메뉴 건너뛰기




Volumn 24, Issue 4, 1998, Pages 335-373

Methanotrophs, Methylosinus trichosporium OB3b, sMMO, and their application to bioremediation

Author keywords

Methanotrophs; Methylosinus trichosporium OB3b; pMMO; sMMO

Indexed keywords

CHLORAL HYDRATE; CHLOROFORM; COPPER; CYCLOPROPANE; DICHLOROMETHANE; FORMATE DEHYDROGENASE; METHANE MONOOXYGENASE; METHANOL DEHYDROGENASE; NAPHTHALENE DERIVATIVE; ORGANOHALOGEN DERIVATIVE; PROTEIN A; PROTEIN B; PROTEIN C; TRICHLOROETHYLENE; TRICHLOROPHENOL DERIVATIVE; UNCLASSIFIED DRUG; VINYL CHLORIDE;

EID: 0032432107     PISSN: 1040841X     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408419891294217     Document Type: Review
Times cited : (91)

References (168)
  • 1
    • 0025291817 scopus 로고
    • Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: Mechanistic and environmental implications
    • Fox B, Bourneman J, Wackett L, and Lipscomb J. 1990. Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications. Biochemistry 29: 6419-6427.
    • (1990) Biochemistry , vol.29 , pp. 6419-6427
    • Fox, B.1    Bourneman, J.2    Wackett, L.3    Lipscomb, J.4
  • 2
    • 0024377330 scopus 로고
    • Degradation of trichloroethylene by Methylosinus trichosporium OB3b
    • Tsien H, Brusseau G, Hanson R, and Wackett L. 1989. Degradation of trichloroethylene by Methylosinus trichosporium OB3b. Appl. Environ. Microbiol. 55: 3155-3161.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 3155-3161
    • Tsien, H.1    Brusseau, G.2    Hanson, R.3    Wackett, L.4
  • 3
    • 0018947980 scopus 로고
    • New findings in methane-utilising bacteria highlight their importance in the biosphere and their commercial potential
    • Higgins I, Best D, and Hammond R. 1980. New findings in methane-utilising bacteria highlight their importance in the biosphere and their commercial potential. Nature 286: 561-564.
    • (1980) Nature , vol.286 , pp. 561-564
    • Higgins, I.1    Best, D.2    Hammond, R.3
  • 5
    • 0026098328 scopus 로고
    • Effects of toxicity and reductant supply on trichloroethylene transformation by a mixed methanotrophic culture
    • Alvarez-Cohen L and Mc Carty P. 1991. Effects of toxicity and reductant supply on trichloroethylene transformation by a mixed methanotrophic culture. Appl. Environ. Microbiol. 57: 228-235.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 228-235
    • Alvarez-Cohen, L.1    Mc Carty, P.2
  • 6
    • 0026098606 scopus 로고
    • Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b and toxicity of trichloroethylene
    • Oldenhuis R, Oedzes J, Waarde J, and Janssen D. 1991. Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b and toxicity of trichloroethylene. Appl. Environ. Microbiol. 57: 7-14.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 7-14
    • Oldenhuis, R.1    Oedzes, J.2    Waarde, J.3    Janssen, D.4
  • 7
    • 0024444795 scopus 로고
    • Degradation of chlorinated aliphatic hydrocarbons by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase
    • Oldenhuis R, Vink R, Janssen D, and Witholt B. 1989. Degradation of chlorinated aliphatic hydrocarbons by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. Appl. Environ. Microbiol. 55: 2819-2826.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2819-2826
    • Oldenhuis, R.1    Vink, R.2    Janssen, D.3    Witholt, B.4
  • 8
    • 0017404563 scopus 로고
    • The soluble methane monooxygenase of Methylococcus capsulatus (Bath)
    • Colby J, Stirling D, and Dalton H. 1977. The soluble methane monooxygenase of Methylococcus capsulatus (Bath). J. Biochem. 165: 395-402.
    • (1977) J. Biochem. , vol.165 , pp. 395-402
    • Colby, J.1    Stirling, D.2    Dalton, H.3
  • 9
    • 0019202599 scopus 로고
    • Microbial oxidation of gaseous hydrocarbons: Oxidation of lower n-alkenes and n-alkanes by resting cell suspensions of various methylotrophic bacteria, and the effect of methane metabolites
    • Hou C, Patel R, Laskin A, and Barnaby N. 1980. Microbial oxidation of gaseous hydrocarbons: oxidation of lower n-alkenes and n-alkanes by resting cell suspensions of various methylotrophic bacteria, and the effect of methane metabolites. FEMS Microbiol. Lett. 9: 267-270.
    • (1980) FEMS Microbiol. Lett. , vol.9 , pp. 267-270
    • Hou, C.1    Patel, R.2    Laskin, A.3    Barnaby, N.4
  • 12
    • 0020559210 scopus 로고
    • Copper stress underlies the fundamental change in the intracellular location of methane monooxygenase in methane-oxidizing organisms: Studies in batch and continuous cultures
    • Stanley S, Prior S, Leak S, and Dalton H. 1983. Copper stress underlies the fundamental change in the intracellular location of methane monooxygenase in methane-oxidizing organisms: studies in batch and continuous cultures. Biotechnol. Lett. 5: 487-492.
    • (1983) Biotechnol. Lett. , vol.5 , pp. 487-492
    • Stanley, S.1    Prior, S.2    Leak, S.3    Dalton, H.4
  • 13
    • 0019387176 scopus 로고
    • The effect of growth conditions on intracytoplasmic membranes and methane monooxygenase activities in Methylosinus trichosporium OB3b
    • Scott D, Brannan D, and Higgins I. 1981. The effect of growth conditions on intracytoplasmic membranes and methane monooxygenase activities in Methylosinus trichosporium OB3b. J. Gen. Microbiol. 125: 63-72.
    • (1981) J. Gen. Microbiol. , vol.125 , pp. 63-72
    • Scott, D.1    Brannan, D.2    Higgins, I.3
  • 14
    • 0017577979 scopus 로고
    • Purification of the methane monooxygenase enzyme system from Methylosinus trichosporium OB3b
    • Tonge G, Harrison D, and Higgins I. 1977. Purification of the methane monooxygenase enzyme system from Methylosinus trichosporium OB3b. J. Biochem. 161: 333-344.
    • (1977) J. Biochem. , vol.161 , pp. 333-344
    • Tonge, G.1    Harrison, D.2    Higgins, I.3
  • 15
    • 1542488004 scopus 로고
    • Recent progress in research on methanotrophs and methane monooxygenases
    • Hou C 1986. Recent progress in research on methanotrophs and methane monooxygenases. Biotechnol. Gen. Eng. Rev. 4: 145-168.
    • (1986) Biotechnol. Gen. Eng. Rev. , vol.4 , pp. 145-168
    • Hou, C.1
  • 16
    • 0021697309 scopus 로고
    • Substrate specificities of the soluble and particulate methane monooxygenase of Methylosinus trichosporium OB3b
    • Burrows K, Cornish A, Scott D, and Higgins I. 1984. Substrate specificities of the soluble and particulate methane monooxygenase of Methylosinus trichosporium OB3b. J. Gen. Microbiol. 130: 3327-3333.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 3327-3333
    • Burrows, K.1    Cornish, A.2    Scott, D.3    Higgins, I.4
  • 17
    • 0021911405 scopus 로고
    • The effect of copper ions on membrane content and methane monooxygenase activity in methanol grown cells of Methylococcus capsulatus (Bath)
    • Prior S and Dalton H. 1985. The effect of copper ions on membrane content and methane monooxygenase activity in methanol grown cells of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 131: 155-163.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 155-163
    • Prior, S.1    Dalton, H.2
  • 18
    • 0026455068 scopus 로고
    • Methylosinus trichosporium OB3b mutants having constitutive expression of soluble methane monooxygenase in the presence of high levels of copper
    • Phelps P, Agarwal S, Speitel G, and Georgiou G. 1992. Methylosinus trichosporium OB3b mutants having constitutive expression of soluble methane monooxygenase in the presence of high levels of copper. Appl. Environ. Microbiol. 58: 11, 3701-3708.
    • (1992) Appl. Environ. Microbiol. , vol.58 , Issue.11 , pp. 3701-3708
    • Phelps, P.1    Agarwal, S.2    Speitel, G.3    Georgiou, G.4
  • 20
    • 0025369495 scopus 로고
    • Screening of obligate methanotrophs for soluble methane monooxygenase genes
    • Stainthorpe A, Salmond G, Dalton H, and Murrell J. 1990. Screening of obligate methanotrophs for soluble methane monooxygenase genes. FEMS Microbiol. Lett. 70: 211-216.
    • (1990) FEMS Microbiol. Lett. , vol.70 , pp. 211-216
    • Stainthorpe, A.1    Salmond, G.2    Dalton, H.3    Murrell, J.4
  • 21
    • 0026596126 scopus 로고
    • Soluble methane monooxygenase component B gene probe for identification of methanotrophs that rapidly degrade trichloroethylene
    • Tsien H and Hanson R. 1992. Soluble methane monooxygenase component B gene probe for identification of methanotrophs that rapidly degrade trichloroethylene. Appl. Environ. Microbiol. 58: 953-960.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 953-960
    • Tsien, H.1    Hanson, R.2
  • 22
    • 0022346556 scopus 로고
    • Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Green J and Dalton H. 1985. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 15795-15801.
