메뉴 건너뛰기




Volumn 43, Issue 7, 2008, Pages 753-757

A proteomic analysis of Klebsiella oxytoca after exposure to succinonitrile

Author keywords

Biodegradation; Klebsiella oxytoca; MALDI TOF MS; Oxidative stress; Proteome; Succinonitrile

Indexed keywords

BACTERIA; BIODEGRADATION; BIOSYNTHESIS; OXIDATIVE STRESS; POLYACRYLATES;

EID: 44249108534     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.03.001     Document Type: Article
Times cited : (10)

References (33)
  • 2
    • 0002894473 scopus 로고
    • Setting the world of nitrile chemistry afire
    • Henqaban J.F., and Idol J.D. Setting the world of nitrile chemistry afire. Chem Eng News 49 (1971) 16-18
    • (1971) Chem Eng News , vol.49 , pp. 16-18
    • Henqaban, J.F.1    Idol, J.D.2
  • 3
    • 0037209758 scopus 로고    scopus 로고
    • The nitrile-degrading enzymes: current status and future prospects
    • Banerjee A., Sharma R., and Banerjee U.C. The nitrile-degrading enzymes: current status and future prospects. Appl Microbiol Biotechnol 60 (2002) 33-44
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 33-44
    • Banerjee, A.1    Sharma, R.2    Banerjee, U.C.3
  • 4
    • 0029160202 scopus 로고
    • Pseudomonas marginalis: its degradative capability on organic nitriles and amides
    • Babu G.R., Wolfram J.H., Marian J.M., and Chapatwala K.D. Pseudomonas marginalis: its degradative capability on organic nitriles and amides. Appl Microbiol Biotechnol 43 (1995) 739-745
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 739-745
    • Babu, G.R.1    Wolfram, J.H.2    Marian, J.M.3    Chapatwala, K.D.4
  • 5
  • 8
    • 0031036437 scopus 로고    scopus 로고
    • The effect of growth conditions on survival and recovery of Klebeiella oxytoca after exposure to chlorine
    • Power K.N., Schneider R.P., and Marshall K.C. The effect of growth conditions on survival and recovery of Klebeiella oxytoca after exposure to chlorine. Water Res 1 (1997) 135-139
    • (1997) Water Res , vol.1 , pp. 135-139
    • Power, K.N.1    Schneider, R.P.2    Marshall, K.C.3
  • 9
    • 34548066021 scopus 로고    scopus 로고
    • The salt stress relief and growth promotion effect of Rs-5 on the cotton
    • Yue H., Mo W., Li C., Zheng Y., and Li H. The salt stress relief and growth promotion effect of Rs-5 on the cotton. Plant Soil 297 (2007) 139-145
    • (2007) Plant Soil , vol.297 , pp. 139-145
    • Yue, H.1    Mo, W.2    Li, C.3    Zheng, Y.4    Li, H.5
  • 10
  • 11
    • 33846366010 scopus 로고    scopus 로고
    • Characterization of the proteins of bacterial strain isolated from contaminated site involved in heavy metal resistance-A proteomic approach
    • Bar C., Patil R., Doshi J., Kulkarni M.J., and Gade W.N. Characterization of the proteins of bacterial strain isolated from contaminated site involved in heavy metal resistance-A proteomic approach. J Biotechnol 128 (2007) 444-451
    • (2007) J Biotechnol , vol.128 , pp. 444-451
    • Bar, C.1    Patil, R.2    Doshi, J.3    Kulkarni, M.J.4    Gade, W.N.5
  • 12
    • 34547504157 scopus 로고    scopus 로고
    • A proteomic analysis of Corynebacterium glutamicum after exposure to the herbicide 2,4-dichlorophenoxy acetic acid (2,4-D)
    • Fanous A., Weiland F., Luck C., Grog A., Friess A., and Parlar H. A proteomic analysis of Corynebacterium glutamicum after exposure to the herbicide 2,4-dichlorophenoxy acetic acid (2,4-D). Chemosphere 69 (2007) 25-31
    • (2007) Chemosphere , vol.69 , pp. 25-31
    • Fanous, A.1    Weiland, F.2    Luck, C.3    Grog, A.4    Friess, A.5    Parlar, H.6
  • 13
    • 0037332546 scopus 로고    scopus 로고
    • Biotransformation of cyanide to methane and ammonium by Klebsiella oxytoca
    • Kao C.M., Liu J.K., Lou H.R., