10.1098/rstb.2006.1838
    • The oxygenation of the atmosphere and oceans. HD Holland, Philos Trans R Soc Lond B Biol Sci 2006 361 903 915 16754606 10.1098/rstb.2006.1838
    • (2006) Philos Trans R Soc Lond B Biol Sci , vol.361 , pp. 903-915
    • Holland, H.D.1
  • 47
    • 33645776968 scopus 로고    scopus 로고
    • The evolutionary diversification of cyanobacteria: Molecular-phylogenetic and paleontological perspectives
    • 16569695. 10.1073/pnas.0600999103
    • The evolutionary diversification of cyanobacteria: molecular-phylogenetic and paleontological perspectives. A Tomitani AH Knoll CM Cavanaugh T Ohno, Proc Natl Acad Sci USA 2006 103 5442 5447 16569695 10.1073/pnas.0600999103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5442-5447
    • Tomitani, A.1    Knoll, A.H.2    Cavanaugh, C.M.3    Ohno, T.4
  • 49
    • 34548687408 scopus 로고    scopus 로고
    • Early archaeon microorganisms preferred elemental sulfur, not sulfate
    • 10.1126/science.1145861. 17872441
    • Early archaeon microorganisms preferred elemental sulfur, not sulfate. P Philippot M Van Zuilen K Lepot C Thomazo J Farquhar MJ Van Kranendonk, Science 2007 317 1534 1537 10.1126/science.1145861 17872441
    • (2007) Science , vol.317 , pp. 1534-1537
    • Philippot, P.1    Van Zuilen, M.2    Lepot, K.3    Thomazo, C.4    Farquhar, J.5    Van Kranendonk, M.J.6
  • 50
    • 33947183722 scopus 로고    scopus 로고
    • The CymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species
    • 17209025. 10.1128/JB.01698-06
    • The CymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species. JN Murphy CW Saltikov, J Bacteriol 2007 189 2283 2290 17209025 10.1128/JB.01698-06
    • (2007) J Bacteriol , vol.189 , pp. 2283-2290
    • Murphy, J.N.1    Saltikov, C.W.2
  • 51
    • 0042572520 scopus 로고    scopus 로고
    • The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis
    • 10.1021/bi034456f. 12899636
    • The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis. C Schwalb SK Chapman GA Reid, Biochemistry 2003 42 9491 9497 10.1021/bi034456f 12899636
    • (2003) Biochemistry , vol.42 , pp. 9491-9497
    • Schwalb, C.1    Chapman, S.K.2    Reid, G.A.3
  • 54
    • 33947186216 scopus 로고    scopus 로고
    • Alkalilimnicola ehrlichii sp. nov., a novel, arsenite-oxidizing haloalkaliphilic gammaproteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor
    • 10.1099/ijs.0.64576-0. 17329775
    • Alkalilimnicola ehrlichii sp. nov., a novel, arsenite-oxidizing haloalkaliphilic gammaproteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor. SE Hoeft JS Blum JF Stolz FR Tabita B Witte GM King JM Santini RS Oremland, Int J Syst Evol Microbiol 2007 57 504 512 10.1099/ijs.0.64576-0 17329775
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 504-512
    • Hoeft, S.E.1    Blum, J.S.2    Stolz, J.F.3    Tabita, F.R.4    Witte, B.5    King, G.M.6    Santini, J.M.7    Oremland, R.S.8
  • 56
    • 33745313750 scopus 로고    scopus 로고
    • Pdb database. http://www.rcsb.org/pdb/welcome.do
    • Pdb Database
  • 58
    • 49249121050 scopus 로고    scopus 로고
    • pSAAM package. http://www.life.uiuc.edu/crofts/ahab/psaam.html
    • PSAAM Package
  • 59
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 10.1093/nar/25.24.4876
    • The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. JD Thomson TJ Gilson F Plewniak F Jeanmougin DG Higgins, Nucleic Acid Res 1997 24 4876 4882 10.1093/nar/25.24.4876
    • (1997) Nucleic Acid Res , vol.24 , pp. 4876-4882
    • Thomson, J.D.1    Gilson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.