    • (1985) J. Biol. Chem. , pp. 15795-15801
    • Green, J.1    Dalton, H.2
  • 23
    • 0026417085 scopus 로고
    • Batch cultivation of Methylosinus trichosporium OB3b. I. Production of soluble methane monooxygenase
    • Park S, Hanna M, Taylor R, and Droege W. 1991. Batch cultivation of Methylosinus trichosporium OB3b. I. Production of soluble methane monooxygenase. Biotechnol. Bioeng. 38: 423-433.
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 423-433
    • Park, S.1    Hanna, M.2    Taylor, R.3    Droege, W.4
  • 24
    • 2442749144 scopus 로고
    • Cultivation of Methylosinus trichosporium OB3b for the production of particulatemethane monooxygenase
    • 98-BIOT
    • Shah N, Park S, Taylor R, and Droege M. 1992. Cultivation of Methylosinus trichosporium OB3b for the production of particulatemethane monooxygenase. Abstr. Am. Chem. Soc. 203: 1, 98-BIOT.
    • (1992) Abstr. Am. Chem. Soc. , vol.203 , Issue.1
    • Shah, N.1    Park, S.2    Taylor, R.3    Droege, M.4
  • 25
    • 0026928603 scopus 로고
    • Cultivation of Methylosinus trichosporium OB3b. III. Production of particulate methane monooxygenase in continuous culture
    • Shah N, Park S, Taylor R, and Droege M. 1992. Cultivation of Methylosinus trichosporium OB3b. III. Production of particulate methane monooxygenase in continuous culture. Biotechnol. Bioeng. 40: 6, 705-712.
    • (1992) Biotechnol. Bioeng. , vol.40 , Issue.6 , pp. 705-712
    • Shah, N.1    Park, S.2    Taylor, R.3    Droege, M.4
  • 26
    • 0023213807 scopus 로고
    • Purification and properties of the hydroxylase component of methane monooxygenase
    • Patel R and Savas J. 1987. Purification and properties of the hydroxylase component of methane monooxygenase. J. Bacteriol. 169: 2313-2317.
    • (1987) J. Bacteriol. , vol.169 , pp. 2313-2317
    • Patel, R.1    Savas, J.2
  • 27
    • 0026023610 scopus 로고
    • Purification and characterization of the soluble methane monooxygenase from Methylosinus sporium 5 demonstrates the highly conserved nature of this enzyme in methanotrophs
    • Pilkington S and Dalton H. 1991. Purification and characterization of the soluble methane monooxygenase from Methylosinus sporium 5 demonstrates the highly conserved nature of this enzyme in methanotrophs. FEMS Microbiol. Lett. 78: 103-108.
    • (1991) FEMS Microbiol. Lett. , vol.78 , pp. 103-108
    • Pilkington, S.1    Dalton, H.2
  • 28
    • 84950843334 scopus 로고
    • Purification and properties of a soluble methane monooxygenase from Methylocystis sp. M
    • Nakajima T, Uchiyama H, Yagi O, and Nakahara T. 1992. Purification and properties of a soluble methane monooxygenase from Methylocystis sp. M. Biosci, Biotechnol. Biochem. 56: 5, 736-740.
    • (1992) Biosci, Biotechnol. Biochem. , vol.56 , Issue.5 , pp. 736-740
    • Nakajima, T.1    Uchiyama, H.2    Yagi, O.3    Nakahara, T.4
  • 29
    • 0027450659 scopus 로고
    • Soluble methane monooxygenase production and trichloroethylene degradation by a type I methanotroph
    • Koh S, Bowman J, and Sayler G. 1993. Soluble methane monooxygenase production and trichloroethylene degradation by a type I methanotroph. Appl. Environ. Microbiol. 59: 960-967.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 960-967
    • Koh, S.1    Bowman, J.2    Sayler, G.3
  • 30
    • 0026044876 scopus 로고
    • The methane monooxygenase gene cluster of Methylosinus trichosporium OB3b - Cloning and sequencing of the mmoC gene
    • Cardy D, Laidler V, Salmond G, and Murrell J. 1991. The methane monooxygenase gene cluster of Methylosinus trichosporium OB3b - cloning and sequencing of the mmoC gene. Arch. Microbiol. 156: 6, 477-483.
    • (1991) Arch. Microbiol. , vol.156 , Issue.6 , pp. 477-483
    • Cardy, D.1    Laidler, V.2    Salmond, G.3    Murrell, J.4
  • 31
    • 0000468411 scopus 로고
    • Biological methane activation - Lessons for the chemists
    • Dalton H. 1992. Biological methane activation - lessons for the chemists. Catalysis Today 13: 2-3, 455-461.
    • (1992) Catalysis Today , vol.13 , Issue.2-3 , pp. 455-461
    • Dalton, H.1
  • 32
    • 0024970671 scopus 로고
    • Methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox B, Froland W, Dege J, and Lipscomb J. 1989. Methane monooxygenase from Methylosinus trichosporium OB3b. J. Biol. Chem. 264: 10023-10033.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10023-10033
    • Fox, B.1    Froland, W.2    Dege, J.3    Lipscomb, J.4
  • 33
    • 0021759122 scopus 로고
    • Purification and characterisation of component a of the methane monooxygenase from Methylococcus capsulatus (Bath)
    • Woodland M and Dalton H. 1984. Purification and characterisation of component A of the methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 259: 53-59.
    • (1984) J. Biol. Chem. , vol.259 , pp. 53-59
    • Woodland, M.1    Dalton, H.2
  • 34
    • 0025005005 scopus 로고
    • Methane monooxygenase catalysed oxygenation of 1,1-dimethylcyclopropane - Evidence for radical and carbocationic intermediates
    • Ruzicka F, Huang D, Donnelly M, and Frey P. 1990. Methane monooxygenase catalysed oxygenation of 1,1-dimethylcyclopropane - evidence for radical and carbocationic intermediates. Biochemistry. 29: 7, 1696-1700.
    • (1990) Biochemistry , vol.29 , Issue.7 , pp. 1696-1700
    • Ruzicka, F.1    Huang, D.2    Donnelly, M.3    Frey, P.4
  • 35
    • 0026463051 scopus 로고
    • Evidence for two histidine ligands at the diiron site of methane monooxygenase
    • Drummond D, Smith S, and Dalton H. 1992. Evidence for two histidine ligands at the diiron site of methane monooxygenase. J. Biochem. 210: 629-637.
    • (1992) J. Biochem. , vol.210 , pp. 629-637
    • Drummond, D.1    Smith, S.2    Dalton, H.3
  • 36
    • 0026088028 scopus 로고
    • Complex formation between the components of methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox B, Liu Y, Dege J, and Lipscomb J. 1991. Complex formation between the components of methane monooxygenase from Methylosinus trichosporium OB3b. J. Biol. Chem. 266: 540-550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 540-550
    • Fox, B.1    Liu, Y.2    Dege, J.3    Lipscomb, J.4
  • 37
    • 0026446780 scopus 로고
    • Biological methane activation involves the intermediary of carbon centred radicals
    • Wilkens C, Dalton H, Podmore I, Dieghton N, and Syonous M. 1992. Biological methane activation involves the intermediary of carbon centred radicals. Eur. J. Biochem. 210: 67-72.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 67-72
    • Wilkens, C.1    Dalton, H.2    Podmore, I.3    Dieghton, N.4    Syonous, M.5
  • 38
    • 0028258247 scopus 로고
    • Evidence for chlorine migration during oxidation of 2-chlorobiphenyl by a type II methanotroph
    • Adrians P. 1994. Evidence for chlorine migration during oxidation of 2-chlorobiphenyl by a type II methanotroph. Appl. Environ. Microbiol. 60: 1658-1662.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1658-1662
    • Adrians, P.1
  • 39
    • 0027995836 scopus 로고
    • Cometabolic transformation of monochlorophenyls and dichlorophenyls and chlorohydroxy-biphenyls by methanotrophic groundwater isolates
    • Adrians P and Gribogalic D. 1994. Cometabolic transformation of monochlorophenyls and dichlorophenyls and chlorohydroxy-biphenyls by methanotrophic groundwater isolates. Environ. Sci. Technol. 28: 1325-1330.
    • (1994) Environ. Sci. Technol. , vol.28 , pp. 1325-1330
    • Adrians, P.1    Gribogalic, D.2
  • 40
    • 0029973732 scopus 로고    scopus 로고
    • 1,2,3-trichlorobenzene transformation by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase
    • Sullivan J and Chase H. 1996. 1,2,3-trichlorobenzene transformation by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. Appl. Microbiol. Biotechnol. 45: 427-433.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 427-433
    • Sullivan, J.1    Chase, H.2
  • 41
    • 0025528777 scopus 로고
    • Optimization of trichloroethylene oxidation by methanotrophs and the use of a colourmetric assay to detect soluble methane monooxygenase activity
    • Brusseau G, Tsien G, Hanson R, and Wackett L. 1990. Optimization of trichloroethylene oxidation by methanotrophs and the use of a colourmetric assay to detect soluble methane monooxygenase activity. Biodegradation 1: 19-29.
    • (1990) Biodegradation , vol.1 , pp. 19-29
    • Brusseau, G.1    Tsien, G.2    Hanson, R.3    Wackett, L.4
  • 42
    • 0022624528 scopus 로고
    • Growth yields of methanotrophs I. Effect of copper on the energetics of methane oxidation
    • Leak D and Dalton H. 1986. Growth yields of methanotrophs I. Effect of copper on the energetics of methane oxidation. Appl. Microbiol. Biotechnol. 23: 470-476.
    • (1986) Appl. Microbiol. Biotechnol. , vol.23 , pp. 470-476
    • Leak, D.1    Dalton, H.2
  • 43
    • 0028304991 scopus 로고
    • The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath)
    • Nguyen H, Shiemke A, Jacobs S, Hales B, Lidstrom M, and Chan S. 1994. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269: 21, 14995-15005.
    • (1994) J. Biol. Chem. , vol.269 , Issue.21 , pp. 14995-15005
    • Nguyen, H.1    Shiemke, A.2    Jacobs, S.3    Hales, B.4    Lidstrom, M.5    Chan, S.6
  • 44
    • 0000815740 scopus 로고
    • Trichloroethylene oxidation by the membrane associated methane monooxygenase in type I, type II, and type X methanotrophs
    • DiSpirito A, Gulledge J, Shiemke A K, Murrell, J C, Lidstrom M E, Krema, C L, 1992. Trichloroethylene oxidation by the membrane associated methane monooxygenase in type I, type II, and type X methanotrophs. Biodegradation 2: 151-164.
    • (1992) Biodegradation , vol.2 , pp. 151-164
    • DiSpirito, A.1    Gulledge, J.2    Shiemke, A.K.3    Murrell, J.C.4    Lidstrom, M.E.5    Krema, C.L.6
  • 46
    • 0026809785 scopus 로고
    • The structure of bacterial quinoprotein dehydrogenases
    • Anthony C. 1992. The structure of bacterial quinoprotein dehydrogenases. Int. J. Biochem. 24: 1, 29-39.
    • (1992) Int. J. Biochem. , vol.24 , Issue.1 , pp. 29-39
    • Anthony, C.1
  • 47
    • 0018450992 scopus 로고
    • Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (Component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath)
    • Colby J and Dalton H. 1979. Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (Component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath). J. Biochem. 177: 903-908.
    • (1979) J. Biochem. , vol.177 , pp. 903-908
    • Colby, J.1    Dalton, H.2
  • 48
    • 0025289463 scopus 로고
    • Formate dehydrogenase from the methane oxi-dizer Methylosinus trichosporium OB3b
    • Yoch D, Chen Y, and Hardin M. 1990. Formate dehydrogenase from the methane oxi-dizer Methylosinus trichosporium OB3b. J. Bacteriol. 172: 4456-4463.
    • (1990) J. Bacteriol. , vol.172 , pp. 4456-4463
    • Yoch, D.1    Chen, Y.2    Hardin, M.3
  • 49
    • 0024724771 scopus 로고
    • + reductase from the methane oxidizer Methylosinus trichosporium OB3b
    • + reductase from the methane oxidizer Methylosinus trichosporium OB3b. J. Bacteriol. 5012-5016.
    • (1989) J. Bacteriol. , pp. 5012-5016
    • Chen, Y.1    Yoch, D.2
  • 50
    • 0002220543 scopus 로고
    • Degradation of trichloroethylene by methanotrophic bacteria
    • Murrell, J C and Kelly, D P Ed.. Intercept Ltd., Andover
    • Oldenhuis R and Janssen D. 1992. Degradation of trichloroethylene by methanotrophic bacteria. Microbial growth on C1 Compounds (Murrell, J C and Kelly, D P Ed.). Intercept Ltd., Andover.
    • (1992) Microbial Growth on C1 Compounds
    • Oldenhuis, R.1    Janssen, D.2
  • 51
    • 0027142923 scopus 로고
    • Effect of microorganisms on the bioavailability and biodegradation of crystalline naphthalene
    • Volkering F, Breure A, and Vanandel J. 1993. Effect of microorganisms on the bioavailability and biodegradation of crystalline naphthalene. Appl. Microbiol. Biotechnol. 40: 4, 535-540.
    • (1993) Appl. Microbiol. Biotechnol. , vol.40 , Issue.4 , pp. 535-540
    • Volkering, F.1    Breure, A.2    Vanandel, J.3
  • 52
    • 2442747636 scopus 로고
    • Methanotrophic bacteria and facilitated transport of hydrophobic pollutants in aquifer material
    • Jenkins J, Kadner D, and Lion L. 1994. Methanotrophic bacteria and facilitated transport of hydrophobic pollutants in aquifer material. Abstr. Am. Chem. Soc. 205: 213.
    • (1994) Abstr. Am. Chem. Soc. , vol.205 , pp. 213
    • Jenkins, J.1    Kadner, D.2    Lion, L.3
  • 53
    • 0022624491 scopus 로고
    • Steady-state kinetic analysis of soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Green J and Dalton H. 1986. Steady-state kinetic analysis of soluble methane monooxygenase from Methylococcus capsulatus (Bath). Biochem. J. 236: 1, 155-162.
    • (1986) Biochem. J. , vol.236 , Issue.1 , pp. 155-162
    • Green, J.1    Dalton, H.2
  • 54
    • 0025435215 scopus 로고
    • Metal ion-mediated accumulation of alcohols during alkane oxidation by whole cells of Methylosinus trichosporium
    • Mounfort D, Pybus V, and Wilson R. 1990. Metal ion-mediated accumulation of alcohols during alkane oxidation by whole cells of Methylosinus trichosporium. Enzyme and Microbial Technol. 12: 343-349.
    • (1990) Enzyme and Microbial Technol. , vol.12 , pp. 343-349
    • Mounfort, D.1    Pybus, V.2    Wilson, R.3
  • 55
    • 0025371322 scopus 로고
    • Oxidation of aromatic alcohols by purified methanol dehydrogenase from Methylosinus trichosporium
    • Mountford D. 1990. Oxidation of aromatic alcohols by purified methanol dehydrogenase from Methylosinus trichosporium. J. Bacteriol. 172: 3690-3694.
    • (1990) J. Bacteriol. , vol.172 , pp. 3690-3694
    • Mountford, D.1
  • 58
    • 0024429904 scopus 로고
    • Toxicity of trichloroethylene to Pseudomonas putida FI is mediated by toluene dioxygenase
    • Wackett L and Householder S. 1989. Toxicity of trichloroethylene to Pseudomonas putida FI is mediated by toluene dioxygenase. Appl. Environ. Microbiol. 55: 2723-2725.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2723-2725
    • Wackett, L.1    Householder, S.2
  • 59
    • 2442765612 scopus 로고
    • Oxidation of foreign at carbon atoms
    • Jackoby W B, Bend J R, and Caldwell J, Eds.. Academic Press, New York.
    • Wolf C. 1982. Oxidation of foreign at carbon atoms. Metabolic Basis of Detoxification (Jackoby W B, Bend J R, and Caldwell J, Eds.). Academic Press, New York. 1-28.
    • (1982) Metabolic Basis of Detoxification , pp. 1-28
    • Wolf, C.1
  • 60
    • 0024566937 scopus 로고
    • Biotransformation of 1,1,1-trichloroethane, trichloromethane and tetrachloromethane by a Clostridium sp
    • Galli R and Mc Carty P. 1989. Biotransformation of 1,1,1-trichloroethane, trichloromethane and tetrachloromethane by a Clostridium sp. Appl. Environ. Microbiol. 55: 837-844.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 837-844
    • Galli, R.1    Mc Carty, P.2
  • 61
    • 0024368089 scopus 로고
    • Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Stainthorpe A, Murrell J, Salmond G, Dalton H, and Lees V. 1989. Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath). Arch. Microbiol. 152: 2, 154-159.
    • (1989) Arch. Microbiol. , vol.152 , Issue.2 , pp. 154-159
    • Stainthorpe, A.1    Murrell, J.2    Salmond, G.3    Dalton, H.4    Lees, V.5
  • 62
    • 0025006802 scopus 로고
    • The methane monooxygenase gene cluster of Methylo-coccus capsulatus (Bath)
    • Stainthorpe A, Lees V, Salmond G, Dalton H, and Murrell J. 1990. The methane monooxygenase gene cluster of Methylo-coccus capsulatus (Bath). Gene 91: 1, 27-34.
    • (1990) Gene , vol.91 , Issue.1 , pp. 27-34
    • Stainthorpe, A.1    Lees, V.2    Salmond, G.3    Dalton, H.4    Murrell, J.5
  • 63
    • 0025369495 scopus 로고
    • Screening of obligate methanotrophs for soluble methane monooxygenase genes
    • Stainthorpe A, Salmond G, Dalton H, and Murrell J. 1990. Screening of obligate methanotrophs for soluble methane monooxygenase genes. FEMS Microbiol Lett. 70: 2, 211-216.
    • (1990) FEMS Microbiol Lett. , vol.70 , Issue.2 , pp. 211-216
    • Stainthorpe, A.1    Salmond, G.2    Dalton, H.3    Murrell, J.4
  • 64
    • 0023255826 scopus 로고
    • Cloning of the gamma subunit methane monooxygenase from Methylococcus capsulatus
    • Mullens I and Dalton H. 1987. Cloning of the gamma subunit methane monooxygenase from Methylococcus capsulatus. Bio-Technology 5: 5, 490-493.
    • (1987) Bio-Technology , vol.5 , Issue.5 , pp. 490-493
    • Mullens, I.1    Dalton, H.2
  • 65
    • 0025011069 scopus 로고
    • Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase
    • Pilkington S, Salmond G, Murrell J and Dalton H. 1990. Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase. FEMS Microbiol. Lett. 72: 3, 345-348.
