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Volumn 81, Issue 15, 2015, Pages 5003-5014

Comparative analysis of denitrifying activities of Hyphomicrobium nitrativorans, Hyphomicrobium denitrificans, and Hyphomicrobium zavarzinii

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ENZYME ACTIVITY; GENE ENCODING; GENE EXPRESSION; GENE EXPRESSION REGULATION; NITRATES; NITRATION; SODIUM CHLORIDE;

EID: 84936980942     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00848-15     Document Type: Article
Times cited : (135)

References (62)
  • 2
    • 0031967850 scopus 로고    scopus 로고
    • Distribution of denitrification and nitrogen fixation genes in Hyphomicrobium spp. and other budding bacteria
    • Fesefeldt A, Kloos K, Bothe H, Lemmer H, Gliesche CG. 1998. Distribution of denitrification and nitrogen fixation genes in Hyphomicrobium spp. and other budding bacteria. Can J Microbiol 44:181-186. http://dx.doi.org/10.1139/w97-139.
    • (1998) Can J Microbiol , vol.44 , pp. 181-186
    • Fesefeldt, A.1    Kloos, K.2    Bothe, H.3    Lemmer, H.4    Gliesche, C.G.5
  • 3
    • 0028787903 scopus 로고
    • DNA-probing indicates the occurrence of denitrification and nitrogen fixation genes in Hyphomicrobium. Distribution of denitrifying and nitrogen fixing isolates of Hyphomicrobium in a sewage treatment plant
    • Kloos K, Fesefeldt A, Gliesche CG, Bothe H. 1995. DNA-probing indicates the occurrence of denitrification and nitrogen fixation genes in Hyphomicrobium. Distribution of denitrifying and nitrogen fixing isolates of Hyphomicrobium in a sewage treatment plant. FEMS Microbiol Ecol 18:205-213. http://dx.doi.org/10.1111/j.1574-6941.1995.tb00177.x.
    • (1995) FEMS Microbiol Ecol , vol.18 , pp. 205-213
    • Kloos, K.1    Fesefeldt, A.2    Gliesche, C.G.3    Bothe, H.4
  • 4
    • 0020850328 scopus 로고
    • Denitrification with methanol: fundamental study of the growth and denitrification capacity of Hyphomicrobium sp
    • Timmermans P, Van Haute A. 1983. Denitrification with methanol: fundamental study of the growth and denitrification capacity of Hyphomicrobium sp. Water Res 17:1249-1255. http://dx.doi.org/10.1016/0043-1354(83)90249-X.
    • (1983) Water Res , vol.17 , pp. 1249-1255
    • Timmermans, P.1    Van Haute, A.2
  • 5
    • 0029007133 scopus 로고
    • Characterization and description of Hyphomicrobium denitrificans sp. nov
    • Urakami T, Sasaki J, Suzuki K-I, Komagata K. 1995. Characterization and description of Hyphomicrobium denitrificans sp. nov. Int J Syst Bacteriol 45:528-532. http://dx.doi.org/10.1099/00207713-45-3-528.
    • (1995) Int J Syst Bacteriol , vol.45 , pp. 528-532
    • Urakami, T.1    Sasaki, J.2    Suzuki, K.-I.3    Komagata, K.4
  • 6
    • 0017833397 scopus 로고
    • Biology, physiology and biochemistry of Hyphomicrobia
    • Harder W, Attwood MM. 1978. Biology, physiology and biochemistry of Hyphomicrobia. Adv Microb Physiol 17:303-359. http://dx.doi.org/10.1016/S0065-2911(08)60060-0.
