메뉴 건너뛰기




Volumn 17, Issue 12, 2015, Pages 4929-4941

Bioreactor microbial ecosystems for thiocyanate and cyanide degradation unravelled with genome-resolved metagenomics

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM DERIVATIVE; CARBON; CYANIDE; NITROGEN; SULFUR; SULFUR DERIVATIVE; THIOCYANATE; THIOCYANIC ACID DERIVATIVE; WASTE WATER;

EID: 84955628366     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/1462-2920.12936     Document Type: Article
Times cited : (90)

References (72)
  • 1
    • 33846799140 scopus 로고    scopus 로고
    • Structure of thiocyanate hydrolase: a new nitrile hydratase family protein with a novel five-coordinate cobalt(III) center
    • Arakawa, T., Kawano, Y., Kataoka, S., Katayama, Y., Kamiya, N., Yohda, M., and Odaka, M. (2007) Structure of thiocyanate hydrolase: a new nitrile hydratase family protein with a novel five-coordinate cobalt(III) center. J Mol Biol 366: 1497-1509.
    • (2007) J Mol Biol , vol.366 , pp. 1497-1509
    • Arakawa, T.1    Kawano, Y.2    Kataoka, S.3    Katayama, Y.4    Kamiya, N.5    Yohda, M.6    Odaka, M.7
  • 2
    • 32444438519 scopus 로고    scopus 로고
    • The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans
    • Beller, H.R., Chain, P.S.G., Letain, T.E., Chakicherla, A., Larimer, F.W., Richardson, P.M., etal. (2006) The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans. J Bacteriol 188: 1473-1488.
    • (2006) J Bacteriol , vol.188 , pp. 1473-1488
    • Beller, H.R.1    Chain, P.S.G.2    Letain, T.E.3    Chakicherla, A.4    Larimer, F.W.5    Richardson, P.M.6
  • 3
    • 36849049219 scopus 로고    scopus 로고
    • Thiocyanate hydrolase, the primary enzyme initiating thiocyanate degradation in the novel obligately chemolithoautotrophic halophilic sulfur-oxidizing bacterium Thiohalophilus thiocyanoxidans
    • Bezsudnova, E.Y., Sorokin, D.Y., Tikhonova, T.V., and Popov, V.O. (2007) Thiocyanate hydrolase, the primary enzyme initiating thiocyanate degradation in the novel obligately chemolithoautotrophic halophilic sulfur-oxidizing bacterium Thiohalophilus thiocyanoxidans. Biochim Biophys Acta 1774: 1563-1570.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1563-1570
    • Bezsudnova, E.Y.1    Sorokin, D.Y.2    Tikhonova, T.V.3    Popov, V.O.4
  • 5
    • 0028175077 scopus 로고
    • Microbial degradation of metal complexed cyanides and thiocyanate from mining wastewaters
    • Boucabeille, C., Bories, A., Ollivier, P., and Michel, G. (1994) Microbial degradation of metal complexed cyanides and thiocyanate from mining wastewaters. Environ Pollut 84: 59-67.
    • (1994) Environ Pollut , vol.84 , pp. 59-67
    • Boucabeille, C.1    Bories, A.2    Ollivier, P.3    Michel, G.4
  • 6
    • 84937766998 scopus 로고    scopus 로고
    • The ASTER process: technology development through to piloting, demonstration, and commercialization.
    • Proceedings of the ALTA 2011 Nickel-Cobalt-Copper, Uranium and Gold Conference, Perth, Australia.
    • van Buuren, C., Makhotla, N., and Olivier, J.W. (2011) The ASTER process: technology development through to piloting, demonstration, and commercialization. Proceedings of the ALTA 2011 Nickel-Cobalt-Copper, Uranium and Gold Conference, Perth, Australia.
    • (2011)
    • van Buuren, C.1    Makhotla, N.2    Olivier, J.W.3
  • 9
    • 77951703678 scopus 로고    scopus 로고
    • Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification
    • Cherney, M.M., Zhang, Y., Solomonson, M., Weiner, J.H., and James, M.N.G. (2010) Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification. J Mol Biol 398: 292-305.