    • (1990) FEMS Microbiol. Lett. , vol.72 , Issue.3 , pp. 345-348
    • Pilkington, S.1    Salmond, G.2    Murrell, J.3    Dalton, H.4
  • 66
    • 0026876403 scopus 로고
    • Genetics and molecular biology of methanotrophs
    • Murrell J. 1992. Genetics and molecular biology of methanotrophs. FEMS Microbiol. Rev. 88: 3-4, 233-248.
    • (1992) FEMS Microbiol. Rev. , vol.88 , Issue.3-4 , pp. 233-248
    • Murrell, J.1
  • 67
    • 0026779760 scopus 로고
    • Functional expression in Escherichia coli of proteins B and C from methane monooxygenase of Methylococcus capsulatus (Bath)
    • West C, Salmond G, Dalton H, and Murrell J. 1992. Functional expression in Escherichia coli of proteins B and C from methane monooxygenase of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 138: 1301-1307.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1301-1307
    • West, C.1    Salmond, G.2    Dalton, H.3    Murrell, J.4
  • 68
    • 0023132685 scopus 로고
    • Transfer of broad host range plasmids to the Type-I obligate Methanotroph Methylomonas Albus
    • Mc Pheat W, Mann N, and Dalton H. 1987. Transfer of broad host range plasmids to the Type-I obligate Methanotroph Methylomonas Albus. FEMS Microbiol. Lett. 41: 2, 185-188.
    • (1987) FEMS Microbiol. Lett. , vol.41 , Issue.2 , pp. 185-188
    • Mc Pheat, W.1    Mann, N.2    Dalton, H.3
  • 69
    • 0023182890 scopus 로고
    • Restoration of phenotype in Escherichia coli auxotrophs by Pulb 113 mediated mobilisation from methylotrophic bacteria
    • Altaho N and Warner P. 1987. Restoration of phenotype in Escherichia coli auxotrophs by Pulb 113 mediated mobilisation from methylotrophic bacteria. FEMS Microbiol. Lett. 43: 2, 235-239.
    • (1987) FEMS Microbiol. Lett. , vol.43 , Issue.2 , pp. 235-239
    • Altaho, N.1    Warner, P.2
  • 70
    • 0026779760 scopus 로고
    • Functional expression in Escherichia coli of Protein B and Protein C from soluble methane monooxygenase of Methylococcus capsulatus (Bath)
    • West C, Salmond G, Dalton H and Murrell J. 1992. Functional expression in Escherichia coli of Protein B and Protein C from soluble methane monooxygenase of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 138: 7, 1301-1307.
    • (1992) J. Gen. Microbiol. , vol.138 , Issue.7 , pp. 1301-1307
    • West, C.1    Salmond, G.2    Dalton, H.3    Murrell, J.4
  • 71
    • 0024441496 scopus 로고
    • Biological reductive dechlorination of tetrachloroethyl-ene and trichloroethylene under methanogenic conditions
    • Freedman D and Gossett J. 1989. Biological reductive dechlorination of tetrachloroethyl-ene and trichloroethylene under methanogenic conditions. Appl. Environ. Microbiol. 55: 2144-2151.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2144-2151
    • Freedman, D.1    Gossett, J.2
  • 72
    • 0021215237 scopus 로고
    • Propylene oxide production from propylene by immobilized whole cells of Methylosinus sp. CRL 31 in a gas-solid reactor
    • Hou C. 1984. Propylene oxide production from propylene by immobilized whole cells of Methylosinus sp. CRL 31 in a gas-solid reactor. Appl. Microbiol. Biotechnol. 19: 1-4.
    • (1984) Appl. Microbiol. Biotechnol. , vol.19 , pp. 1-4
    • Hou, C.1
  • 73
    • 0022624491 scopus 로고
    • Steady-state kinetic analysis of soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Green J and Dalton H. 1986. Steady-state kinetic analysis of soluble methane monooxygenase from Methylococcus capsulatus (Bath). J. Biochem. 236: 155-162.
    • (1986) J. Biochem. , vol.236 , pp. 155-162
    • Green, J.1    Dalton, H.2
  • 74
    • 0022365236 scopus 로고
    • Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath)
    • Prior S and Dalton H. 1985. Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath). FEMS Microbiol. Lett. 29: 105-109.
    • (1985) FEMS Microbiol. Lett. , vol.29 , pp. 105-109
    • Prior, S.1    Dalton, H.2
  • 75
    • 0022033560 scopus 로고
    • Spectroscopic evidence for a photosensitive oxygenated state of ammonia monooxygenase
    • Shears J and Wood P. 1985. Spectroscopic evidence for a photosensitive oxygenated state of ammonia monooxygenase. Biochem. J. 226: 2, 499-507.
    • (1985) Biochem. J. , vol.226 , Issue.2 , pp. 499-507
    • Shears, J.1    Wood, P.2
  • 76
    • 0025727942 scopus 로고
    • Inhibition by ammonia of methane utilisation in Methylococcus capsulatus (Bath)
    • Carlson H, Joergensen L, and Degn H. 1991. Inhibition by ammonia of methane utilisation in Methylococcus capsulatus (Bath). Appl. Microbiol. Biotechnol. 35: 124-127.
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 124-127
    • Carlson, H.1    Joergensen, L.2    Degn, H.3
  • 77
    • 0026128761 scopus 로고
    • Methanol suppression of trichloroethane degradation by Methylosinus trichosporium OB3b and methane-oxidizing mixed cultures
    • Eng W, Palumbo A, Haran S, and Standberg G. 1991. Methanol suppression of trichloroethane degradation by Methylosinus trichosporium OB3b and methane-oxidizing mixed cultures. App. Biochem. Biotechnol. 28/29: 887-889.
    • (1991) App. Biochem. Biotechnol. , vol.28-29 , pp. 887-889
    • Eng, W.1    Palumbo, A.2    Haran, S.3    Standberg, G.4
  • 78
    • 0021355141 scopus 로고
    • Effects of nitrapyrin [2-chloro-6-(trichloromethyl) pyridine] on the obligate methanotroph Methylosinus trichosporium OB3b
    • Topp E and Knowles R. 1984. Effects of nitrapyrin [2-chloro-6-(trichloromethyl) pyridine] on the obligate methanotroph Methylosinus trichosporium OB3b. App. Environ. Microbiol. 47: 258-262.
    • (1984) App. Environ. Microbiol. , vol.47 , pp. 258-262
    • Topp, E.1    Knowles, R.2
  • 79
    • 0023518366 scopus 로고
    • Methanol accumulation by resting cells of Methylosinus trichosporium (I)
    • Mehta P, Mishra S, and Ghose T. 1987. Methanol accumulation by resting cells of Methylosinus trichosporium (I). J. Gen. App. Microbiol. 33: 221-229.
    • (1987) J. Gen. App. Microbiol. , vol.33 , pp. 221-229
    • Mehta, P.1    Mishra, S.2    Ghose, T.3
  • 80
    • 0023678807 scopus 로고
    • Degradation of trans-1,2-dichloroethane by mixed and pure cultures of methanotrophic bacteria
    • Janssen D, Grobben G, Hoekstra R, Oldenhuis R, and Witholt B. 1988. Degradation of trans-1,2-dichloroethane by mixed and pure cultures of methanotrophic bacteria. App. Microbiol. Biotechnol. 29: 392-399.
    • (1988) App. Microbiol. Biotechnol. , vol.29 , pp. 392-399
    • Janssen, D.1    Grobben, G.2    Hoekstra, R.3    Oldenhuis, R.4    Witholt, B.5
  • 81
    • 0025198755 scopus 로고
    • Toxicity of 1,1,1-trichloroethane on a mixed culture of methane-oxidising bacteria
    • Broholm K, Jensen B, Christensen T, and Olsen L. 1990. Toxicity of 1,1,1-trichloroethane on a mixed culture of methane-oxidising bacteria. App. Environ. Microbiol. 56: 2488-2493.
    • (1990) App. Environ. Microbiol. , vol.56 , pp. 2488-2493
    • Broholm, K.1    Jensen, B.2    Christensen, T.3    Olsen, L.4
  • 82
    • 0026737501 scopus 로고
    • A sequencing biofilm reactor for the treatment of chlorinated solvents using methanotrophs
    • Speitel G and Leonard J. 1992. A sequencing biofilm reactor for the treatment of chlorinated solvents using methanotrophs. Water Environ. Res. 64: 712-719.
    • (1992) Water Environ. Res. , vol.64 , pp. 712-719
    • Speitel, G.1    Leonard, J.2
  • 83
    • 0025947803 scopus 로고
    • Biodegradation of chlorinated solvents in a sparged, methanotrophic biofilm reactor
    • Strand S, Wodrich J, and Stensel H. 1991. Biodegradation of chlorinated solvents in a sparged, methanotrophic biofilm reactor. Res. J. WPCF. 63: 859-866.
    • (1991) Res. J. WPCF , vol.63 , pp. 859-866
    • Strand, S.1    Wodrich, J.2    Stensel, H.3
  • 84
    • 0024764127 scopus 로고
    • Degradation of trichloroethylene and trans-1,2-dichloroethylene by a methanotrophic consortium in a fixed film packed bed reactor
    • Standberg G, Donaldson T, and Farr L. 1989. Degradation of trichloroethylene and trans-1,2-dichloroethylene by a methanotrophic consortium in a fixed film packed bed reactor. Environ. Sci. Technol. 23: 1422-1425.