    • (1978) Adv Microb Physiol , vol.17 , pp. 303-359
    • Harder, W.1    Attwood, M.M.2
  • 7
    • 65349194992 scopus 로고    scopus 로고
    • Impact of varying electron donors on the molecular microbial ecology and biokinetics of methylotrophic denitrifying bacteria
    • Baytshtok V, Lu H, Park H, Kim S, Yu R, Chandran K. 2009. Impact of varying electron donors on the molecular microbial ecology and biokinetics of methylotrophic denitrifying bacteria. Biotechnol Bioeng 102:1527-1536. http://dx.doi.org/10.1002/bit.22213.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1527-1536
    • Baytshtok, V.1    Lu, H.2    Park, H.3    Kim, S.4    Yu, R.5    Chandran, K.6
  • 8
    • 33745774127 scopus 로고    scopus 로고
    • Community structures and activities of nitrifying and denitrifying bacteria in industrial wastewater-treating biofilms
    • Satoh H, Yamakawa T, Kindaichi T, Ito T, Okabe S. 2006. Community structures and activities of nitrifying and denitrifying bacteria in industrial wastewater-treating biofilms. Biotechnol Bioeng 94:762-772. http://dx.doi.org/10.1002/bit.20894.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 762-772
    • Satoh, H.1    Yamakawa, T.2    Kindaichi, T.3    Ito, T.4    Okabe, S.5
  • 9
    • 84865968220 scopus 로고    scopus 로고
    • High-rate denitrification using polyethylene glycol gel carriers entrapping heterotrophic denitrifying bacteria
    • Isaka K, Kimura Y, Osaka T, Tsuneda S. 2012. High-rate denitrification using polyethylene glycol gel carriers entrapping heterotrophic denitrifying bacteria. Water Res 46:4941-4948. http://dx.doi.org/10.1016/j.watres.2012.05.050.
    • (2012) Water Res , vol.46 , pp. 4941-4948
    • Isaka, K.1    Kimura, Y.2    Osaka, T.3    Tsuneda, S.4
  • 10
    • 52949102549 scopus 로고    scopus 로고
    • Molecular and biokinetic characterization of methylotrophic denitrification using nitrate and nitrite as terminal electron acceptors
    • Baytshtok V, Kim S, Yu R, Park H, Chandran K. 2008. Molecular and biokinetic characterization of methylotrophic denitrification using nitrate and nitrite as terminal electron acceptors. Water Sci Technol 58(2):359-365. http://dx.doi.org/10.2166/wst.2008.391.
    • (2008) Water Sci Technol , vol.58 , Issue.2 , pp. 359-365
    • Baytshtok, V.1    Kim, S.2    Yu, R.3    Park, H.4    Chandran, K.5
  • 11
    • 0020064009 scopus 로고
    • Denitrification
    • Knowles R. 1982. Denitrification. Microbiol Rev 46:43-70.
    • (1982) Microbiol Rev , vol.46 , pp. 43-70
    • Knowles, R.1
  • 12
    • 0037184270 scopus 로고    scopus 로고
    • Denitrifying genes in bacterial and archaeal genomes
    • Philippot L. 2002. Denitrifying genes in bacterial and archaeal genomes. Biochim Biophys Acta 1577:355-376. http://dx.doi.org/10.1016/S0167-4781(02)00420-7.
    • (2002) Biochim Biophys Acta , vol.1577 , pp. 355-376
    • Philippot, L.1
  • 13
    • 0035107176 scopus 로고    scopus 로고
    • Functional, biochemical and genetic diversity of prokaryotic nitrate reductases
    • Richardson DJ, Berks BC, Russell DA, Spiro S, Taylor CJ. 2001. Functional, biochemical and genetic diversity of prokaryotic nitrate reductases. Cell Mol Life Sci 58:165-178. http://dx.doi.org/10.1007/PL00000845.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 165-178
    • Richardson, D.J.1    Berks, B.C.2    Russell, D.A.3    Spiro, S.4    Taylor, C.J.5
  • 14
    • 79953239813 scopus 로고    scopus 로고
    • Microbial nitrate respiration-genes, enzymes and environmental distribution
    • Kraft B, Strous M, Tegetmeyer HE. 2011. Microbial nitrate respiration-genes, enzymes and environmental distribution. J Biotechnol 155:104-117. http://dx.doi.org/10.1016/j.jbiotec.2010.12.025.