    • (2010) J Mol Biol , vol.398 , pp. 292-305
    • Cherney, M.M.1    Zhang, Y.2    Solomonson, M.3    Weiner, J.H.4    James, M.N.G.5
  • 11
    • 34047225116 scopus 로고    scopus 로고
    • Common themes and variations in the rhodanese superfamily
    • Cipollone, R., Ascenzi, P., and Visca, P. (2007) Common themes and variations in the rhodanese superfamily. IUBMB Life 59: 51-59.
    • (2007) IUBMB Life , vol.59 , pp. 51-59
    • Cipollone, R.1    Ascenzi, P.2    Visca, P.3
  • 13
    • 0027267892 scopus 로고
    • Purification and properties of cyanide hydratase from Fusarium lateritium and analysis of the corresponding chy1 gene
    • Cluness, M.J., Turner, P.D., Clements, E., Brown, D.T., and O'Reilly, C. (1993) Purification and properties of cyanide hydratase from Fusarium lateritium and analysis of the corresponding chy1 gene. J Gen Microbiol 139: 1807-1815.
    • (1993) J Gen Microbiol , vol.139 , pp. 1807-1815
    • Cluness, M.J.1    Turner, P.D.2    Clements, E.3    Brown, D.T.4    O'Reilly, C.5
  • 15
    • 0030725851 scopus 로고    scopus 로고
    • Biological treatment of gold ore cyanidation wastewater in fixed bed reactors
    • Dictor, M.C., Battaglia-Brunet, F., Morin, D., Bories, A., and Clarens, M. (1997) Biological treatment of gold ore cyanidation wastewater in fixed bed reactors. Environ Pollut 97: 287-294.
    • (1997) Environ Pollut , vol.97 , pp. 287-294
    • Dictor, M.C.1    Battaglia-Brunet, F.2    Morin, D.3    Bories, A.4    Clarens, M.5
  • 16
    • 3042666256 scopus 로고    scopus 로고
    • Muscle: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. (2004) Muscle: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 17
    • 77957244650 scopus 로고    scopus 로고
    • Search and clustering orders of magnitude faster than BLAST
    • Edgar, R.C. (2010) Search and clustering orders of magnitude faster than BLAST. Bioinformatics 26: 2460-2461.
    • (2010) Bioinformatics , vol.26 , pp. 2460-2461
    • Edgar, R.C.1
  • 18
    • 3042746490 scopus 로고    scopus 로고
    • Thiocyanate overload and thyroid disease
    • Erdogan, M.F. (2003) Thiocyanate overload and thyroid disease. Biofactors 19: 107-111.
    • (2003) Biofactors , vol.19 , pp. 107-111
    • Erdogan, M.F.1
  • 19
    • 76049112484 scopus 로고    scopus 로고
    • Polyphasic bacterial community analysis of an aerobic activated sludge removing phenols and thiocyanate from coke plant effluent
    • Felföldi, T., Székely, A.J., Gorál, R., Barkács, K., Scheirich, G., András, J., etal. (2010) Polyphasic bacterial community analysis of an aerobic activated sludge removing phenols and thiocyanate from coke plant effluent. Bioresour Technol 101: 3406-3414.
    • (2010) Bioresour Technol , vol.101 , pp. 3406-3414
    • Felföldi, T.1    Székely, A.J.2    Gorál, R.3    Barkács, K.4    Scheirich, G.5    András, J.6
  • 20
    • 24944573053 scopus 로고    scopus 로고
    • Bacterial cyanide oxygenase is a suite of enzymes catalyzing the scavenging and adventitious utilization of cyanide as a nitrogenous growth substrate
    • Fernandez, R.F., and Kunz, D.A. (2005) Bacterial cyanide oxygenase is a suite of enzymes catalyzing the scavenging and adventitious utilization of cyanide as a nitrogenous growth substrate. J Bacteriol 187: 6396-6402.
    • (2005) J Bacteriol , vol.187 , pp. 6396-6402
    • Fernandez, R.F.1    Kunz, D.A.2
  • 21
    • 0033973913 scopus 로고    scopus 로고
    • 2O-producing Xanthomonas-like isolates from biofilters as Stenotrophomonas nitritireducens sp. nov., Luteimonas mephitis gen. nov., sp. nov. and Pseudoxanthomonas broegbernensis gen. nov., sp. nov
    • 2O-producing Xanthomonas-like isolates from biofilters as Stenotrophomonas nitritireducens sp. nov., Luteimonas mephitis gen. nov., sp. nov. and Pseudoxanthomonas broegbernensis gen. nov., sp. nov. Int J Syst Evol Microbiol 50 (Part 1): 273-282.
