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Volumn 74, Issue 13, 2008, Pages 4028-4035

Novel pathway for catabolism of the organic sulfur compound 3,3′-dithiodipropionic acid via 3-mercaptopropionic acid and 3-sulfinopropionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC COMPOUNDS; BIODEGRADATION; SULFATE MINERALS; SULFUR COMPOUNDS;

EID: 46949090171     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00422-08     Document Type: Article
Times cited : (27)

References (70)
  • 1
    • 0035872360 scopus 로고    scopus 로고
    • Thiols in coastal waters of the North Sea and English Channel
    • Al-Farawati, R., and C. M. G. van den Berg. 2001. Thiols in coastal waters of the North Sea and English Channel. Environ. Sci. Technol. 35:1902-1911.
    • (2001) Environ. Sci. Technol , vol.35 , pp. 1902-1911
    • Al-Farawati, R.1    van den Berg, C.M.G.2
  • 4
    • 0037154431 scopus 로고    scopus 로고
    • MOSC domains: Ancient, predicted sulfur-carrier domains, present in diverse metal-sulfur cluster biosynthesis proteins including molybdenum cofactor sulfurases
    • Anatharam, V., and L. Aravind. 2002. MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal-sulfur cluster biosynthesis proteins including molybdenum cofactor sulfurases. FEMS Microbiol. Lett. 207:55-61.
    • (2002) FEMS Microbiol. Lett , vol.207 , pp. 55-61
    • Anatharam, V.1    Aravind, L.2
  • 5
    • 0029187871 scopus 로고
    • Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism, from Yallowia lipolytica
    • Aoki, H., H. Uchiyama, H. Umetsu, and T. Tabuchi. 1995. Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism, from Yallowia lipolytica. Biosci. Biotechnol. Biochem. 59:1825-1828.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 1825-1828
    • Aoki, H.1    Uchiyama, H.2    Umetsu, H.3    Tabuchi, T.4
  • 6
    • 46949085731 scopus 로고    scopus 로고
    • Bachmann, B. J. 1987. Linkage map of Escherichia coli K-12, p. 807-876. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 7th ed., 2. American Society for Microbiology, Washington, DC.
    • Bachmann, B. J. 1987. Linkage map of Escherichia coli K-12, p. 807-876. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 7th ed., vol. 2. American Society for Microbiology, Washington, DC.
  • 7
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 8
    • 0023749235 scopus 로고
    • Pseudomonas oleovorans as a source of poly(β-hydroxyalkanoates) for potential applications as biodegradable polyesters
    • Brandl, H., A. Gross, R. W. Lenz, and R. C. Fuller. 1988. Pseudomonas oleovorans as a source of poly(β-hydroxyalkanoates) for potential applications as biodegradable polyesters. Appl. Environ. Microbiol. 54:1977-1982.
    • (1988) Appl. Environ. Microbiol , vol.54 , pp. 1977-1982
    • Brandl, H.1    Gross, A.2    Lenz, R.W.3    Fuller, R.C.4
  • 9
    • 0022397910 scopus 로고
    • Primary structure of the succinyl-CoA synthetase of Escherichia coli
    • Buck, D., M. E. Spencer, and J. R. Guest. 1985. Primary structure of the succinyl-CoA synthetase of Escherichia coli. Biochemistry 24:6245-6252.
    • (1985) Biochemistry , vol.24 , pp. 6245-6252
    • Buck, D.1    Spencer, M.E.2    Guest, J.R.3
  • 10
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection
    • Bullock, W. O., J. M. Fernandez, and J. M. Stuart. 1987. XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection. BioTechniques 5:376-379.
    • (1987) BioTechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Stuart, J.M.3
  • 11
    • 35148888991 scopus 로고    scopus 로고
    • Transcriptional response of Silicibacter pomeroyi DSS-3 to dimethylsulfoniopropionate (DMSP)
    • Bürgmann, H., E. C. Howard, W. Ye, F. Sun, S. Sun, S. Napierala, and M. A. Moran. 2007. Transcriptional response of Silicibacter pomeroyi DSS-3 to dimethylsulfoniopropionate (DMSP). Environ. Microbiol. 9:2742-2755.