    • (2011) J Biotechnol , vol.155 , pp. 104-117
    • Kraft, B.1    Strous, M.2    Tegetmeyer, H.E.3
  • 15
    • 0037173555 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of Cu-containing nitrite reductase from Hyphomicrobium denitrificans A3151
    • Deligeer, Fukunaga R, Kataoka K, Yamaguchi K, Kobayashi K, Tagawa S, Suzuki S. 2002. Spectroscopic and functional characterization of Cu-containing nitrite reductase from Hyphomicrobium denitrificans A3151. J Inorg Biochem 91:132-138. http://dx.doi.org/10.1016/S0162-0134(02)00442-7.
    • (2002) J Inorg Biochem , vol.91 , pp. 132-138
    • Deligeer1    Fukunaga, R.2    Kataoka, K.3    Yamaguchi, K.4    Kobayashi, K.5    Tagawa, S.6    Suzuki, S.7
  • 16
    • 8444245920 scopus 로고    scopus 로고
    • Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: a new class of copper-containing nitrite reductases
    • Yamaguchi K, Kataoka K, Kobayashi M, Itoh K, Fukui A, Suzuki S. 2004. Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: a new class of copper-containing nitrite reductases. Biochemistry 43:14180-14188. http://dx.doi.org/10.1021/bi0492657.
    • (2004) Biochemistry , vol.43 , pp. 14180-14188
    • Yamaguchi, K.1    Kataoka, K.2    Kobayashi, M.3    Itoh, K.4    Fukui, A.5    Suzuki, S.6
  • 18
    • 1342304268 scopus 로고    scopus 로고
    • Characterization of nitrous oxide reductase from a methylotrophic denitrifying bacterium, Hyphomicrobium denitrificans A3151
    • Yamaguchi K, Kawamura A, Ogawa H, Suzuki S. 2003. Characterization of nitrous oxide reductase from a methylotrophic denitrifying bacterium, Hyphomicrobium denitrificans A3151. J Biochem 134:853-858. http://dx.doi.org/10.1093/jb/mvg211.
    • (2003) J Biochem , vol.134 , pp. 853-858
    • Yamaguchi, K.1    Kawamura, A.2    Ogawa, H.3    Suzuki, S.4
  • 19
    • 36348959091 scopus 로고    scopus 로고
    • Development of a fed-batch process for the production of a dye-linked formaldehyde dehydrogenase in Hyphomicrobium zavarzinii ZV 580
    • Jérôme V, Hermann M, Hilbrig F, Freitag R. 2007. Development of a fed-batch process for the production of a dye-linked formaldehyde dehydrogenase in Hyphomicrobium zavarzinii ZV 580. Appl Microbiol Biotechnol 77:779-788. http://dx.doi.org/10.1007/s00253-007-1218-z.
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 779-788
    • Jérôme, V.1    Hermann, M.2    Hilbrig, F.3    Freitag, R.4
  • 20
    • 0028228003 scopus 로고
    • A novel dye-linked formaldehyde dehydrogenase with some properties indicating the presence of a protein-bound redox-active quinone cofactor
    • Klein CR, Kesseler FP, Perrei C, Frank J, Duine JA, Schwartz AC. 1994. A novel dye-linked formaldehyde dehydrogenase with some properties indicating the presence of a protein-bound redox-active quinone cofactor. Biochem J 301:289-295.
    • (1994) Biochem J , vol.301 , pp. 289-295
    • Klein, C.R.1    Kesseler, F.P.2    Perrei, C.3    Frank, J.4    Duine, J.A.5    Schwartz, A.C.6
  • 21
    • 84885213963 scopus 로고    scopus 로고
    • Hyphomicrobium nitrativorans sp. nov., isolated from the biofilm of a methanol-fed denitrification system treating seawater at the Montreal Biodome (Canada)
    • Martineau C, Villeneuve C, Mauffrey F, Villemur R. 2013. Hyphomicrobium nitrativorans sp. nov., isolated from the biofilm of a methanol-fed denitrification system treating seawater at the Montreal Biodome (Canada). Int J Syst Evol Microbiol 63:3777-3781. http://dx.doi.org/10.1099/ijs.0.048124-0.