    • (2000) Int J Syst Evol Microbiol , vol.50 , pp. 273-282
    • Finkmann, W.1    Altendorf, K.2    Stackebrandt, E.3    Lipski, A.4
  • 24
    • 77952511174 scopus 로고    scopus 로고
    • Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family
    • Haft, D.H., Basu, M.K., and Mitchell, D.A. (2010) Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family. BMC Biol 8: 70.
    • (2010) BMC Biol , vol.8 , pp. 70
    • Haft, D.H.1    Basu, M.K.2    Mitchell, D.A.3
  • 25
    • 84937758588 scopus 로고    scopus 로고
    • Characterisation of the complex microbial community associated with the ASTER™ thiocyanate biodegradation system
    • Huddy, R.J., van Zyl, A.W., van Hille, R.P., and Harrison, S.T.L. (2015) Characterisation of the complex microbial community associated with the ASTER™ thiocyanate biodegradation system. Miner Eng 76: 65-71.
    • (2015) Miner Eng , vol.76 , pp. 65-71
    • Huddy, R.J.1    van Zyl, A.W.2    van Hille, R.P.3    Harrison, S.T.L.4
  • 26
    • 84867609258 scopus 로고    scopus 로고
    • Comparative metagenomics of three Dehalococcoides-containing enrichment cultures: the role of the non-dechlorinating community
    • Hug, L.A., Beiko, R.G., Rowe, A.R., Richardson, R.E., and Edwards, E.A. (2012) Comparative metagenomics of three Dehalococcoides-containing enrichment cultures: the role of the non-dechlorinating community. BMC Genomics 13: 327.
    • (2012) BMC Genomics , vol.13 , pp. 327
    • Hug, L.A.1    Beiko, R.G.2    Rowe, A.R.3    Richardson, R.E.4    Edwards, E.A.5
  • 27
    • 84903383681 scopus 로고    scopus 로고
    • Community genomic analyses constrain the distribution of metabolic traits across the Chloroflexi phylum and indicate roles in sediment carbon cycling
    • Hug, L.A., Castelle, C.J., Wrighton, K.C., Thomas, B.C., Sharon, I., Frischkorn, K.R., etal. (2013) Community genomic analyses constrain the distribution of metabolic traits across the Chloroflexi phylum and indicate roles in sediment carbon cycling. Microbiome 1: 22.
    • (2013) Microbiome , vol.1 , pp. 22
    • Hug, L.A.1    Castelle, C.J.2    Wrighton, K.C.3    Thomas, B.C.4    Sharon, I.5    Frischkorn, K.R.6
  • 28
    • 0033524367 scopus 로고    scopus 로고
    • Kinetics and modeling of autotrophic thiocyanate biodegradation
    • Hung, C.-H., and Pavlostathis, S.G. (1999) Kinetics and modeling of autotrophic thiocyanate biodegradation. Biotechnol Bioeng 62: 1-11.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 1-11
    • Hung, C.-H.1    Pavlostathis, S.G.2
  • 29
    • 84886705273 scopus 로고    scopus 로고
    • Cloning and expression of a gene encoding a novel thermostable thiocyanate-degrading enzyme from a mesophilic alphaproteobacteria strain THI201
    • Hussain, A., Ogawa, T., Saito, M., Sekine, T., Nameki, M., Matsushita, Y., etal. (2013) Cloning and expression of a gene encoding a novel thermostable thiocyanate-degrading enzyme from a mesophilic alphaproteobacteria strain THI201. Microbiology 159: 2294-2302.
    • (2013) Microbiology , vol.159 , pp. 2294-2302
    • Hussain, A.1    Ogawa, T.2    Saito, M.3    Sekine, T.4    Nameki, M.5    Matsushita, Y.6
  • 31
    • 84865561269 scopus 로고    scopus 로고
    • Gene and translation initiation site prediction in metagenomic sequences
    • Hyatt, D., Locascio, P.F., Hauser, L.J., and Uberbacher, E.C. (2012) Gene and translation initiation site prediction in metagenomic sequences. Bioinformatics 28: 2223-2230.