    • (2007) Environ. Microbiol , vol.9 , pp. 2742-2755
    • Bürgmann, H.1    Howard, E.C.2    Ye, W.3    Sun, F.4    Sun, S.5    Napierala, S.6    Moran, M.A.7
  • 12
    • 28544450404 scopus 로고
    • The enzymatic oxidation of cysteamine to hypotaurine in the presence of sulfide
    • Cavallini, D., R. Scandurra, and C. De Marco. 1963. The enzymatic oxidation of cysteamine to hypotaurine in the presence of sulfide. J. Biol. Chem. 238:2999-3005.
    • (1963) J. Biol. Chem , vol.238 , pp. 2999-3005
    • Cavallini, D.1    Scandurra, R.2    De Marco, C.3
  • 13
    • 15444380484 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase
    • Chai, S. C., A. A. Jerkins, J. J. Banik, I. Shalev, J. L. Pinkham, P. C. Uden, and M. J. Maroney. 2004. Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase. J. Biol. Chem. 280:9865-9869.
    • (2004) J. Biol. Chem , vol.280 , pp. 9865-9869
    • Chai, S.C.1    Jerkins, A.A.2    Banik, J.J.3    Shalev, I.4    Pinkham, J.L.5    Uden, P.C.6    Maroney, M.J.7
  • 14
    • 0019859345 scopus 로고
    • ATP hydrolysis-dependent protease activity of the Lon (CapR) protein of Escherichia coli K-12
    • Charette, M. F., G. W. Henderson, and A. Markovitz. 1981. ATP hydrolysis-dependent protease activity of the Lon (CapR) protein of Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 78:4728-4732.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4728-4732
    • Charette, M.F.1    Henderson, G.W.2    Markovitz, A.3
  • 16
    • 34247523225 scopus 로고    scopus 로고
    • An investigation into the pharmacokinetics of 3-mercaptopropionic acid and development of a steady-state chemical seizure model using in vivo microdialysis and electrophysiological monitoring
    • Crick, E. W., I. Osorio, N. C. Bhavaraju, T. H. Linz, and C. E. Lunte. 2007. An investigation into the pharmacokinetics of 3-mercaptopropionic acid and development of a steady-state chemical seizure model using in vivo microdialysis and electrophysiological monitoring. Epilepsy Res. 74:116-125.
    • (2007) Epilepsy Res , vol.74 , pp. 116-125
    • Crick, E.W.1    Osorio, I.2    Bhavaraju, N.C.3    Linz, T.H.4    Lunte, C.E.5
  • 17
    • 0021795820 scopus 로고
    • Mitochondrial metabolism of 3-mercaptopropionic acid
    • Cuebas, D., J. D. Beckmann, F. E. Frerman, and H. Schulz. 1985. Mitochondrial metabolism of 3-mercaptopropionic acid. J. Biol. Chem. 260:7330-7336.
    • (1985) J. Biol. Chem , vol.260 , pp. 7330-7336
    • Cuebas, D.1    Beckmann, J.D.2    Frerman, F.E.3    Schulz, H.4
  • 18
    • 34548477656 scopus 로고    scopus 로고
    • Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase
    • Dominy, J. E., Jr., C. R. Simmons, L. L. Hirschberger, J. Hwang, R. M. Coloso, and M. H. Stipanuk. 2007. Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. J. Biol. Chem. 282:25189-25198.
    • (2007) J. Biol. Chem , vol.282 , pp. 25189-25198
    • Dominy Jr., J.E.1    Simmons, C.R.2    Hirschberger, L.L.3    Hwang, J.4    Coloso, R.M.5    Stipanuk, M.H.6
  • 19
    • 33746622949 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial cysteine dioxygenase: A new route of cysteine degradation for eubacteria
    • Dominy, J. E., Jr., C. R. Simmons, P. A. Karplus, A. M. Gehring, and M. H. Stipanuk. 2006. Identification and characterization of a bacterial cysteine dioxygenase: a new route of cysteine degradation for eubacteria. J. Bacteriol. 188:5561-5569.