    • (1989) Environ. Sci. Technol. , vol.23 , pp. 1422-1425
    • Standberg, G.1    Donaldson, T.2    Farr, L.3
  • 85
    • 0026832838 scopus 로고
    • Effects of adsorbents on degradation of toxic organic compounds by co-immobilised systems
    • Siahpush H, Lin J, and Wang H. 1992. Effects of adsorbents on degradation of toxic organic compounds by co-immobilised systems. Biotechnol. Bioeng. 39: 619-628.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 619-628
    • Siahpush, H.1    Lin, J.2    Wang, H.3
  • 86
    • 0027625494 scopus 로고
    • Biofilm reactors for treatment of gas streams containing chlorinated solvents
    • Speitel G and Mc Lay D. 1993. Biofilm reactors for treatment of gas streams containing chlorinated solvents. J. Environ. Eng. ASCE. 119: 4, 658-678.
    • (1993) J. Environ. Eng. ASCE , vol.119 , Issue.4 , pp. 658-678
    • Speitel, G.1    Mc Lay, D.2
  • 87
    • 0026816619 scopus 로고
    • Methanotrophic cometabolism of trichloroethylene (TCE) in a two stage bioreactor system
    • Mc Farlane M, Vogel C, and Spain J. 1992. Methanotrophic cometabolism of trichloroethylene (TCE) in a two stage bioreactor system. Water Res. 26: 259-265.
    • (1992) Water Res. , vol.26 , pp. 259-265
    • Mc Farlane, M.1    Vogel, C.2    Spain, J.3
  • 88
    • 0025907193 scopus 로고
    • Product toxicity and cometabolic competitive inhibition modelling of chloroform and trichloroethylene transformation by methanotrophic resting cells
    • Alvarez-Cohen L and Mc Carty P. 1991. Product toxicity and cometabolic competitive inhibition modelling of chloroform and trichloroethylene transformation by methanotrophic resting cells. Appl. Environ. Microbiol. 57: 1031-1037.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1031-1037
    • Alvarez-Cohen, L.1    Mc Carty, P.2
  • 89
    • 0026334031 scopus 로고
    • Two-stage dispersed growth treatment of halogenated aliphatic compounds by cometabolism
    • Alvarez-Cohen L and Mc Carty P. 1991. Two-stage dispersed growth treatment of halogenated aliphatic compounds by cometabolism. Environ. Sci. Technol. 25: 1387-1393.
    • (1991) Environ. Sci. Technol. , vol.25 , pp. 1387-1393
    • Alvarez-Cohen, L.1    Mc Carty, P.2
  • 90
    • 0017577979 scopus 로고
    • Purification and properties of the methane monooxygenase enzyme system from Methylosinus trichosporium OB3b
    • Tongue G, Harrison D, and Higgins I. 1977. Purification and properties of the methane monooxygenase enzyme system from Methylosinus trichosporium OB3b. J. Biochem. 161: 333-344.
    • (1977) J. Biochem. , vol.161 , pp. 333-344
    • Tongue, G.1    Harrison, D.2    Higgins, I.3
  • 91
    • 0026254044 scopus 로고
    • Enhanced biodegradation of polyaromatic hydrocarbons in the activated sludge process
    • Cardinal L and Stenstrom M, (1991) Enhanced biodegradation of polyaromatic hydrocarbons in the activated sludge process. Research Journal WCPF. 63: 950-957
    • (1991) Research Journal WCPF , vol.63 , pp. 950-957
    • Cardinal, L.1    Stenstrom, M.2
  • 92
    • 0024871951 scopus 로고
    • Experimental observations on flow patterns and energy losses from oscillatory flow in ducts containing sharp edges
    • Brunhold C, Hunns J, Mackley M, and Thompson J. 1989. Experimental observations on flow patterns and energy losses from oscillatory flow in ducts containing sharp edges. Chem. Eng. Sci. 44: 1227-1244
    • (1989) Chem. Eng. Sci. , vol.44 , pp. 1227-1244
    • Brunhold, C.1    Hunns, J.2    Mackley, M.3    Thompson, J.4
  • 93
    • 0028002904 scopus 로고
    • Biotransformation catalysed by the genus Rhodococcus
    • Warhurst A and Fewson C. 1994. Biotransformation catalysed by the genus Rhodococcus. Crit. Rev. Biotechnol. 14: 29-73.
    • (1994) Crit. Rev. Biotechnol. , vol.14 , pp. 29-73
    • Warhurst, A.1    Fewson, C.2
  • 94
    • 0023758106 scopus 로고
    • Bacterial metabolism of side chain fluorinated aromatics - Co-metabolism of 3-trifluoromethyl (Tfm)-benzoate by Pseudomonas putida (Arvilla) Mt2 and Rhodococcus rubropertinctus N657
    • Engesser K, Cain R, and Knackmuss H. 1988. Bacterial metabolism of side chain fluorinated aromatics - co-metabolism of 3-trifluoromethyl (Tfm)-benzoate by Pseudomonas putida (Arvilla) Mt2 and Rhodococcus rubropertinctus N657. Arch. Microbiol. 149: 3, 188-197.
    • (1988) Arch. Microbiol. , vol.149 , Issue.3 , pp. 188-197
    • Engesser, K.1    Cain, R.2    Knackmuss, H.3
  • 95
    • 0025901169 scopus 로고
    • Degradation of 2-methylalanine and chlorinated isomers of 2-methylalanine by Rhodococcus rhodochrous strain CTM
    • Fuchs K, Schriener A, and Lingens F. 1991. Degradation of 2-methylalanine and chlorinated isomers of 2-methylalanine by Rhodococcus rhodochrous strain CTM. J. Gen. Microbiol. 137: 2033-2039.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2033-2039
    • Fuchs, K.1    Schriener, A.2    Lingens, F.3
  • 96
    • 0025071808 scopus 로고
    • Kinetic studies of phenol degradation by Rhodococcus sp. P1 2. Continuous cultivation
    • Hensel J and Straube G. 1990. Kinetic studies of phenol degradation by Rhodococcus sp. P1 2. Continuous cultivation. Antonie Van Leeuwenhoek Int. J. Gen. Mol. Microbiol. 57: 1, 33-36.
    • (1990) Antonie Van Leeuwenhoek Int. J. Gen. Mol. Microbiol. , vol.57 , Issue.1 , pp. 33-36
    • Hensel, J.1    Straube, G.2
  • 97
    • 0022871539 scopus 로고
    • Degradation of polychlorinated phenols by Rhodococcus chlorophenolicus
    • Apajalahti J and Salkinoja-Salonen M. 1986. Degradation of polychlorinated phenols by Rhodococcus chlorophenolicus. Appl. Microbiol Biotechnol. 25: 62-67.
    • (1986) Appl. Microbiol Biotechnol. , vol.25 , pp. 62-67
    • Apajalahti, J.1    Salkinoja-Salonen, M.2
  • 98
    • 0022574369 scopus 로고
    • Rhodococcus chlorophenolicus sp. nov., a chlorophenol-mineralising actinomycete
    • Apajalahti J, Karpanoja J, and Salkinoja-Salonen M. 1986. Rhodococcus chlorophenolicus sp. nov., a chlorophenol-mineralising actinomycete. Int. Syst. Microbiol. 36: 246-251.
    • (1986) Int. Syst. Microbiol. , vol.36 , pp. 246-251
    • Apajalahti, J.1    Karpanoja, J.2    Salkinoja-Salonen, M.3
  • 99
    • 0021177784 scopus 로고
    • Degradation of o-toluidene by Rhodococcus rhodochrous
    • Appel M, Raabe T, and Lingens F. 1984. Degradation of o-toluidene by Rhodococcus rhodochrous. FEMS Microbiol. Lett. 24: 123-126.
    • (1984) FEMS Microbiol. Lett. , vol.24 , pp. 123-126
    • Appel, M.1    Raabe, T.2    Lingens, F.3
  • 100
    • 0026303461 scopus 로고
    • Dechlorination of pentachlorophenol by membrane bound enzymes of Rhodococcus chlorophenolicus PCP-1
    • Uotila J, Salkinoja-Salonen M, and Apajalahti J. 1991. Dechlorination of pentachlorophenol by membrane bound enzymes of Rhodococcus chlorophenolicus PCP-1. Biodegradation 2: 25-31.
    • (1991) Biodegradation , vol.2 , pp. 25-31
    • Uotila, J.1    Salkinoja-Salonen, M.2    Apajalahti, J.3
  • 101
    • 0025976406 scopus 로고
    • Molecular analysis of the methane monooxygenase (mmoX) gene-cluster of Methylosinus trichosporium OB3b
    • Cardy D, Laidler V, Salmond G, and Murrell J. 1991. Molecular analysis of the methane monooxygenase (mmoX) gene-cluster of Methylosinus trichosporium OB3b. Mol. Microbiol. 2: 335-342.
    • (1991) Mol. Microbiol. , vol.2 , pp. 335-342
    • Cardy, D.1    Laidler, V.2    Salmond, G.3    Murrell, J.4
  • 102
    • 0026774359 scopus 로고
    • Cloning and nucleotide sequence of the Csp1 gene encoding Ps1, one of the two major secreted proteins of Coryne-bacterium glutamicum - The deduced N-terminal region of Ps1 is similar to the Mycobacterium antigen 85 complex
    • Joliff G, Mathieu L, Hahn V, Bayan N, Duchiron F, Renaud M, Shechter E, and Leblon G. 1992. Cloning and nucleotide sequence of the Csp1 gene encoding Ps1, one of the two major secreted proteins of Coryne-bacterium glutamicum - the deduced N-terminal region of Ps1 is similar to the Mycobacterium antigen 85 complex. Mol. Microbiol. 6: 16, 2349-2362.