    • (2012) Bioinformatics , vol.28 , pp. 2223-2230
    • Hyatt, D.1    Locascio, P.F.2    Hauser, L.J.3    Uberbacher, E.C.4
  • 34
    • 79955058143 scopus 로고    scopus 로고
    • Convergent evolution in biosynthesis of cyanogenic defence compounds in plants and insects
    • Jensen, N.B., Zagrobelny, M., Hjernø, K., Olsen, C.E., Houghton-Larsen, J., Borch, J., etal. (2011) Convergent evolution in biosynthesis of cyanogenic defence compounds in plants and insects. Nat Commun 2: 273.
    • (2011) Nat Commun , vol.2 , pp. 273
    • Jensen, N.B.1    Zagrobelny, M.2    Hjernø, K.3    Olsen, C.E.4    Houghton-Larsen, J.5    Borch, J.6
  • 35
    • 33746918762 scopus 로고    scopus 로고
    • Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K
    • Kataoka, S., Arakawa, T., Hori, S., Katayama, Y., Hara, Y., Matsushita, Y., etal. (2006) Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K. FEBS Lett 580: 4667-4672.
    • (2006) FEBS Lett , vol.580 , pp. 4667-4672
    • Kataoka, S.1    Arakawa, T.2    Hori, S.3    Katayama, Y.4    Hara, Y.5    Matsushita, Y.6
  • 36
    • 0031924251 scopus 로고    scopus 로고
    • Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase
    • Katayama, Y., Matsushita, Y., Kaneko, M., Kondo, M., Mizuno, T., and Nyunoya, H. (1998) Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase. J Bacteriol 180: 2583-2589.
    • (1998) J Bacteriol , vol.180 , pp. 2583-2589
    • Katayama, Y.1    Matsushita, Y.2    Kaneko, M.3    Kondo, M.4    Mizuno, T.5    Nyunoya, H.6
  • 37
    • 65549128998 scopus 로고    scopus 로고
    • Eukaryotic nirK genes encoding copper-containing nitrite reductase: originating from the protomitochondrion?
    • Kim, S.-W., Fushinobu, S., Zhou, S., Wakagi, T., and Shoun, H. (2009) Eukaryotic nirK genes encoding copper-containing nitrite reductase: originating from the protomitochondrion? Appl Environ Microbiol 75: 2652-2658.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2652-2658
    • Kim, S.-W.1    Fushinobu, S.2    Zhou, S.3    Wakagi, T.4    Shoun, H.5
  • 38
    • 84905901158 scopus 로고    scopus 로고
    • The environmental controls that govern the end product of bacterial nitrate respiration
    • Kraft, B., Tegetmeyer, H.E., Sharma, R., Klotz, M.G., Ferdelman, T.G., Hettich, R.L., etal. (2014) The environmental controls that govern the end product of bacterial nitrate respiration. Science 345: 676-679.
    • (2014) Science , vol.345 , pp. 676-679
    • Kraft, B.1    Tegetmeyer, H.E.2    Sharma, R.3    Klotz, M.G.4    Ferdelman, T.G.5    Hettich, R.L.6
  • 39
    • 84859210032 scopus 로고    scopus 로고
    • Fast gapped-read alignment with Bowtie 2
    • Langmead, B., and Salzberg, S.L. (2012) Fast gapped-read alignment with Bowtie 2. Nat Methods 9: 357-359.