    • (2006) J. Bacteriol , vol.188 , pp. 5561-5569
    • Dominy Jr., J.E.1    Simmons, C.R.2    Karplus, P.A.3    Gehring, A.M.4    Stipanuk, M.H.5
  • 20
    • 0022355317 scopus 로고
    • Substrate specificity of aspartate transcarbamylase. Interaction of the enzyme with analogs of aspartate and succinate
    • Foote, J., A. M. Lauritzen, and W. N. Lipscomb. 1985. Substrate specificity of aspartate transcarbamylase. Interaction of the enzyme with analogs of aspartate and succinate. J. Biol. Chem. 260:9624-9629.
    • (1985) J. Biol. Chem , vol.260 , pp. 9624-9629
    • Foote, J.1    Lauritzen, A.M.2    Lipscomb, W.N.3
  • 21
    • 0019371241 scopus 로고
    • Naturally occurring genetic transfer of hydrogen-oxidizing ability between strains of Alcaligenes eutrophus
    • Friedrich, B., C. Hogrefe, and H. G. Schlegel. 1981. Naturally occurring genetic transfer of hydrogen-oxidizing ability between strains of Alcaligenes eutrophus. J. Bacteriol. 147:198-205.
    • (1981) J. Bacteriol , vol.147 , pp. 198-205
    • Friedrich, B.1    Hogrefe, C.2    Schlegel, H.G.3
  • 22
    • 0021712959 scopus 로고
    • Heat shock regulatory gene htpR influences rates of protein degradation and expression of the Ion gene in Escherichia coli
    • Goff, S. A., L. P. Casson, and A. L. Goldberg. 1984. Heat shock regulatory gene htpR influences rates of protein degradation and expression of the Ion gene in Escherichia coli. Proc. Natl. Acad. Sci. USA 81:6647-6651.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6647-6651
    • Goff, S.A.1    Casson, L.P.2    Goldberg, A.L.3
  • 23
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 136:557-580.
    • (1983) J. Mol. Biol , vol.136 , pp. 557-580
    • Hanahan, D.1
  • 24
    • 33845408957 scopus 로고    scopus 로고
    • Distribution of the thiols glutathione and 3-mercaptopropionic acid in Connecticut lakes
    • Hu, H., G. Benoit, and S. E. Mylon. 2006. Distribution of the thiols glutathione and 3-mercaptopropionic acid in Connecticut lakes. Limnol. Oceanogr. 51:2763-2774.
    • (2006) Limnol. Oceanogr , vol.51 , pp. 2763-2774
    • Hu, H.1    Benoit, G.2    Mylon, S.E.3
  • 26
    • 0015947282 scopus 로고
    • Enzymatic and chemical synthesis of 3-sulfinopropionic acid an analog of succinic acid
    • Jollés-Bergeret, B. 1974. Enzymatic and chemical synthesis of 3-sulfinopropionic acid an analog of succinic acid. Eur. J. Biochem. 42:349-353.
    • (1974) Eur. J. Biochem , vol.42 , pp. 349-353
    • Jollés-Bergeret, B.1
  • 27
    • 34547758450 scopus 로고    scopus 로고
    • Cysteine dioxygenase: Structure and mechanism
    • Joseph, C. A., and M. J. Maroney. 2007. Cysteine dioxygenase: structure and mechanism. Chem. Commun. 2007:3338-3349.
    • (2007) Chem. Commun , vol.2007 , pp. 3338-3349
    • Joseph, C.A.1    Maroney, M.J.2
  • 28
    • 0034010828 scopus 로고    scopus 로고
    • Riding the sulfur cycle - metabolism of sulfonates and sulfate esters in gram-negative bacteria
    • Kertesz, M. A. 1999. Riding the sulfur cycle - metabolism of sulfonates and sulfate esters in gram-negative bacteria. FEMS Microbiol. Rev. 24:135-175.
    • (1999) FEMS Microbiol. Rev , vol.24 , pp. 135-175
    • Kertesz, M.A.1
  • 29
    • 0000782533 scopus 로고
    • Biotransformation of organosulphur compounds in sediments via 3-mercaptopropionate
    • Kiene, R. P., and B. F. Taylor. 1988. Biotransformation of organosulphur compounds in sediments via 3-mercaptopropionate. Nature 332:148-150.
    • (1988) Nature , vol.332 , pp. 148-150
    • Kiene, R.P.1    Taylor, B.F.2
  • 30
    • 0033832734 scopus 로고    scopus 로고
    • New and important roles for DMSP in marine microbial communities
    • Kiene, R. P., L. J. Linn, and J. A. Bruton. 2000. New and important roles for DMSP in marine microbial communities. J. Sea Res. 43:209-224.