    • (2013) Int J Syst Evol Microbiol , vol.63 , pp. 3777-3781
    • Martineau, C.1    Villeneuve, C.2    Mauffrey, F.3    Villemur, R.4
  • 22
    • 84998814304 scopus 로고    scopus 로고
    • Complete genome sequence of Hyphomicrobium nitrativorans strain NL23, a denitrifying bacterium isolated from biofilm of a methanol-fed denitrification system treating seawater at the Montreal Biodome
    • Martineau C, Villeneuve C, Mauffrey F, Villemur R. 2014. Complete genome sequence of Hyphomicrobium nitrativorans strain NL23, a denitrifying bacterium isolated from biofilm of a methanol-fed denitrification system treating seawater at the Montreal Biodome. Genome Announc 2(1):e01165-13 http://dx.doi.org/10.1128/genomeA.01165-13.
    • (2014) Genome Announc , vol.2 , Issue.1
    • Martineau, C.1    Villeneuve, C.2    Mauffrey, F.3    Villemur, R.4
  • 23
    • 77957007562 scopus 로고    scopus 로고
    • Dissimilatory reduction of nitrate in seawater by a Methylophaga strain containing two highly divergent narG sequences
    • Auclair J, Lepine F, Parent S, Villemur R. 2010. Dissimilatory reduction of nitrate in seawater by a Methylophaga strain containing two highly divergent narG sequences. ISME J 4:1302-1313. http://dx.doi.org/10.1038/ismej.2010.47.
    • (2010) ISME J , vol.4 , pp. 1302-1313
    • Auclair, J.1    Lepine, F.2    Parent, S.3    Villemur, R.4
  • 24
    • 84878879126 scopus 로고    scopus 로고
    • Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri sp. nov., isolated from the biofilm of the methanol-fed denitrification system treating the seawater at the Montreal Biodome
    • Villeneuve C, Martineau C, Mauffrey F, Villemur R. 2013. Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri sp. nov., isolated from the biofilm of the methanol-fed denitrification system treating the seawater at the Montreal Biodome. Int J Syst Evol Microbiol 63:2216-2222. http://dx.doi.org/10.1099/ijs.0.044545-0.
    • (2013) Int J Syst Evol Microbiol , vol.63 , pp. 2216-2222
    • Villeneuve, C.1    Martineau, C.2    Mauffrey, F.3    Villemur, R.4
  • 25
    • 80052329732 scopus 로고    scopus 로고
    • Genome sequences of eight morphologically diverse alphaproteobacteria
    • Brown PJB, Kysela DT, Buechlein A, Hemmerich C, Brun YV. 2011. Genome sequences of eight morphologically diverse alphaproteobacteria. J Bacteriol 193:4567-4568. http://dx.doi.org/10.1128/JB.05453-11.
    • (2011) J Bacteriol , vol.193 , pp. 4567-4568
    • Brown, P.J.B.1    Kysela, D.T.2    Buechlein, A.3    Hemmerich, C.4    Brun, Y.V.5
  • 29
    • 77956193448 scopus 로고    scopus 로고
    • progressiveMauve: multiple genome alignment with gene gain, loss and rearrangement
    • Darling AE, Mau B, Perna NT. 2010. progressiveMauve: multiple genome alignment with gene gain, loss and rearrangement. PLoS One 5:e11147 http://dx.doi.org/10.1371/journal.pone.0011147.
    • (2010) PLoS One , vol.5
    • Darling, A.E.1    Mau, B.2    Perna, N.T.3
  • 30
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. 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
  • 31
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: Molecular Evolutionary Genetics Analysis version 6.0
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S. 2013. MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30:2725-2729. http://dx.doi.org/10.1093/molbev/mst197.