    • (2012) Nat Methods , vol.9 , pp. 357-359
    • Langmead, B.1    Salzberg, S.L.2
  • 40
    • 54949114344 scopus 로고    scopus 로고
    • Characterization of the Pseudomonas pseudoalcaligenes CECT5344 Cyanase, an enzyme that is not essential for cyanide assimilation
    • Luque-Almagro, V.M., Huertas, M.-J., Sáez, L.P., Luque-Romero, M.M., Moreno Vivián, C., Castillo, F., etal. (2008) Characterization of the Pseudomonas pseudoalcaligenes CECT5344 Cyanase, an enzyme that is not essential for cyanide assimilation. Appl Environ Microbiol 74: 6280-6288.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6280-6288
    • Luque-Almagro, V.M.1    Huertas, M.-J.2    Sáez, L.P.3    Luque-Romero, M.M.4    Moreno Vivián, C.5    Castillo, F.6
  • 41
    • 79952259001 scopus 로고    scopus 로고
    • Cyanide degradation by Pseudomonas pseudoalcaligenes CECT5344 involves a malate: quinone oxidoreductase and an associated cyanide-insensitive electron transfer chain
    • Luque-Almagro, V.M., Merchan, F., Blasco, R., Igeno, M.I., Martínez-Luque, M., Moreno-Vivián, C., etal. (2011) Cyanide degradation by Pseudomonas pseudoalcaligenes CECT5344 involves a malate: quinone oxidoreductase and an associated cyanide-insensitive electron transfer chain. Microbiology 157: 739-746.
    • (2011) Microbiology , vol.157 , pp. 739-746
    • Luque-Almagro, V.M.1    Merchan, F.2    Blasco, R.3    Igeno, M.I.4    Martínez-Luque, M.5    Moreno-Vivián, C.6
  • 42
    • 78650601515 scopus 로고    scopus 로고
    • Multiple syntrophic interactions in a terephthalate-degrading methanogenic consortium
    • Lykidis, A., Chen, C.-L., Tringe, S.G., McHardy, A.C., Copeland, A., Kyrpides, N.C., etal. (2010) Multiple syntrophic interactions in a terephthalate-degrading methanogenic consortium. ISME J 5: 122-130.
    • (2010) ISME J , vol.5 , pp. 122-130
    • Lykidis, A.1    Chen, C.-L.2    Tringe, S.G.3    McHardy, A.C.4    Copeland, A.5    Kyrpides, N.C.6
  • 43
    • 67649872642 scopus 로고    scopus 로고
    • The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2009) The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106: 9625-9630.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9625-9630
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 44
    • 77951225834 scopus 로고    scopus 로고
    • A new structure-based classification of sulfide:quinone oxidoreductases
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2010) A new structure-based classification of sulfide:quinone oxidoreductases. Proteins 78: 1073-1083.
    • (2010) Proteins , vol.78 , pp. 1073-1083
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 46
    • 84874988656 scopus 로고    scopus 로고
    • Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is one of the β-carbonic anhydrase family enzymes
    • Ogawa, T., Noguchi, K., Saito, M., Nagahata, Y., Kato, H., Ohtaki, A., etal. (2013) Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is one of the β-carbonic anhydrase family enzymes. J Am Chem Soc 135: 3818-3825.
    • (2013) J Am Chem Soc , vol.135 , pp. 3818-3825
    • Ogawa, T.1    Noguchi, K.2    Saito, M.3    Nagahata, Y.4    Kato, H.5    Ohtaki, A.6
  • 47
    • 0035114118 scopus 로고    scopus 로고
    • The nitrilase superfamily: classification, structure and function
    • REVIEWS0001
    • Pace, H.C., and Brenner, C. (2001) The nitrilase superfamily: classification, structure and function. Genome Biol 2: REVIEWS0001.
    • (2001) Genome Biol , vol.2
    • Pace, H.C.1    Brenner, C.2
  • 48
    • 84861760530 scopus 로고    scopus 로고
    • IDBA-UD: a de novo assembler for single-cell and metagenomic sequencing data with highly uneven depth
    • Peng, Y., Leung, H.C.M., Yiu, S.M., and Chin, F.Y.L. (2012) IDBA-UD: a de novo assembler for single-cell and metagenomic sequencing data with highly uneven depth. Bioinformatics 28: 1420-1428.
    • (2012) Bioinformatics , vol.28 , pp. 1420-1428
    • Peng, Y.1    Leung, H.C.M.2    Yiu, S.M.3    Chin, F.Y.L.4
  • 49
    • 0035134348 scopus 로고    scopus 로고
    • Empirical model for the autotrophic biodegradation of thiocyanate in an activated sludge reactor
    • du Plessis, C.A., Barnard, P., Muhlbauer, R.M., and Naldrett, K. (2001) Empirical model for the autotrophic biodegradation of thiocyanate in an activated sludge reactor. Lett Appl Microbiol 32: 103-107.