    • (2000) J. Sea Res , vol.43 , pp. 209-224
    • Kiene, R.P.1    Linn, L.J.2    Bruton, J.A.3
  • 31
    • 0025058973 scopus 로고
    • Sulfur-containing amino acids as precursors of thiols in anoxic coastal sediments
    • Kiene, R. P., K. D. Malloy, and F. B. Taylor. 1990. Sulfur-containing amino acids as precursors of thiols in anoxic coastal sediments. Appl. Environ. Microbiol. 56:156-161.
    • (1990) Appl. Environ. Microbiol , vol.56 , pp. 156-161
    • Kiene, R.P.1    Malloy, K.D.2    Taylor, F.B.3
  • 32
    • 0022555843 scopus 로고
    • The heat shock response
    • Lindquist, S. 1986. The heat shock response. Annu. Rev. Biochem. 55:1151-1191.
    • (1986) Annu. Rev. Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 36
    • 0142093990 scopus 로고    scopus 로고
    • Novel precursor substrates for polythioesters (PTE) and limits of PTE biosynthesis in Ralstonia eutropha
    • Lütke-Eversloh, T., and A. Steinbüchel. 2003. Novel precursor substrates for polythioesters (PTE) and limits of PTE biosynthesis in Ralstonia eutropha. FEMS Microbiol. Lett. 221:191-196.
    • (2003) FEMS Microbiol. Lett , vol.221 , pp. 191-196
    • Lütke-Eversloh, T.1    Steinbüchel, A.2
  • 37
    • 0036163665 scopus 로고    scopus 로고
    • Characterization of biological polythioesters: Physical properties of novel copolymers synthesized by Ralstonia eutropha
    • Lütke-Eversloh, T., J. Kawada, R. H. Marchessault, and A. Steinbüchel. 2002. Characterization of biological polythioesters: physical properties of novel copolymers synthesized by Ralstonia eutropha. Biomacromolecules 3:159-166.
    • (2002) Biomacromolecules , vol.3 , pp. 159-166
    • Lütke-Eversloh, T.1    Kawada, J.2    Marchessault, R.H.3    Steinbüchel, A.4
  • 38
    • 0035155574 scopus 로고    scopus 로고
    • Identification of a new class of biopolymer: Bacterial synthesis of sulfur-containing polymer with thioester linkages
    • Lütke-Eversloh, T., K. Bergander, H. Luftmann, and A. Steinbüchel. 2001. Identification of a new class of biopolymer: bacterial synthesis of sulfur-containing polymer with thioester linkages. Microbiology 147:11-19.
    • (2001) Microbiology , vol.147 , pp. 11-19
    • Lütke-Eversloh, T.1    Bergander, K.2    Luftmann, H.3    Steinbüchel, A.4
  • 39
    • 85010439719 scopus 로고
    • A procedure for the isolation of desoxyribonucleic acid from microorganisms
    • Marmur, J. 1961. A procedure for the isolation of desoxyribonucleic acid from microorganisms. J. Mol. Biol. 1:208-218.
    • (1961) J. Mol. Biol , vol.1 , pp. 208-218
    • Marmur, J.1
  • 40
    • 46949096334 scopus 로고    scopus 로고
    • Massey, V. 1963. Lipoyldehydrogenase, p. 275-306. In P. D. Boyer, H. Lardy, and K. Myrback (ed.), The enzymes, 2nd ed., 7. Academic Press, New York, NY.
    • Massey, V. 1963. Lipoyldehydrogenase, p. 275-306. In P. D. Boyer, H. Lardy, and K. Myrback (ed.), The enzymes, 2nd ed., vol. 7. Academic Press, New York, NY.
  • 43
    • 0000386375 scopus 로고
    • Biogeochemical cycling of sulfur-thiols in coastal marine sediments
    • M. Sohn ed, American Chemical Society, Washington, DC
    • Mopper, K., and B. F. Taylor. 1986. Biogeochemical cycling of sulfur-thiols in coastal marine sediments, p. 324-339. In M. Sohn (ed.), Organic marine geochemistry. American Chemical Society, Washington, DC.