    • (1992) Mol. Microbiol. , vol.6 , Issue.16 , pp. 2349-2362
    • Joliff, G.1    Mathieu, L.2    Hahn, V.3    Bayan, N.4    Duchiron, F.5    Renaud, M.6    Shechter, E.7    Leblon, G.8
  • 103
    • 0028360496 scopus 로고
    • Trichloroethylene and chloroform degradation by a recombinant Pseudomonad expressing soluble methane monooxygenase from Methylosinus trichosporium OB3b
    • Jahng D and Wood T. 1994. Trichloroethylene and chloroform degradation by a recombinant Pseudomonad expressing soluble methane monooxygenase from Methylosinus trichosporium OB3b. Appl. Environ. Microbiol. 60: 7, 2473-2482.
    • (1994) Appl. Environ. Microbiol. , vol.60 , Issue.7 , pp. 2473-2482
    • Jahng, D.1    Wood, T.2
  • 104
  • 105
    • 0025369495 scopus 로고
    • Screening of obligate methanotrophs for soluble methane monooxygenase genes
    • Stainthorpe A, Salmond G, Dalton H, and Murrell J. 1990. Screening of obligate methanotrophs for soluble methane monooxygenase genes. FEMS Microbiol. Lett. 70: 211-216.
    • (1990) FEMS Microbiol. Lett. , vol.70 , pp. 211-216
    • Stainthorpe, A.1    Salmond, G.2    Dalton, H.3    Murrell, J.4
  • 106
    • 84994459439 scopus 로고
    • Biotransformation of chlorinated and non-chlorinated aromatics and alicyclics by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase
    • Stuttgart, in press
    • Sullivan J and Chase H. 1995. Biotransformation of chlorinated and non-chlorinated aromatics and alicyclics by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. 3rd International Symposium on Biochemical Engineering. Stuttgart, in press.
    • (1995) 3rd International Symposium on Biochemical Engineering
    • Sullivan, J.1    Chase, H.2
  • 107
    • 0026737501 scopus 로고
    • A sequencing biofilm reactor for the treatment of chlorinated solvents using methanotrophs
    • Speitel G and Leonard J. 1992. A sequencing biofilm reactor for the treatment of chlorinated solvents using methanotrophs. Water Environ. Res. 64: 5, 712-719.
    • (1992) Water Environ. Res. , vol.64 , Issue.5 , pp. 712-719
    • Speitel, G.1    Leonard, J.2
  • 108
    • 0024444795 scopus 로고
    • Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase
    • Oldenhuis R, Oedzes J, van der Waarde J, and Janssen D. 1991. Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. Appl. Environ. Microbiol. 55: 2819-2826.
    • (1991) Appl. Environ. Microbiol. , vol.55 , pp. 2819-2826
    • Oldenhuis, R.1    Oedzes, J.2    Van Der Waarde, J.3    Janssen, D.4
  • 109
    • 0028805359 scopus 로고
    • Cloning and expression of the s-triazine hydrolase gene (trza) from Rhodococcus corallinus and development of Rhodococcus recombinant strains capable of dealkylating and dechlorinating the herbicide atrazine
    • Shao Z, Seffens W, Mulbry W, and Behki R. 1995. Cloning and expression of the s-triazine hydrolase gene (trza) from Rhodococcus corallinus and development of Rhodococcus recombinant strains capable of dealkylating and dechlorinating the herbicide atrazine. J. Bacteriol. 177: 20, 5748-5755.
    • (1995) J. Bacteriol. , vol.177 , Issue.20 , pp. 5748-5755
    • Shao, Z.1    Seffens, W.2    Mulbry, W.3    Behki, R.4
  • 110
    • 0002708140 scopus 로고
    • The genetics and molecular biology of obligate methane-oxidising bacteria
    • Murrell J C and Dalton H. Eds., Plenum Press, New York
    • Murrell J. 1992. The genetics and molecular biology of obligate methane-oxidising bacteria. 115-148. (Murrell J C and Dalton H. Eds.), Methane and methanol utilisers. Plenum Press, New York.
    • (1992) Methane and Methanol Utilisers , pp. 115-148
    • Murrell, J.1
  • 111
    • 0027406522 scopus 로고
    • Detection of methylotrophic bacteria in natural samples by molecular probing techniques
    • Murrell J, Mc Gowan V, and Cardy D. 1993. Detection of methylotrophic bacteria in natural samples by molecular probing techniques. Chemosphere 26: 1-4, 1-11.
    • (1993) Chemosphere , vol.26 , pp. 1-4
    • Murrell, J.1    Mc Gowan, V.2    Cardy, D.3
  • 112
    • 0014793445 scopus 로고
    • Exospores and cysts formed by methane utilising bacteria
    • Whittenbury R, Davies S, and Davies J. 1970. Exospores and cysts formed by methane utilising bacteria. J. Gen. Microbiol. 61: 219-226.
    • (1970) J. Gen. Microbiol. , vol.61 , pp. 219-226
    • Whittenbury, R.1    Davies, S.2    Davies, J.3
  • 114
    • 0025020587 scopus 로고
    • Ribosomal RNA sequence analysis for the determination for phylogenetic relationship among methylotrophs
    • Tsuji K, Tsien H-C, Hanson R, De Palma S, Scholtz R, and La Roche S. 1990. Ribosomal RNA sequence analysis for the determination for phylogenetic relationship among methylotrophs. J. Gen. Microbiol. 136: 1-10.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1-10
    • Tsuji, K.1    Tsien, H.-C.2    Hanson, R.3    De Palma, S.4    Scholtz, R.5    La Roche, S.6
  • 115
    • 0025869973 scopus 로고
    • Contribution of genome characteristics to assessment of taxonomy of obligate methanotrophs
    • Bowman J, Sly L, and Hayward A. 1991. Contribution of genome characteristics to assessment of taxonomy of obligate methanotrophs. Int. J. Syst. Bacteriol. 41: 2, 301-305.
    • (1991) Int. J. Syst. Bacteriol. , vol.41 , Issue.2 , pp. 301-305
    • Bowman, J.1    Sly, L.2    Hayward, A.3
  • 117
    • 0031238586 scopus 로고    scopus 로고
    • Trichloroethylene and methane feeding strategies to sustain degradation by methanotrophic enrichment
    • Walter G, Strand S, Herwig R, Treat T, and Stensel S. 1997. Trichloroethylene and methane feeding strategies to sustain degradation by methanotrophic enrichment. Water Environ. Res. 69: 6, 1066-1074.
    • (1997) Water Environ. Res. , vol.69 , Issue.6 , pp. 1066-1074
    • Walter, G.1    Strand, S.2    Herwig, R.3    Treat, T.4    Stensel, S.5
  • 118
    • 0028008449 scopus 로고
    • A gas lift bioreactor for vapour phase destruction of chlorinated organics
    • Ensley B and Kurisko P. 1994. A gas lift bioreactor for vapour phase destruction of chlorinated organics. Appl. Environ. Microbiol. 60: 285-290.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 285-290
    • Ensley, B.1    Kurisko, P.2
  • 119
    • 0025848929 scopus 로고
    • Performance characterisation of model bioreactor for the biodegradation of trichloroethylene by Pseudomonas cepacia G4
    • Foison B and Chapman P. 1991. Performance characterisation of model bioreactor for the biodegradation of trichloroethylene by Pseudomonas cepacia G4. Appl. Environ. Microbiol. 57: 1602-1608.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1602-1608
    • Foison, B.1    Chapman, P.2
  • 120
    • 0028141688 scopus 로고
    • Cometabolic degradation of trichloroethylene by Pseudomonas cepacia G4 in a chemostat with toluene as the primary substrate
    • Landa A, Sipkema M, Weijma J, Beenackers A, Dolfing J, and Janssen D. 1994. Cometabolic degradation of trichloroethylene by Pseudomonas cepacia G4 in a chemostat with toluene as the primary substrate. Appl. Environ. Microbiol. 60: 3368-3374.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3368-3374
    • Landa, A.1    Sipkema, M.2    Weijma, J.3    Beenackers, A.4    Dolfing, J.5    Janssen, D.6
  • 122
    • 0343118728 scopus 로고    scopus 로고
    • Trichloroethylene mineralisation in a fixed film bioreactor using a pure culture expressing constitutively toluene ortho monooxygenase
    • Sun A and Wood T. 1997. Trichloroethylene mineralisation in a fixed film bioreactor using a pure culture expressing constitutively toluene ortho monooxygenase. Biotechnol. Bioeng. 55: 676-685.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 676-685
    • Sun, A.1    Wood, T.2
  • 127
    • 0031572223 scopus 로고    scopus 로고
    • Direct evidence for a soluble methane monooxygenase from Type I methanotrophic bacteria: Purification and properties of a soluble methane mono-oxygenase from Methylomonas sp. GYJ3
    • Shen R, Chi-Li Y, Qing-Quan Ma, and ShuBen L. 1997. Direct evidence for a soluble methane monooxygenase from Type I methanotrophic bacteria: purification and properties of a soluble methane mono-oxygenase from Methylomonas sp. GYJ3. Arch. Biochem. Biophys. 345: 2, 223-229.
    • (1997) Arch. Biochem. Biophys. , vol.345 , Issue.2 , pp. 223-229
    • Shen, R.1    Chi-Li, Y.2    Ma, Q.-Q.3    Shuben, L.4
  • 128
    • 0030986084 scopus 로고    scopus 로고
    • The soluble methane monooxygenase gene cluster of the trichloroethylene-degrading methanotroph Methylocystis sp. strain M
    • Mc Donald I, Uchiyama H, Kambe S, Yagi O, and Murrell J. 1997. The soluble methane monooxygenase gene cluster of the trichloroethylene-degrading methanotroph Methylocystis sp. strain M. Appl. Environ. Microbiol. 63: 5, 1898-1904.