    • (2001) Lett Appl Microbiol , vol.32 , pp. 103-107
    • du Plessis, C.A.1    Barnard, P.2    Muhlbauer, R.M.3    Naldrett, K.4
  • 50
    • 33646758598 scopus 로고    scopus 로고
    • Bacterial community structure in activated sludge reactors treating free or metal-complexed cyanides
    • Quan, Z.X., Rhee, S.K., Bae, J.W., Baek, J.H., Park, Y.H., and Lee, S.T. (2006) Bacterial community structure in activated sludge reactors treating free or metal-complexed cyanides. J Microbiol Biotechnol 16: 232-239.
    • (2006) J Microbiol Biotechnol , vol.16 , pp. 232-239
    • Quan, Z.X.1    Rhee, S.K.2    Bae, J.W.3    Baek, J.H.4    Park, Y.H.5    Lee, S.T.6
  • 51
    • 84871956840 scopus 로고    scopus 로고
    • Time series community genomics analysis reveals rapid shifts in bacterial species, strains, and phage during infant gut colonization
    • Sharon, I., Morowitz, M.J., Thomas, B.C., Costello, E.K., Relman, D.A., and Banfield, J.F. (2013) Time series community genomics analysis reveals rapid shifts in bacterial species, strains, and phage during infant gut colonization. Genome Res 23: 111-120.
    • (2013) Genome Res , vol.23 , pp. 111-120
    • Sharon, I.1    Morowitz, M.J.2    Thomas, B.C.3    Costello, E.K.4    Relman, D.A.5    Banfield, J.F.6
  • 53
    • 4344621662 scopus 로고    scopus 로고
    • Anaerobic growth of the haloalkaliphilic denitrifying sulfur-oxidizing bacterium Thialkalivibrio thiocyanodenitrificans sp. nov. with thiocyanate
    • Sorokin, D.Y., Tourova, T.P., Antipov, A.N., Muyzer, G., and Kuenen, J.G. (2004) Anaerobic growth of the haloalkaliphilic denitrifying sulfur-oxidizing bacterium Thialkalivibrio thiocyanodenitrificans sp. nov. with thiocyanate. Microbiology 150: 2435-2442.
    • (2004) Microbiology , vol.150 , pp. 2435-2442
    • Sorokin, D.Y.1    Tourova, T.P.2    Antipov, A.N.3    Muyzer, G.4    Kuenen, J.G.5
  • 54
    • 34249098465 scopus 로고    scopus 로고
    • Denitrification in a binary culture and thiocyanate metabolism in Thiohalophilus thiocyanoxidans gen. nov. sp. nov. - a moderately halophilic chemolithoautotrophic sulfur-oxidizing Gammaproteobacterium from hypersaline lakes
    • Sorokin, D.Y., Tourova, T.P., Bezsoudnova, E.Y., Pol, A., and Muyzer, G. (2007) Denitrification in a binary culture and thiocyanate metabolism in Thiohalophilus thiocyanoxidans gen. nov. sp. nov. - a moderately halophilic chemolithoautotrophic sulfur-oxidizing Gammaproteobacterium from hypersaline lakes. Arch Microbiol 187: 441-450.
    • (2007) Arch Microbiol , vol.187 , pp. 441-450
    • Sorokin, D.Y.1    Tourova, T.P.2    Bezsoudnova, E.Y.3    Pol, A.4    Muyzer, G.5
  • 55
    • 84864717257 scopus 로고    scopus 로고
    • Thioalkalivibrio sulfidiphilus sp. nov., a haloalkaliphilic, sulfur-oxidizing gammaproteobacterium from alkaline habitats
    • Sorokin, D.Y., Muntyan, M.S., Panteleeva, A.N., and Muyzer, G. (2012) Thioalkalivibrio sulfidiphilus sp. nov., a haloalkaliphilic, sulfur-oxidizing gammaproteobacterium from alkaline habitats. Int J Syst Evol Microbiol 62: 1884-1889.
    • (2012) Int J Syst Evol Microbiol , vol.62 , pp. 1884-1889
    • Sorokin, D.Y.1    Muntyan, M.S.2    Panteleeva, A.N.3    Muyzer, G.4
  • 56
    • 0023718189 scopus 로고
    • The acute toxicity of thiocyanate and cyanate to rainbow trout as modified by water temperature and pH
    • Speyer, M.R., and Raymond, P. (1988) The acute toxicity of thiocyanate and cyanate to rainbow trout as modified by water temperature and pH. Environ Toxicol Chem 7: 565-571.