    • (1986) Organic marine geochemistry , pp. 324-339
    • Mopper, K.1    Taylor, B.F.2
  • 44
    • 0023691425 scopus 로고
    • Genetic application of an inverse polymerase chain reaction
    • Ochman, H., A. L. Gerber, and D. L. Hartl. 1988. Genetic application of an inverse polymerase chain reaction. Genetics 120:621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.L.2    Hartl, D.L.3
  • 45
    • 0025344277 scopus 로고
    • Isolation of prokaryotic RNA and detection of specific mRNA with biotinylated probes
    • Oelmüller, U., N. Krüger, A. Steinbüchel, and C. G. Friedrich. 1990. Isolation of prokaryotic RNA and detection of specific mRNA with biotinylated probes. J. Microbiol. Methods 11:73-84.
    • (1990) J. Microbiol. Methods , vol.11 , pp. 73-84
    • Oelmüller, U.1    Krüger, N.2    Steinbüchel, A.3    Friedrich, C.G.4
  • 46
    • 0021266784 scopus 로고
    • lon gene product of Escherichia coli is a heat shock protein
    • Phillips, T. A., R. A. VanBogelen, and F. C. Neidhardt. 1984. lon gene product of Escherichia coli is a heat shock protein. J. Bacteriol. 159:283-287.
    • (1984) J. Bacteriol , vol.159 , pp. 283-287
    • Phillips, T.A.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 47
    • 0021856524 scopus 로고
    • 3-Mercaptopropionic acid, a potent inhibitor of fatty acid oxidation in rat heart mitochondria
    • Sabbagh, E., D. Cuebas, and H. Schulz. 1985. 3-Mercaptopropionic acid, a potent inhibitor of fatty acid oxidation in rat heart mitochondria. J. Biol. Chem. 260:7337-7342.
    • (1985) J. Biol. Chem , vol.260 , pp. 7337-7342
    • Sabbagh, E.1    Cuebas, D.2    Schulz, H.3
  • 49
    • 34250134974 scopus 로고
    • Electrochemical studies on the composition, stability-constants and thermodynamics of Ti (I) complexes with dithiodipropionic acid
    • Saxena, R. S., and A. Gupta. 1984. Electrochemical studies on the composition, stability-constants and thermodynamics of Ti (I) complexes with dithiodipropionic acid. Monatsschr. Chem. 115:1293-1298.
    • (1984) Monatsschr. Chem , vol.115 , pp. 1293-1298
    • Saxena, R.S.1    Gupta, A.2
  • 50
    • 34250969714 scopus 로고
    • Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen.
    • Schlegel, H. G., H. Kaltwasser, and G. Gottschalk. 1961. Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38:209-222.
    • (1961) Arch. Mikrobiol , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 51
    • 0021205685 scopus 로고
    • High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-mob transposon
    • Simon, R. 1984. High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-mob transposon. Mol. Gen. Genet. 196:413-420.
    • (1984) Mol. Gen. Genet , vol.196 , pp. 413-420
    • Simon, R.1
  • 52
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 53
    • 0014927018 scopus 로고
    • 3-Mercaptopropionic acid: Convulsant and lethal properties compared with other sulfur-convulsants; protection therefrom
    • Sprince, H., C. M. Parker, and G. G. Smith. 1970. 3-Mercaptopropionic acid: convulsant and lethal properties compared with other sulfur-convulsants; protection therefrom. Agents Actions 1:231-233.
    • (1970) Agents Actions , vol.1 , pp. 231-233
    • Sprince, H.1    Parker, C.M.2    Smith, G.G.3
  • 54
    • 0030714624 scopus 로고    scopus 로고
    • Propionate oxidation in Escherichia coli: Evidence for operation of a methylcitrate cycle in bacteria
    • Textor, S., V. F. Wendisch, A. A. Graf, U. Müller, M. I. Linder, D. Linder, and W. Buckel. 1997. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168:428-436.