    • (1997) Appl. Environ. Microbiol. , vol.63 , Issue.5 , pp. 1898-1904
    • Mc Donald, I.1    Uchiyama, H.2    Kambe, S.3    Yagi, O.4    Murrell, J.5
  • 129
    • 0031935375 scopus 로고    scopus 로고
    • Methane and trichloroethylene degradation by Methylosinus trichosporium OB3b expressing particulate methane monooxygenase
    • Sontoh S and Semrau J. 1998. Methane and trichloroethylene degradation by Methylosinus trichosporium OB3b expressing particulate methane monooxygenase. Appl. Environ. Microbiol. 64: 1106-1114.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1106-1114
    • Sontoh, S.1    Semrau, J.2
  • 130
    • 0030753674 scopus 로고    scopus 로고
    • Copper-dependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium OB3b
    • Nielsen A, Gerdes K, and Murrell J. 1997. Copper-dependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium OB3b. Mol. Microbiol. 25: 2. 399-409.
    • (1997) Mol. Microbiol. , vol.25 , Issue.2 , pp. 399-409
    • Nielsen, A.1    Gerdes, K.2    Murrell, J.3
  • 131
    • 0030885887 scopus 로고    scopus 로고
    • Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for the substrate gating and component interactions
    • Rosenzweig A, Brandstetter H, Whittington D, Nordlund P, Lippard S, and Frederick C. 1997. Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for the substrate gating and component interactions. Prot. Struct. Funct Genet. 29: 141-152.
    • (1997) Prot. Struct. Funct Genet. , vol.29 , pp. 141-152
    • Rosenzweig, A.1    Brandstetter, H.2    Whittington, D.3    Nordlund, P.4    Lippard, S.5    Frederick, C.6
  • 132
    • 0030848173 scopus 로고    scopus 로고
    • Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly and Gln modification
    • Lloyd J, Bhambra A, Murrell J, and Dalton H. 1997. Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly and Gln modification. Eur. J. Biochem. 248: 72-79.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 72-79
    • Lloyd, J.1    Bhambra, A.2    Murrell, J.3    Dalton, H.4
  • 133
    • 0030871234 scopus 로고    scopus 로고
    • Inhibition of methane oxidation by Methylococcus capsulatus (Bath) with hydrochlorofluorocarbons and fluorinated methanes
    • Matheson L, Jahnke L, and Oremland R. 1997. Inhibition of methane oxidation by Methylococcus capsulatus (Bath) with hydrochlorofluorocarbons and fluorinated methanes. Appl. Environ. Microbiol. 63: 2952-2956.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2952-2956
    • Matheson, L.1    Jahnke, L.2    Oremland, R.3
  • 134
    • 0030844081 scopus 로고    scopus 로고
    • Effect of chlorinated ethene conversion on viability and activity of Methylosinus trichosporium OB3b
    • van Hylckama Vlieg J, de Koning W, and Janssen D. 1997. Effect of chlorinated ethene conversion on viability and activity of Methylosinus trichosporium OB3b. Appl. Environ. Microbiol. 63: 4961-4964.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4961-4964
    • Van Hylckama Vlieg, J.1    De Koning, W.2    Janssen, D.3
  • 135
    • 0344505236 scopus 로고    scopus 로고
    • Isolation of copper biochelates from Methylosinus trichosporium OB3b and soluble methane monooxygenase mutants
    • Tellez C, Gaus K, Graham D, Arnold R, and Guzman R. 1998. Isolation of copper biochelates from Methylosinus trichosporium OB3b and soluble methane monooxygenase mutants. Appl. Environ.Microbiol. 64: 1115-1122.
    • (1998) Appl. Environ.Microbiol. , vol.64 , pp. 1115-1122
    • Tellez, C.1    Gaus, K.2    Graham, D.3    Arnold, R.4    Guzman, R.5
  • 136
    • 0030609921 scopus 로고    scopus 로고
    • A para-site-specific hydroxylation of aromatic compounds by Mycobacterium sp. strain 12523: Stabilization of the hydroxylation activity
    • Semba H and Sakano. 1997. A para-site-specific hydroxylation of aromatic compounds by Mycobacterium sp. strain 12523: stabilization of the hydroxylation activity. Appl. Microbiol. Biotechnol. 48: 256-260.
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 256-260
    • Semba, H.1    Sakano2
  • 137
    • 0031239118 scopus 로고    scopus 로고
    • Biodegradation of trichloroethylene by Methylocystis sp. strain M immobilized in gel beads in a fluidized bed reactor
    • Shimomura T, Suda F, Uchiyama H, and Yagi O. 1997. Biodegradation of trichloroethylene by Methylocystis sp. strain M immobilized in gel beads in a fluidized bed reactor. Water Res. 31: 9, 2383-2386.
    • (1997) Water Res. , vol.31 , Issue.9 , pp. 2383-2386
    • Shimomura, T.1    Suda, F.2    Uchiyama, H.3    Yagi, O.4
  • 138
    • 0031214794 scopus 로고    scopus 로고
    • Two-stage methanotrophic bioreactor for the treatment of chlorinated organic waste water
    • Chang H and Alvarez-Cohen L. 1997. Two-stage methanotrophic bioreactor for the treatment of chlorinated organic waste water. Water Res. 31: 8, 2026-2036.
    • (1997) Water Res. , vol.31 , Issue.8 , pp. 2026-2036
    • Chang, H.1    Alvarez-Cohen, L.2
  • 139
    • 0028008778 scopus 로고
    • Oxidation reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b
    • Paulsen K, Liu Y, Fox B, Lipscomb J, Munck J, and Stankovich T. 1994. Oxidation reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b. Biochemistry 33: 713-722.
    • (1994) Biochemistry , vol.33 , pp. 713-722
    • Paulsen, K.1    Liu, Y.2    Fox, B.3    Lipscomb, J.4    Munck, J.5    Stankovich, T.6
  • 140
    • 0029858185 scopus 로고    scopus 로고
    • Direct electrochemistry of the hydroxylase of the soluble methane monooxy genase from Methylococcus capsulatus (Bath)
    • Kazlauskaite H, Hill A, Wilkins P, and Dalton H. 1996. Direct electrochemistry of the hydroxylase of the soluble methane monooxy genase from Methylococcus capsulatus (Bath). Eur. J. Biochem. 241: 552-556.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 552-556
    • Kazlauskaite, H.1    Hill, A.2    Wilkins, P.3    Dalton, H.4
  • 141
    • 0026630133 scopus 로고
    • Methane monooxygenase-component B and reductase alter the regioselectivity of the hydroxylase component-catalysed reactions
    • Froland W, Andersson K, Lee S, Liu Y, and Lipscomb J. 1992. Methane monooxygenase-component B and reductase alter the regioselectivity of the hydroxylase component-catalysed reactions. J. Biol. Chem. 267: 17588-17597.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17588-17597
    • Froland, W.1    Andersson, K.2    Lee, S.3    Liu, Y.4    Lipscomb, J.5
  • 142
    • 0025766709 scopus 로고
    • Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath): Effects of protein B, reductase and substrate
    • Liu K and Lippard S. 1991. Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath): effects of protein B, reductase and substrate. J. Biol. Chem. 266: 12836-12839.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12836-12839
    • Liu, K.1    Lippard, S.2
  • 143
    • 0030904926 scopus 로고    scopus 로고
    • Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K
    • Davydov A, Davydov R, Graslund A, Lipscomb J, and Andersson K. 1997. Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K. J. Biol. Chem. 272: 7, 22-7026.
    • (1997) J. Biol. Chem. , vol.272 , Issue.7 , pp. 22-7026
    • Davydov, A.1    Davydov, R.2    Graslund, A.3    Lipscomb, J.4    Andersson, K.5
  • 144
    • 0025109631 scopus 로고
    • Soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Pilkington S and Dalton H. 1990. Soluble methane monooxygenase from Methylococcus capsulatus (Bath). Method. Enzymol. 188: 181-190.
    • (1990) Method. Enzymol. , vol.188 , pp. 181-190
    • Pilkington, S.1    Dalton, H.2
  • 145
    • 0026581822 scopus 로고
    • Bacterial resistance to inorganic mercury salts and organomercurials
    • Misra T. 1992. Bacterial resistance to inorganic mercury salts and organomercurials. Plasmid 27: 4-16.
    • (1992) Plasmid , vol.27 , pp. 4-16
    • Misra, T.1
  • 146
    • 0028918916 scopus 로고
    • DNA-bend modulation in a repressor-to-activator switching mechanism
    • Ansari A, Bradner J, and O'Halloran T. 1995. DNA-bend modulation in a repressor-to-activator switching mechanism. Nature 374: 371-375.
    • (1995) Nature , vol.374 , pp. 371-375
    • Ansari, A.1    Bradner, J.2    O'Halloran, T.3
  • 147
    • 0026549141 scopus 로고
    • Gene regulation of plasmid- And chromosome-determined inorganic ion transport in bacteria
    • Silver S and Walderhaug M. 1992. Gene regulation of plasmid-and chromosome-determined inorganic ion transport in bacteria. Microbiol. Rev. 56: 195-228.