    • (1988) Environ Toxicol Chem , vol.7 , pp. 565-571
    • Speyer, M.R.1    Raymond, P.2
  • 57
    • 0035477384 scopus 로고    scopus 로고
    • Thiocyanate removal from saline CIP process water by a rotating biological contactor, with reuse of the water for bioleaching
    • Stott, M.B., Franzmann, P.D., Zappia, L.R., Watling, H.R., Quan, L.P., Clark, B.J., etal. (2001) Thiocyanate removal from saline CIP process water by a rotating biological contactor, with reuse of the water for bioleaching. Hydrometallurgy 62: 93-105.
    • (2001) Hydrometallurgy , vol.62 , pp. 93-105
    • Stott, M.B.1    Franzmann, P.D.2    Zappia, L.R.3    Watling, H.R.4    Quan, L.P.5    Clark, B.J.6
  • 58
    • 0028127220 scopus 로고
    • The utilization of thiocyanate as a nitrogen source by a heterotrophic bacterium: the degradative pathway involves formation of ammonia and tetrathionate
    • Stratford, J., Dias, A.E., and Knowles, C.J. (1994) The utilization of thiocyanate as a nitrogen source by a heterotrophic bacterium: the degradative pathway involves formation of ammonia and tetrathionate. Microbiology 140: 2657-2662.
    • (1994) Microbiology , vol.140 , pp. 2657-2662
    • Stratford, J.1    Dias, A.E.2    Knowles, C.J.3
  • 59
    • 0023790390 scopus 로고
    • Characterization of the cyn operon in Escherichia coli K12
    • Sung, Y.C., and Fuchs, J.A. (1988) Characterization of the cyn operon in Escherichia coli K12. J Biol Chem 263: 14769-14775.
    • (1988) J Biol Chem , vol.263 , pp. 14769-14775
    • Sung, Y.C.1    Fuchs, J.A.2
  • 60
    • 0026680444 scopus 로고
    • The Escherichia coli K-12 cyn operon is positively regulated by a member of the lysR family
    • Sung, Y.C., and Fuchs, J.A. (1992) The Escherichia coli K-12 cyn operon is positively regulated by a member of the lysR family. J Bacteriol 174: 3645-3650.
    • (1992) J Bacteriol , vol.174 , pp. 3645-3650
    • Sung, Y.C.1    Fuchs, J.A.2
  • 61
    • 34347388470 scopus 로고    scopus 로고
    • UniRef: comprehensive and non-redundant UniProt reference clusters
    • Suzek, B.E., Huang, H., McGarvey, P., Mazumder, R., and Wu, C.H. (2007) UniRef: comprehensive and non-redundant UniProt reference clusters. Bioinformatics 23: 1282-1288.
    • (2007) Bioinformatics , vol.23 , pp. 1282-1288
    • Suzek, B.E.1    Huang, H.2    McGarvey, P.3    Mazumder, R.4    Wu, C.H.5
  • 62
    • 60049084739 scopus 로고    scopus 로고
    • Microbial nitrilases: versatile, spiral forming, industrial enzymes
    • Thuku, R.N., Brady, D., Benedik, M.J., and Sewell, B.T. (2009) Microbial nitrilases: versatile, spiral forming, industrial enzymes. J Appl Microbiol 106: 703-727.
    • (2009) J Appl Microbiol , vol.106 , pp. 703-727
    • Thuku, R.N.1    Brady, D.2    Benedik, M.J.3    Sewell, B.T.4
  • 63
    • 84884703068 scopus 로고    scopus 로고
    • Biodegradation of thiocyanate by a novel strain of Burkholderia phytofirmans from soil contaminated by gold mine tailings
    • Vu, H.P., Mu, A., and Moreau, J.W. (2013) Biodegradation of thiocyanate by a novel strain of Burkholderia phytofirmans from soil contaminated by gold mine tailings. Lett Appl Microbiol 57: 368-372.