    • (2013) Mol Biol Evol , vol.30 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 32
    • 0004253337 scopus 로고    scopus 로고
    • Handbook of microbiological media
    • 4th ed, CRC Press, Boca Raton, FL
    • Atlas RM. 2010. Handbook of microbiological media, 4th ed, vol 1, p 769-868. CRC Press, Boca Raton, FL.
    • (2010) , vol.1 , pp. 769-868
    • Atlas, R.M.1
  • 33
    • 0017294592 scopus 로고
    • Acetylene inhibition of nitrous oxide reduction by denitrifying bacteria
    • Yoshinari T, Knowles R. 1976. Acetylene inhibition of nitrous oxide reduction by denitrifying bacteria. Biochem Biophys Res Commun 69:705-710. http://dx.doi.org/10.1016/0006-291X(76)90932-3.
    • (1976) Biochem Biophys Res Commun , vol.69 , pp. 705-710
    • Yoshinari, T.1    Knowles, R.2
  • 34
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • In Misener S, Krawetz S (ed), Humana Press, Totowa, NJ
    • Rozen S, Skaletsky H. 1999. Primer3 on the WWW for general users and for biologist programmers, p 365-386. In Misener S, Krawetz S (ed), Bioinformatics methods and protocols, vol 132. Humana Press, Totowa, NJ.
    • (1999) Bioinformatics methods and protocols , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 37
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F. 2002. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 3:RESEARCH0034. http://dx.doi.org/10.1186/gb-2002-3-7-research0034.
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 38
    • 3442876969 scopus 로고    scopus 로고
    • Normalization of real-time quantitative reverse transcription-PCR data: a model-based variance estimation approach to identify genes suited for normalization, applied to bladder and colon cancer data sets
    • Andersen CL, Jensen JL, Orntoft TF. 2004. Normalization of real-time quantitative reverse transcription-PCR data: a model-based variance estimation approach to identify genes suited for normalization, applied to bladder and colon cancer data sets. Cancer Res 64:5245-5250. http://dx.doi.org/10.1158/0008-5472.CAN-04-0496.
    • (2004) Cancer Res , vol.64 , pp. 5245-5250
    • Andersen, C.L.1    Jensen, J.L.2    Orntoft, T.F.3
  • 39
    • 1842483281 scopus 로고    scopus 로고
    • Determination of stable housekeeping genes, differentially regulated target genes and sample integrity: BestKeeper-Excel-based tool using pair-wise correlations
    • Pfaffl MW, Tichopad A, Prgomet C, Neuvians TP. 2004. Determination of stable housekeeping genes, differentially regulated target genes and sample integrity: BestKeeper-Excel-based tool using pair-wise correlations. Biotechnol Lett 26:509-515. http://dx.doi.org/10.1023/B:BILE.0000019559.84305.47.
    • (2004) Biotechnol Lett , vol.26 , pp. 509-515
    • Pfaffl, M.W.1    Tichopad, A.2    Prgomet, C.3    Neuvians, T.P.4
  • 40
    • 33750295976 scopus 로고    scopus 로고
    • Selection of housekeeping genes for gene expression studies in human reticulocytes using real-time PCR
    • Silver N, Best S, Jiang J, Thein SL. 2006. Selection of housekeeping genes for gene expression studies in human reticulocytes using real-time PCR. BMC Mol Biol 7:33. http://dx.doi.org/10.1186/1471-2199-7-33.
    • (2006) BMC Mol Biol , vol.7 , pp. 33
    • Silver, N.1    Best, S.2    Jiang, J.3    Thein, S.L.4
  • 41
    • 53849131672 scopus 로고    scopus 로고
    • Interdependence of two NarK domains in a fused nitrate/nitrite transporter
    • Goddard AD, Moir JWB, Richardson DJ, Ferguson SJ. 2008. Interdependence of two NarK domains in a fused nitrate/nitrite transporter. Mol Microbiol 70:667-681. http://dx.doi.org/10.1111/j.1365-2958.2008.06436.x.