    • (1997) Arch. Microbiol , vol.168 , pp. 428-436
    • Textor, S.1    Wendisch, V.F.2    Graf, A.A.3    Müller, U.4    Linder, M.I.5    Linder, D.6    Buckel, W.7
  • 55
    • 13544260530 scopus 로고    scopus 로고
    • Application of the BPEC pathway for large-scale biotechnological production of poly(3-mercaptopropionate) by recombinant Escherichia coli including a novel in situ isolation method
    • Thakor, N., T. Lütke-Eversloh, and A. Steinbüchel. 2005. Application of the BPEC pathway for large-scale biotechnological production of poly(3-mercaptopropionate) by recombinant Escherichia coli including a novel in situ isolation method. Appl. Environ. Microbiol. 71:835-841.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 835-841
    • Thakor, N.1    Lütke-Eversloh, T.2    Steinbüchel, A.3
  • 56
    • 0025124122 scopus 로고
    • Formation of blends of various poly(3-hydroxyalkanoic acids) by a recombinant strain of Pseudomonas oleovorans
    • Timm, A., D. Byrom, and A. Steinbüchel. 1990. Formation of blends of various poly(3-hydroxyalkanoic acids) by a recombinant strain of Pseudomonas oleovorans. Appl. Microbiol. Biotechnol. 33:296-301.
    • (1990) Appl. Microbiol. Biotechnol , vol.33 , pp. 296-301
    • Timm, A.1    Byrom, D.2    Steinbüchel, A.3
  • 58
    • 0032313398 scopus 로고    scopus 로고
    • A potentially biodegradable polyamide containing disulfide bonds as a positive material for secondary batteries
    • Tsutsumi, H., S. Okada, and T. Oishi. 1998. A potentially biodegradable polyamide containing disulfide bonds as a positive material for secondary batteries. Electrochim. Acta 43:427-429.
    • (1998) Electrochim. Acta , vol.43 , pp. 427-429
    • Tsutsumi, H.1    Okada, S.2    Oishi, T.3
  • 59
    • 0009508243 scopus 로고    scopus 로고
    • Optimized determination of cystine/cysteine and acid-stable amino acids from a single hydrolysate of casein- and sorghum-based diet and digesta samples
    • Tuan, Y.-H., and R. D. Phillips. 1997. Optimized determination of cystine/cysteine and acid-stable amino acids from a single hydrolysate of casein- and sorghum-based diet and digesta samples. J. Agric. Food Chem. 45:3535-3540.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 3535-3540
    • Tuan, Y.-H.1    Phillips, R.D.2
  • 60
    • 0002713471 scopus 로고    scopus 로고
    • Anaerobic microorganisms involved in the degradation of DMS(P)
    • R. P. Kiene, P. T. Visscher, M. D. Keller, and G. O. Kirst ed, Plenum Press, New York, NY
    • van der Maarel, M. J. E. C., and T. A. Hansen. 1996. Anaerobic microorganisms involved in the degradation of DMS(P), p. 351-360. In R. P. Kiene, P. T. Visscher, M. D. Keller, and G. O. Kirst (ed.), Biological and environmental chemistry of DMSP and related sulfonium compounds. Plenum Press, New York, NY.
    • (1996) Biological and environmental chemistry of DMSP and related sulfonium compounds , pp. 351-360
    • van der Maarel, M.J.E.C.1    Hansen, T.A.2
  • 61
    • 0028855425 scopus 로고
    • Methanogenic conversion of 3-S-methylmercaptopropionate to 3-mercaptopropionate
    • van der Maarel, M. J. E. C., M. Jansen, and T. A. Hansen. 1995. Methanogenic conversion of 3-S-methylmercaptopropionate to 3-mercaptopropionate. Appl. Environ. Microbiol. 61:48-51.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 48-51
    • van der Maarel, M.J.E.C.1    Jansen, M.2    Hansen, T.A.3
  • 62
    • 1642270691 scopus 로고    scopus 로고
    • Use of a novel fluorinated organosulfur compound to isolate bacteria capable of carbon-sulfur bond cleavage
    • Van Hamme, J. D., P. M. Fedorak, J. M. Foght, M. R. Gray, and H. D. Dettman. 2004. Use of a novel fluorinated organosulfur compound to isolate bacteria capable of carbon-sulfur bond cleavage. Appl. Environ. Microbiol. 70:1487-1493.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 1487-1493
    • Van Hamme, J.D.1    Fedorak, P.M.2    Foght, J.M.3    Gray, M.R.4    Dettman, H.D.5
  • 63
    • 34249764344 scopus 로고
    • Synthesis and radioprotective properties of 2-arylethylammonium salts of sulfinic acids
    • Vasil'eva, T. P., and V. V. Znamenskii. 1994. Synthesis and radioprotective properties of 2-arylethylammonium salts of sulfinic acids. Pharmaceut. Chem. J. 28:47-50.
    • (1994) Pharmaceut. Chem. J , vol.28 , pp. 47-50
    • Vasil'eva, T.P.1    Znamenskii, V.V.2
  • 64
    • 0028000333 scopus 로고
    • Demethylation of dimethylsulfoniopropionate to 3-mercaptopropionate by an aerobic marine bacterium
    • Visscher, P. T., and B. F. Taylor. 1994. Demethylation of dimethylsulfoniopropionate to 3-mercaptopropionate by an aerobic marine bacterium. Appl. Environ. Microbiol. 60:4617-4619.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 4617-4619
    • Visscher, P.T.1    Taylor, B.F.2
  • 65
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases
    • F. Muller ed, CRC Press, Boca Raton, FL
    • Williams, C. H., Jr. 1992. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases, p. 121-211. In F. Muller (ed.), Chemistry and biochemistry of flavoenzymes, vol. III. CRC Press, Boca Raton, FL.
    • (1992) Chemistry and biochemistry of flavoenzymes , vol.3 , pp. 121-211
    • Williams Jr., C.H.1
  • 66
    • 33745302842 scopus 로고    scopus 로고
    • Tetrathiobacter mimigardefordensis sp. nov., isolated from compost, a betaproteobacterium capable of utilizing the organic disulfide 3,3′-dithiodipropionic acid
    • Wübbeler, J. H., T. Lütke-Eversloh, P. Vandamme, S. Van Trappen, and A. Steinbüchel. 2006. Tetrathiobacter mimigardefordensis sp. nov., isolated from compost, a betaproteobacterium capable of utilizing the organic disulfide 3,3′-dithiodipropionic acid. Int. J. Syst. Evol. Microbiol. 56:1305-1310.
    • (2006) Int. J. Syst. Evol. Microbiol , vol.56 , pp. 1305-1310
    • Wübbeler, J.H.1    Lütke-Eversloh, T.2    Vandamme, P.3    Van Trappen, S.4    Steinbüchel, A.5
  • 67
    • 0036952070 scopus 로고    scopus 로고
    • Dimethylsulfoniopropionate: Its sources, role in the marine food web, and biological degradation to dimethylsulfide
    • Yoch, D. C. 2002. Dimethylsulfoniopropionate: its sources, role in the marine food web, and biological degradation to dimethylsulfide. Appl. Environ. Microbiol. 68:5804-5815.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 5804-5815
    • Yoch, D.C.1
  • 68
    • 33847611960 scopus 로고    scopus 로고
    • Electrocatalytic activity of three-dimensional monolayer of 3-mercaptopropionic acid assembled on gold nanoparticle arrays
    • Zhang, J., and M. Oyama. 2007. Electrocatalytic activity of three-dimensional monolayer of 3-mercaptopropionic acid assembled on gold nanoparticle arrays. Electrochem. Commun. 9:459-464.
    • (2007) Electrochem. Commun , vol.9 , pp. 459-464
    • Zhang, J.1    Oyama, M.2
  • 69
    • 9244238730 scopus 로고    scopus 로고
    • Thiols in wetland interstitial waters and their role in mercury and methylmercury speciation
    • Zhang, J., F. Wang, J. D. House, and B. Page. 2004. Thiols in wetland interstitial waters and their role in mercury and methylmercury speciation. Limnol. Oceanogr. 49:2276-2286.
    • (2004) Limnol. Oceanogr , vol.49 , pp. 2276-2286
    • Zhang, J.1    Wang, F.2    House, J.D.3    Page, B.4
  • 70
    • 0027331573 scopus 로고
    • Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity
    • Ziemienowicz, A., D. Skowyra, J. Zeilstra-Ryalls, O. Fayet, C. Georgopoulos, and M. Zylicz. 1993. Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity J. Biol. Chem. 268:25425-25431.
    • (1993) J. Biol. Chem , vol.268 , pp. 25425-25431
    • Ziemienowicz, A.1    Skowyra, D.2    Zeilstra-Ryalls, J.3    Fayet, O.4    Georgopoulos, C.5    Zylicz, M.6


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