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Volumn 193, Issue 5, 2011, Pages 1250-1258

Purification and characterization of dimethylsulfide monooxygenase from Hyphomicrobium sulfonivorans

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALDEHYDE; ALKANESULFONIC ACID; CADMIUM; DIBENZOTHIOPHENE DERIVATIVE; DIMETHYLSULFIDE MONOOXYGENASE; FLAVINE MONONUCLEOTIDE REDUCTASE; LEAD; MERCURY; NITRILOTRIACETIC ACID; ORGANOSULFUR DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79951641836     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00977-10     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 34250746955 scopus 로고    scopus 로고
    • Influence of divalent metal ions on degradation of dimethylsulphide by intact cells of Thiobacillus thioparus TK-m
    • Adoki, A. 2007. Influence of divalent metal ions on degradation of dimethylsulphide by intact cells of Thiobacillus thioparus Tk-m. Afr. J. Biotechnol. 6:1343-1347. (Pubitemid 46954112)
    • (2007) African Journal of Biotechnology , vol.6 , Issue.11 , pp. 1343-1347
    • Adoki, A.1
  • 3
    • 3543150204 scopus 로고    scopus 로고
    • Molecular detection and isolation of facultatively methylotrophic bacteria, including Methylobacterium podarium sp. nov., from the human foot microflora
    • Anesti, V., et al. 2004. Molecular detection and isolation of facultatively methylotrophic bacteria, including Methylobacterium podarium sp. nov., from the human foot microflora. Environ. Microbiol. 6:820-830.
    • (2004) Environ. Microbiol. , vol.6 , pp. 820-830
    • Anesti, V.1
  • 4
    • 1342308534 scopus 로고    scopus 로고
    • Environmental VOSCs-formation and degradation of dimethyl sulfide, methanethiol and related materials
    • Bentley, R., and T. G. Chasteen. 2004. Environmental VOSCs-formation and degradation of dimethyl sulfide, methanethiol and related materials. Chemosphere 55:291-317.
    • (2004) Chemosphere , vol.55 , pp. 291-317
    • Bentley, R.1    Chasteen, T.G.2
  • 5
    • 77957310399 scopus 로고    scopus 로고
    • Oxidation of dimethylsulfide to tetrathionate by Methylophaga thiooxidans sp. nov.: A new link in the sulfur cycle
    • Boden, R., D. P. Kelly, J. C. Murrell, and H. Schäfer. 2010. Oxidation of dimethylsulfide to tetrathionate by Methylophaga thiooxidans sp. nov.: a new link in the sulfur cycle. Environ. Microbiol. 12:2688-2699.
    • (2010) Environ. Microbiol. , vol.12 , pp. 2688-2699
    • Boden, R.1    Kelly, D.P.2    Murrell, J.C.3    Schäfer, H.4
  • 6
    • 0034084681 scopus 로고    scopus 로고
    • Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter
    • Borodina, E., D. P. Kelly, F. A. Rainey, N. L. Ward-Rainey, and A. P. Wood. 2000. Dimethylsulfone as a growth substrate for novel methylotrophic species of Hyphomicrobium and Arthrobacter. Arch. Microbiol. 173:425-437.
    • (2000) Arch. Microbiol. , vol.173 , pp. 425-437
    • Borodina, E.1    Kelly, D.P.2    Rainey, F.A.3    Ward-Rainey, N.L.4    Wood, A.P.5
  • 7
    • 0036172529 scopus 로고    scopus 로고
    • Enzymes of dimethylsulfone metabolism and the phylogenetic characterization of the facultative methylotrophs Arthrobacter sulfonivorans sp. nov., Arthrobacter methylotrophus sp. nov., and Hyphomicrobium sulfonivorans sp. nov
    • DOI 10.1007/s00203-001-0373-3
    • Borodina, E., et al. 2002. Enzymes of dimethylsulfone metabolism and the phylogenetic characterization of the facultative methylotrophs Arthrobacter sulfonivorans sp. nov., Arthrobacter methylotrophus sp. nov., and Hyphomicrobium sulfonivorans sp. nov. Arch. Microbiol. 177:173-183. (Pubitemid 34143417)
    • (2002) Archives of Microbiology , vol.177 , Issue.2 , pp. 173-183
    • Borodina, E.1    Kelly, D.P.2    Schumann, P.3    Rainey, F.A.4    Ward-Rainey, N.L.5    Wood, A.P.6
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0023525334 scopus 로고
    • Oceanic phytoplankton, atmospheric sulphur, cloud albedo and climate
    • Charlson, R. J., J. E. Lovelock, M. O. Andreae, and S. G. Warren. 1987. Oceanic phytoplankton, atmospheric sulphur, cloud albedo and climate. Nature 326:655-661.