    • (2008) Mol Microbiol , vol.70 , pp. 667-681
    • Goddard, A.D.1    Moir, J.W.B.2    Richardson, D.J.3    Ferguson, S.J.4
  • 42
    • 0642346959 scopus 로고    scopus 로고
    • Aerobic and anaerobic nitrate and nitrite reduction in free-living cells of Bradyrhizobium sp. (Lupinus)
    • Polcyn W, Luciński R. 2003. Aerobic and anaerobic nitrate and nitrite reduction in free-living cells of Bradyrhizobium sp. (Lupinus). FEMS Microbiol Lett 226:331-337. http://dx.doi.org/10.1016/S0378-1097(03)00620-7.
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 331-337
    • Polcyn, W.1    Luciński, R.2
  • 43
    • 0029636515 scopus 로고
    • Competition between nitrate and nitrite reduction in denitrification by Pseudomonas fluorescens
    • Almeida JS, Reis MAM, Carrondo MJT. 1995. Competition between nitrate and nitrite reduction in denitrification by Pseudomonas fluorescens. Biotechnol Bioeng 46:476-484. http://dx.doi.org/10.1002/bit.260460512.
    • (1995) Biotechnol Bioeng , vol.46 , pp. 476-484
    • Almeida, J.S.1    Reis, M.A.M.2    Carrondo, M.J.T.3
  • 44
    • 0030200160 scopus 로고    scopus 로고
    • Kinetics of denitrification by Pseudomonas denitrificans under growth conditions limited by carbon and/or nitrate or nitrite
    • Kornaros M, Zafiri C, Lyberatos G. 1996. Kinetics of denitrification by Pseudomonas denitrificans under growth conditions limited by carbon and/or nitrate or nitrite. Water Environ Res 68:934-945. http://dx.doi.org/10.2175/106143096X127947.
    • (1996) Water Environ Res , vol.68 , pp. 934-945
    • Kornaros, M.1    Zafiri, C.2    Lyberatos, G.3
  • 45
    • 35348819939 scopus 로고    scopus 로고
    • Genomic analysis reveals widespread occurrence of new classes of copper nitrite reductases
    • Ellis MJ, Grossmann JG, Eady RR, Hasnain SS. 2007. Genomic analysis reveals widespread occurrence of new classes of copper nitrite reductases. J Biol Inorg Chem 12:1119-1127. http://dx.doi.org/10.1007/s00775-007-0282-2.
    • (2007) J Biol Inorg Chem , vol.12 , pp. 1119-1127
    • Ellis, M.J.1    Grossmann, J.G.2    Eady, R.R.3    Hasnain, S.S.4
  • 46
    • 84876550671 scopus 로고    scopus 로고
    • Impacts of nitrate and nitrite on physiology of Shewanella oneidensis
    • Zhang H, Fu H, Wang J, Sun L, Jiang Y, Zhang L, Gao H. 2013. Impacts of nitrate and nitrite on physiology of Shewanella oneidensis. PLoS One 8:e62629. http://dx.doi.org/10.1371/journal.pone.0062629.
    • (2013) PLoS One , vol.8
    • Zhang, H.1    Fu, H.2    Wang, J.3    Sun, L.4    Jiang, Y.5    Zhang, L.6    Gao, H.7
  • 48
    • 0036182372 scopus 로고    scopus 로고
    • Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12
    • Stewart V, Lu Y, Darwin AJ. 2002. Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12. J Bacteriol 184:1314-1323. http://dx.doi.org/10.1128/JB.184.5.1314-1323.2002.
    • (2002) J Bacteriol , vol.184 , pp. 1314-1323
    • Stewart, V.1    Lu, Y.2    Darwin, A.J.3
  • 49
    • 0033571051 scopus 로고    scopus 로고
    • Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?
    • Potter LC, Millington P, Griffiths L, Thomas GH, Cole JA. 1999. Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth? Biochem J 344:77-84. http://dx.doi.org/10.1042/0264-6021:3440077.