    • (2013) Lett Appl Microbiol , vol.57 , pp. 368-372
    • Vu, H.P.1    Mu, A.2    Moreau, J.W.3
  • 64
    • 0034657184 scopus 로고    scopus 로고
    • Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site
    • Walsh, M.A., Otwinowski, Z., Perrakis, A., Anderson, P.M., and Joachimiak, A. (2000) Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Structure 8: 505-514.
    • (2000) Structure , vol.8 , pp. 505-514
    • Walsh, M.A.1    Otwinowski, Z.2    Perrakis, A.3    Anderson, P.M.4    Joachimiak, A.5
  • 65
    • 0026794444 scopus 로고
    • Cloning and properties of a cyanide hydratase gene from the phytopathogenic fungus Gloeocercospora sorghi
    • Wang, P., and VanEtten, H.D. (1992) Cloning and properties of a cyanide hydratase gene from the phytopathogenic fungus Gloeocercospora sorghi. Biochem Biophys Res Commun 187: 1048-1054.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 1048-1054
    • Wang, P.1    VanEtten, H.D.2
  • 66
    • 0023256138 scopus 로고
    • Thiocyanate toxicity to Daphnia magna: modified by pH and temperature
    • Watson, S.J., and Maly, E.J. (1987) Thiocyanate toxicity to Daphnia magna: modified by pH and temperature. Aquat Toxicol 10: 1-8.
    • (1987) Aquat Toxicol , vol.10 , pp. 1-8
    • Watson, S.J.1    Maly, E.J.2
  • 67
    • 0031934387 scopus 로고    scopus 로고
    • A novel pink-pigmented facultative methylotroph, Methylobacterium thiocyanatum sp. nov., capable of growth on thiocyanate or cyanate as sole nitrogen sources
    • Wood, A.P., Kelly, D.P., McDonald, I.R., Jordan, S.L., Morgan, T.D., Khan, S., etal. (1998) A novel pink-pigmented facultative methylotroph, Methylobacterium thiocyanatum sp. nov., capable of growth on thiocyanate or cyanate as sole nitrogen sources. Arch Microbiol 169: 148-158.
    • (1998) Arch Microbiol , vol.169 , pp. 148-158
    • Wood, A.P.1    Kelly, D.P.2    McDonald, I.R.3    Jordan, S.L.4    Morgan, T.D.5    Khan, S.6
  • 69
    • 84878192639 scopus 로고    scopus 로고
    • Two arginine residues in the substrate pocket predominantly control the substrate selectivity of thiocyanate hydrolase
    • Yamanaka, Y., Arakawa, T., Watanabe, T., Namima, S., Sato, M., Hori, S., etal. (2013) Two arginine residues in the substrate pocket predominantly control the substrate selectivity of thiocyanate hydrolase. J Biosci Bioeng 116: 22-27.
    • (2013) J Biosci Bioeng , vol.116 , pp. 22-27
    • Yamanaka, Y.1    Arakawa, T.2    Watanabe, T.3    Namima, S.4    Sato, M.5    Hori, S.6
  • 70
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu, N.Y., Wagner, J.R., Laird, M.R., Melli, G., Rey, S., Lo, R., etal. (2010) PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26: 1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6
  • 71
    • 84905977826 scopus 로고    scopus 로고
    • Biodegradation of thiocyanate by a mixed microbial population.
    • Proceedings of the International Mine Water Association Conference, Aachen, Germany, 2011
    • van Zyl, A.W., Harrison, S.T.L., and van Hille, R.P. (2011) Biodegradation of thiocyanate by a mixed microbial population. Proceedings of the International Mine Water Association Conference, Aachen, Germany, 2011, pp. 119-124.
    • (2011) , pp. 119-124
    • van Zyl, A.W.1    Harrison, S.T.L.2    van Hille, R.P.3
  • 72
    • 84939945876 scopus 로고    scopus 로고
    • Evaluation of the ASTER™ process in the presence of suspended solids
    • van Zyl, A.W., Huddy, R.J., Harrison, S.T.L., and van Hille, R.P. (2015) Evaluation of the ASTER™ process in the presence of suspended solids. Miner Eng 76: 72-80.
    • (2015) Miner Eng , vol.76 , pp. 72-80
    • van Zyl, A.W.1    Huddy, R.J.2    Harrison, S.T.L.3    van Hille, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.