    • (1987) Nature , vol.326 , pp. 655-661
    • Charlson, R.J.1    Lovelock, J.E.2    Andreae, M.O.3    Warren, S.G.4
  • 11
    • 23844537401 scopus 로고    scopus 로고
    • Adaptation and acclimatization to formaldehyde in methylotrophs capable of high-concentration formaldehyde detoxification
    • DOI 10.1099/mic.0.27912-0
    • Chongcharoen, R., T. J. Smith, K. P. Flint, and H. Dalton. 2005. Adaptation and acclimatization to formaldehyde in methylotrophs capable of high-concentration formaldehyde detoxification. Microbiology 151:2615-2622. (Pubitemid 41149784)
    • (2005) Microbiology , vol.151 , Issue.8 , pp. 2615-2622
    • Chongcharoen, R.1    Smith, T.J.2    Flint, K.P.3    Dalton, H.4
  • 12
    • 0019838795 scopus 로고
    • Dimethyl sulphoxide and dimethyl sulphide as a carbon, sulphur and energy source for growth of Hyphomicrobium S
    • De Bont, J. A. M., J. P. van Dijken, and W. Harder. 1981. Dimethyl sulphoxide and dimethyl sulphide as a carbon, sulphur and energy source for growth of Hyphomicrobium S. J. Gen. Microbiol. 127:315-323. (Pubitemid 12139384)
    • (1981) Journal of General Microbiology , vol.127 , Issue.2 , pp. 315-323
    • De Bont, J.A.M.1    Van Dijken, J.P.2    Harder, W.3
  • 13
    • 19944393048 scopus 로고
    • A new sensitive and specific test for the detection of aldehydes: Formation of 6-mercapto-3-substituted-striazole [4,3-b]-s-tetrazines
    • Camb.
    • Dickinson, R. G., and N. W. Jacobson. 1970. A new sensitive and specific test for the detection of aldehydes: formation of 6-mercapto-3-substituted- striazole [4,3-b]-s-tetrazines. Chem. Commun. (Camb.) 24:1719-1721.
    • (1970) Chem. Commun. , vol.24 , pp. 1719-1721
    • Dickinson, R.G.1    Jacobson, N.W.2
  • 14
    • 0034725580 scopus 로고    scopus 로고
    • A metal bridge between two enzyme families
    • Duewel, H. S., and R. W. Woodard. 2000. A metal bridge between two enzyme families. J. Biol. Chem. 275:22824-22831.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22824-22831
    • Duewel, H.S.1    Woodard, R.W.2
  • 15
    • 0037414756 scopus 로고    scopus 로고
    • Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor
    • DOI 10.1074/jbc.M209689200
    • Filisetti, L., N. Fontecave, and V. Nivière. 2003. Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor. J. Biol. Chem. 278:296-303. (Pubitemid 36043576)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 296-303
    • Filisetti, L.1    Fontecave, M.2    Niviere, V.3
  • 16
    • 0022515830 scopus 로고
    • The effect of methanethiol and methionine toxicity on the activities of cytochrome c oxidase and enzymes involved in protection from peroxidative damage
    • Finkelstein, A., and N. J. Benevenga. 1986. The effect of methanethiol and methionine toxicity on the activities of cytochrome c oxidase and enzymes involved in protection from peroxidative damage. J. Nutr. 116:204-215.
    • (1986) J. Nutr. , vol.116 , pp. 204-215
    • Finkelstein, A.1    Benevenga, N.J.2
  • 17
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • Gish, W., and D. J. States. 1993. Identification of protein coding regions by database similarity search. Nat. Genet. 3:266-272.
    • (1993) Nat. Genet. , vol.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 19
    • 0014505028 scopus 로고
    • Fixatives and fixation: A review
    • Hopwood, D. 1969. Fixatives and fixation: a review. Histochem. J. 1:323-360.
    • (1969) Histochem. J. , vol.1 , pp. 323-360
    • Hopwood, D.1
  • 20
    • 0029090782 scopus 로고
    • Identification of a flavin:NADH oxidoreductase involved in the biosyntheis of actinorhodin. Purification and characterisation of the recombinant enzyme
    • Kendrew, S. G., S. E. Harding, D. A. Hopwood, and E. N. G. Marsh. 1995. Identification of a flavin:NADH oxidoreductase involved in the biosyntheis of actinorhodin. Purification and characterisation of the recombinant enzyme. J. Biol. Chem. 270:17339-17343.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17339-17343
    • Kendrew, S.G.1    Harding, S.E.2    Hopwood, D.A.3    Marsh, E.N.G.4
  • 21
    • 0025206113 scopus 로고
    • Biological removal of dimethyl sulfide from sea-water
    • Kiene, R. P., and T. S. Bates. 1990. Biological removal of dimethyl sulfide from sea-water. Nature 345:702-705.
    • (1990) Nature , vol.345 , pp. 702-705
    • Kiene, R.P.1    Bates, T.S.2
  • 22
    • 0346220289 scopus 로고    scopus 로고
    • Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD
    • Kirchner, U., A. H. Westphal, R. Müller, and W. J. H. van Berkel. 2003. Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD. J. Biol. Chem. 278: 47545-47553.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47545-47553
    • Kirchner, U.1    Westphal, A.H.2    Müller, R.3    Van Berkel, W.J.H.4
  • 24
    • 0028265655 scopus 로고
    • Riboflavin synthesis genes are linked with the lux operon of Photobacterium phosphoreum
    • Lee, C. Y., D. J. Okane, and E. A. Meighen. 1994. Riboflavin synthesis genes are linked with the lux operon of Photobacterium phosphoreum. J. Bacteriol. 176:2100-2104.
    • (1994) J. Bacteriol. , vol.176 , pp. 2100-2104
    • Lee, C.Y.1    Okane, D.J.2    Meighen, E.A.3
  • 26
    • 0036016822 scopus 로고    scopus 로고
    • Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes
    • McDevitt, C. A., P. Hugenholtz, G. R. Hanson, and A. G. McEwan. 2002. Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes. Mol. Microbiol. 44:1575-1587.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1575-1587
    • McDevitt, C.A.1    Hugenholtz, P.2    Hanson, G.R.3    McEwan, A.G.4
  • 27
    • 0002017726 scopus 로고
    • nifH genes in obligate methane oxidising bacteria
    • Oakley, C. J., and J. C. Murrell. 1988. nifH genes in obligate methane oxidising bacteria. FEMS Microbiol. Lett. 49:53-57.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 53-57
    • Oakley, C.J.1    Murrell, J.C.2
  • 28
    • 0030854139 scopus 로고    scopus 로고
    • An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces viridifaciens. Cloning, analysis, and over-expression
    • Parry, R. J., and W. Li. 1997. An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces viridifaciens. Cloning, analysis, and over-expression. J. Biol. Chem. 272:23303-23311.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23303-23311
    • Parry, R.J.1    Li, W.2
  • 29
    • 0033635022 scopus 로고    scopus 로고
    • Artemis: Sequence visualisation and annotation
    • Rutherford, K., et al. 2000. Artemis: sequence visualisation and annotation. Bioinformatics 16:944-945.