    • (1999) Biochem J , vol.344 , pp. 77-84
    • Potter, L.C.1    Millington, P.2    Griffiths, L.3    Thomas, G.H.4    Cole, J.A.5
  • 50
    • 0031856846 scopus 로고    scopus 로고
    • Fnr, NarP, and NarL regulation of Escherichia coli K-12 napF (periplasmic nitrate reductase) operon transcription in vitro
    • Darwin AJ, Ziegelhoffer EC, Kiley PJ, Stewart V. 1998. Fnr, NarP, and NarL regulation of Escherichia coli K-12 napF (periplasmic nitrate reductase) operon transcription in vitro. J Bacteriol 180:4192-4198.
    • (1998) J Bacteriol , vol.180 , pp. 4192-4198
    • Darwin, A.J.1    Ziegelhoffer, E.C.2    Kiley, P.J.3    Stewart, V.4
  • 51
    • 0032835980 scopus 로고    scopus 로고
    • The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite
    • Wang H, Tseng C-P, Gunsalus RP. 1999. The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite. J Bacteriol 181:5303-5308.
    • (1999) J Bacteriol , vol.181 , pp. 5303-5308
    • Wang, H.1    Tseng, C.-P.2    Gunsalus, R.P.3
  • 52
    • 0025333241 scopus 로고
    • Periplasmic and membrane-bound respiratory nitrate reductases in Thiosphaera pantotropha: the periplasmic enzyme catalyzes the first step in aerobic denitrification
    • Bell LC, Richardson DJ, Ferguson SJ. 1990. Periplasmic and membrane-bound respiratory nitrate reductases in Thiosphaera pantotropha: the periplasmic enzyme catalyzes the first step in aerobic denitrification. FEBS Lett 265:85-87. http://dx.doi.org/10.1016/0014-5793(90)80889-Q.
    • (1990) FEBS Lett , vol.265 , pp. 85-87
    • Bell, L.C.1    Richardson, D.J.2    Ferguson, S.J.3
  • 53
    • 0033709553 scopus 로고    scopus 로고
    • Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates
    • Sears HJ, Sawers G, Berks BC, Ferguson SJ, Richardson DJ. 2000. Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates. Microbiology 146:2977-2985.
    • (2000) Microbiology , vol.146 , pp. 2977-2985
    • Sears, H.J.1    Sawers, G.2    Berks, B.C.3    Ferguson, S.J.4    Richardson, D.J.5
  • 54
    • 84555195309 scopus 로고    scopus 로고
    • Physiological roles for two periplasmic nitrate reductases in Rhodobacter sphaeroides 2.4.3 (ATCC 17025)
    • Hartsock A, Shapleigh JP. 2011. Physiological roles for two periplasmic nitrate reductases in Rhodobacter sphaeroides 2.4.3 (ATCC 17025). J Bacteriol 193:6483-6489. http://dx.doi.org/10.1128/JB.05324-11.
    • (2011) J Bacteriol , vol.193 , pp. 6483-6489
    • Hartsock, A.1    Shapleigh, J.P.2
  • 55
    • 76449102157 scopus 로고    scopus 로고
    • The periplasmic nitrate reductase in Shewanella: the resolution, distribution and functional implications of two NAP isoforms, NapEDABC and NapDAGHB
    • Simpson PJL, Richardson DJ, Codd R. 2010. The periplasmic nitrate reductase in Shewanella: the resolution, distribution and functional implications of two NAP isoforms, NapEDABC and NapDAGHB. Microbiology 156:302-312. http://dx.doi.org/10.1099/mic.0.034421-0.
    • (2010) Microbiology , vol.156 , pp. 302-312
    • Simpson, P.J.L.1    Richardson, D.J.2    Codd, R.3
  • 56
    • 79955064482 scopus 로고    scopus 로고
    • Physiological and evolutionary studies of NAP systems in Shewanella piezotolerans WP3
    • Chen Y, Wang F, Xu J, Mehmood MA, Xiao X. 2011. Physiological and evolutionary studies of NAP systems in Shewanella piezotolerans WP3. ISME J 5:843-855. http://dx.doi.org/10.1038/ismej.2010.182.