    • (1992) Microbiol. Rev. , vol.56 , pp. 195-228
    • Silver, S.1    Walderhaug, M.2
  • 148
    • 0028101364 scopus 로고
    • Purification and characterisation of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper inducible promoters of Pseudomonas syringae
    • Mills S, Lim C, and Cooksey D. 1994. Purification and characterisation of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper inducible promoters of Pseudomonas syringae. Mol. Gen. Genet. 244: 341-351.
    • (1994) Mol. Gen. Genet. , vol.244 , pp. 341-351
    • Mills, S.1    Lim, C.2    Cooksey, D.3
  • 149
    • 0024707491 scopus 로고
    • Solubilization of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Smith D and Dalton H. 1989. Solubilization of methane monooxygenase from Methylococcus capsulatus (Bath). Eur. J. Biochem. 182: 667-671.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 667-671
    • Smith, D.1    Dalton, H.2
  • 150
    • 0028304991 scopus 로고
    • The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath)
    • Nguyen H, Shiemke A, Jacobs S, Hales B, Lidstrom M, and Chan S. 1994. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269: 14995-15005.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14995-15005
    • Nguyen, H.1    Shiemke, A.2    Jacobs, S.3    Hales, B.4    Lidstrom, M.5    Chan, S.6
  • 151
    • 0030067648 scopus 로고    scopus 로고
    • Membrane associated methane monooxygenase from Methylococcus capsulatus (Bath)
    • Zahn J and DiSpirito A. 1996. Membrane associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 178: 1018-1029.
    • (1996) J. Bacteriol. , vol.178 , pp. 1018-1029
    • Zahn, J.1    DiSpirito, A.2
  • 153
    • 2442722378 scopus 로고
    • Duplicate methane monooxygenase genes in methanotrophs. August 27-September 1, 1995, San Diego, California
    • 1 Compounds. August 27-September 1, 1995, San Diego, California.
    • (1995) 1 Compounds
    • Costello, A.1    Peeples, T.2    Lidstrom, M.3
  • 155
    • 0024565907 scopus 로고
    • Degradation of trichloroethylene by the ammonia-oxidising bacterium Nitrosomonas europaea
    • Arciero D, Vanelli T, Logan T, and Hooper A. 1989. Degradation of trichloroethylene by the ammonia-oxidising bacterium Nitrosomonas europaea. Biochem. Biophys. Res. Commun. 159: 640-643.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 640-643
    • Arciero, D.1    Vanelli, T.2    Logan, T.3    Hooper, A.4
  • 156
    • 0029786747 scopus 로고    scopus 로고
    • Biodegradation of individual and multiple chlorinated aliphatic compounds by methane-oxidizing cultures
    • Chang L and Alvarez-Cohen L. 1996. Biodegradation of individual and multiple chlorinated aliphatic compounds by methane-oxidizing cultures. Appl. Environ. Microbiol. 62: 3371-3377.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3371-3377
    • Chang, L.1    Alvarez-Cohen, L.2
  • 157
    • 0028894917 scopus 로고
    • Methanotrophic chloroethylene transformation capacities and 1,1-dichloroethene transformation product toxicity
    • Dolan M and Mc Carthy P. 1995. Methanotrophic chloroethylene transformation capacities and 1,1-dichloroethene transformation product toxicity. Environ. Sci. Technol. 29: 2741-2747.
    • (1995) Environ. Sci. Technol. , vol.29 , pp. 2741-2747
    • Dolan, M.1    Mc Carthy, P.2
  • 158
    • 0030044305 scopus 로고    scopus 로고
    • Degradation of trichloroethylene by methanol grown cultures of Methylosinus trichosporium OB3b PP358
    • Fitch M, Speitel G, and Georgiou. 1996. Degradation of trichloroethylene by methanol grown cultures of Methylosinus trichosporium OB3b PP358. Appl. Environ. Microbiol. 62: 1124-1128.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1124-1128
    • Fitch, M.1    Speitel, G.2    Georgiou3
  • 159
    • 0029808095 scopus 로고    scopus 로고
    • Transformation kinetics of chlorinated ethenes by Methylosinus trichosporium OB3b and detection of unstable epoxides by on-line gas chromatography
    • van Hylckama J, de Koning W, and Janssen D. 1996. Transformation kinetics of chlorinated ethenes by Methylosinus trichosporium OB3b and detection of unstable epoxides by on-line gas chromatography. Appl. Environ. Microbiol. 62: 3304-3312.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3304-3312
    • Van Hylckama, J.1    De Koning, W.2    Janssen, D.3
  • 160
    • 27844510034 scopus 로고
    • Studies of phosphate metabolism in obligate methanotrophs
    • Trotsenko Y and Shishkina T. 1990. Studies of phosphate metabolism in obligate methanotrophs. FEMS Microbiol. Rev. 87: 267-272.
    • (1990) FEMS Microbiol. Rev. , vol.87 , pp. 267-272
    • Trotsenko, Y.1    Shishkina, T.2
  • 161
    • 38249038312 scopus 로고
    • Measurement of methanotroph and methanogen signature phospholipids for the use in assessment of biomass and community structure in model systems
    • Nichols P, Manuso C, and White D. 1987. Measurement of methanotroph and methanogen signature phospholipids for the use in assessment of biomass and community structure in model systems. Org. Geochem. 11: 451-461.
    • (1987) Org. Geochem. , vol.11 , pp. 451-461
    • Nichols, P.1    Manuso, C.2    White, D.3
  • 162
    • 0018078085 scopus 로고
    • Growth of the methane-utilizing bacterium Methylococcus NCIMB 11083 in mineral salts medium with methanol as the sole carbon source
    • Linton J and Yokes J. 1986. Growth of the methane-utilizing bacterium Methylococcus NCIMB 11083 in mineral salts medium with methanol as the sole carbon source. FEMS Microbiol. Lett. 4: 125-128.
    • (1986) FEMS Microbiol. Lett. , vol.4 , pp. 125-128
    • Linton, J.1    Yokes, J.2
  • 163
    • 0024494909 scopus 로고
    • Metabolism of chlorinated methanes, ethanes, ethylenes by mixed bacterial cultures grown on methane
    • Henson J, Yates M, and Cochran J. 1989. Metabolism of chlorinated methanes, ethanes, ethylenes by mixed bacterial cultures grown on methane. J. Ind. Microbiol. 4: 29-35.
    • (1989) J. Ind. Microbiol. , vol.4 , pp. 29-35
    • Henson, J.1    Yates, M.2    Cochran, J.3
  • 164
    • 37049106234 scopus 로고
    • Oxidation of cyclopropane, methylcyclopropane, and arenes with the monooxygenase system from Methylococcus capsulatus (Bath)
    • Dalton H, Golding B, and Waters B. 1981. Oxidation of cyclopropane, methylcyclopropane, and arenes with the monooxygenase system from Methylococcus capsulatus (Bath). J. C. S Chem. Commun. 189: 482-483.
    • (1981) J. C. S Chem. Commun. , vol.189 , pp. 482-483
    • Dalton, H.1    Golding, B.2    Waters, B.3
  • 165
    • 85071534391 scopus 로고
    • Revised taxonomy of the methanotrophs - Description of Methylobactergen-Nov, validation of Methylosinus and Methylocystis species, and a proposal that the family Methylococcaceae includes only the group I methanotrophs
    • Bowman J, Sly L, Nichols P, and Hayward A. 1993. Revised taxonomy of the methanotrophs - description of Methylobactergen-Nov, validation of Methylosinus and Methylocystis species, and a proposal that the family Methylococcaceae includes only the group I methanotrophs. Int. J. Syst. Bacteriol. 44: 2, 375.
    • (1993) Int. J. Syst. Bacteriol. , vol.44 , Issue.2 , pp. 375
    • Bowman, J.1    Sly, L.2    Nichols, P.3    Hayward, A.4
  • 166
    • 0025869973 scopus 로고
    • Contribution of genome characteristics to assessment of taxonomy of obligate methanotrophs
    • Bowman J, Sly L, and Hayward A. 1991. Contribution of genome characteristics to assessment of taxonomy of obligate methanotrophs. Int. J. Syst. Bacteriol. 41: 2, 301-305.
    • (1991) Int. J. Syst. Bacteriol. , vol.41 , Issue.2 , pp. 301-305
    • Bowman, J.1    Sly, L.2    Hayward, A.3
  • 167
    • 0028874559 scopus 로고
    • An improved Escherichia coli Rhodococcus shuttle vector and plasmid transformation in Rhodococcus sp. using electroporation
    • Shao Z, Dick W, and Behki R. 1995. An improved Escherichia coli Rhodococcus shuttle vector and plasmid transformation in Rhodococcus sp. using electroporation. Lett. Appl. Microbiol. .21: 4, 261-266.
    • (1995) Lett. Appl. Microbiol. . , vol.21 , Issue.4 , pp. 261-266
    • Shao, Z.1    Dick, W.2    Behki, R.3
  • 168
    • 0029035951 scopus 로고
    • Cloning of the genes for degradation of the herbicides EPTC (s-ethyl dipropylthiocarbamate) and atrazine from Rhodococcus sp. strain TE1
    • Shao Z and Behki R. 1995. Cloning of the genes for degradation of the herbicides EPTC (s-ethyl dipropylthiocarbamate) and atrazine from Rhodococcus sp. strain TE1 Appl. Environ. Microbiol. 61: 5, 2061-2065.
    • (1995) Appl. Environ. Microbiol. , vol.61 , Issue.5 , pp. 2061-2065
    • Shao, Z.1    Behki, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.