    • (2000) Bioinformatics , vol.16 , pp. 944-945
    • Rutherford, K.1
  • 30
    • 34247628559 scopus 로고    scopus 로고
    • Isolation of Methylophaga spp. from marine dimethylsulfide-degrading enrichment cultures and identification of polypeptides induced during growth on dimethylsulfide
    • Schäfer, H. 2007. Isolation of Methylophaga spp. from marine dimethylsulfide-degrading enrichment cultures and identification of polypeptides induced during growth on dimethylsulfide. Appl. Environ. Microbiol. 73:2580-2591.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2580-2591
    • Schäfer, H.1
  • 31
    • 18944374389 scopus 로고    scopus 로고
    • Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidising bacteria
    • Schäfer, H., I. R. McDonald, P. D. Nightingale, and J. C. Murrell. 2005. Evidence for the presence of a CmuA methyltransferase pathway in novel marine methyl halide-oxidising bacteria. Environ. Microbiol. 7:839-852.
    • (2005) Environ. Microbiol. , vol.7 , pp. 839-852
    • Schäfer, H.1    McDonald, I.R.2    Nightingale, P.D.3    Murrell, J.C.4
  • 32
    • 74249115346 scopus 로고    scopus 로고
    • Microbial degradation of dimethylsulphide and related C1-sulphur compounds: Organisms and pathways controlling fluxes of sulphur in the biosphere
    • Schäfer, H., N. Myronova, and R. Boden. 2010. Microbial degradation of dimethylsulphide and related C1-sulphur compounds: organisms and pathways controlling fluxes of sulphur in the biosphere. J. Exp. Bot. 61:315-334.
    • (2010) J. Exp. Bot. , vol.61 , pp. 315-334
    • Schäfer, H.1    Myronova, N.2    Boden, R.3
  • 33
    • 0036081012 scopus 로고    scopus 로고
    • BRENDA, enzyme data and metabolic information
    • Schomburg, I., A. Chang, and D. Schomburg. 2002. BRENDA, enzyme data and metabolic function. Nucleic Acids Res. 30:47-49. (Pubitemid 34679500)
    • (2002) Nucleic Acids Research , vol.30 , Issue.1 , pp. 47-49
    • Schomburg, I.1    Chang, A.2    Schomburg, D.3
  • 34
    • 0001683356 scopus 로고
    • Isolation and physiological characterization of autotrophic sulfur bacteria oxidizing dimethyl disulfide as sole source of energy
    • Smith, N. A., and D. P. Kelly. 1988. Isolation and physiological characterization of autotrophic sulfur bacteria oxidizing dimethyl disulfide as sole source of energy. J. Gen. Microbiol. 134:1407-1417.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1407-1417
    • Smith, N.A.1    Kelly, D.P.2
  • 35
    • 7244236628 scopus 로고    scopus 로고
    • A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor
    • DOI 10.1074/jbc.M407722200
    • Valton, J., L. Filisetti, N. Fontecave, and V. Nivière. 2004. A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor. J. Biol. Chem. 279:44362-44369. (Pubitemid 39430840)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44362-44369
    • Valton, J.1    Filisetti, L.2    Fontecave, M.3    Niviere, V.4
  • 36
    • 0027489490 scopus 로고
    • A new mechanism for the aerobic catabolism of dimethyl sulfide
    • Visscher, P. T., and B. F. Taylor. 1993. A new mechanism for the aerobic catabolism of dimethyl sulfide. Appl. Environ. Microbiol. 59:3784-3789.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3784-3789
    • Visscher, P.T.1    Taylor, B.F.2
  • 37
    • 0029863065 scopus 로고    scopus 로고
    • Suicide inactivation of thioether S-methyltransferase by ethyl vinyl sulfide
    • Warner, D. R., and J. L. Hoffman. 1996. Suicide inactivation of thioether S-methyltransferase by ethyl vinyl sulfide. Biochemistry 35:4480-4484.
    • (1996) Biochemistry , vol.35 , pp. 4480-4484
    • Warner, D.R.1    Hoffman, J.L.2


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