    • (2011) ISME J , vol.5 , pp. 843-855
    • Chen, Y.1    Wang, F.2    Xu, J.3    Mehmood, M.A.4    Xiao, X.5
  • 57
    • 84868311632 scopus 로고    scopus 로고
    • Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga sp. strain JAM7
    • Villeneuve C, Martineau C, Mauffrey F, Villemur R. 2012. Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga sp. strain JAM7. J Bacteriol 194:4126-4127. http://dx.doi.org/10.1128/JB.00726-12.
    • (2012) J Bacteriol , vol.194 , pp. 4126-4127
    • Villeneuve, C.1    Martineau, C.2    Mauffrey, F.3    Villemur, R.4
  • 58
    • 0346252346 scopus 로고    scopus 로고
    • The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic nitrate reductase are essential for nitrate respiration
    • Delgado MJ, Bonnard N, Tresierra-Ayala A, Bedmar EJ, Müller P. 2003. The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic nitrate reductase are essential for nitrate respiration. Microbiology 149:3395-3403. http://dx.doi.org/10.1099/mic.0.26620-0.
    • (2003) Microbiology , vol.149 , pp. 3395-3403
    • Delgado, M.J.1    Bonnard, N.2    Tresierra-Ayala, A.3    Bedmar, E.J.4    Müller, P.5
  • 59
    • 23744475357 scopus 로고    scopus 로고
    • Expression of nitrite and nitric oxide reductases in free-living and plant-associated Agrobacterium tumefaciens C58 cells
    • Baek SH, Shapleigh JP. 2005. Expression of nitrite and nitric oxide reductases in free-living and plant-associated Agrobacterium tumefaciens C58 cells. Appl Environ Microbiol 71:4427-4436. http://dx.doi.org/10.1128/AEM.71.8.4427-4436.2005.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4427-4436
    • Baek, S.H.1    Shapleigh, J.P.2
  • 60
    • 0031047127 scopus 로고    scopus 로고
    • Characterization and regulation of the gene encoding nitrite reductase in Rhodobacter sphaeroides 2.4.3
    • Tosques IE, Kwiatkowski AV, Shi J, Shapleigh JP. 1997. Characterization and regulation of the gene encoding nitrite reductase in Rhodobacter sphaeroides 2.4.3. J Bacteriol 179:1090-1095.
    • (1997) J Bacteriol , vol.179 , pp. 1090-1095
    • Tosques, I.E.1    Kwiatkowski, A.V.2    Shi, J.3    Shapleigh, J.P.4
  • 61
    • 0035980280 scopus 로고    scopus 로고
    • Characterization of the nirK gene encoding the respiratory, Cu-containing nitrite reductase of Bradyrhizobium japonicum
    • Velasco L, Mesa S, Delgado MJ, Bedmar EJ. 2001. Characterization of the nirK gene encoding the respiratory, Cu-containing nitrite reductase of Bradyrhizobium japonicum. Biochim Biophys Acta 1521:130-134. http://dx.doi.org/10.1016/S0167-4781(01)00279-2.
    • (2001) Biochim Biophys Acta , vol.1521 , pp. 130-134
    • Velasco, L.1    Mesa, S.2    Delgado, M.J.3    Bedmar, E.J.4
  • 62
    • 0346849873 scopus 로고    scopus 로고
    • Site-directed mutagenesis of NnrR: a transcriptional regulator of nitrite and nitric oxide reductase in Rhodobacter sphaeroides
    • Laratta WP, Shapleigh JP. 2003. Site-directed mutagenesis of NnrR: a transcriptional regulator of nitrite and nitric oxide reductase in Rhodobacter sphaeroides. FEMS Microbiol Lett 229:173-178. http://dx.doi.org/10.1016/S0378-1097(03)00821-8.
    • (2003) FEMS Microbiol Lett , vol.229 , pp. 173-178
    • Laratta, W.P.1    Shapleigh, J.P.2


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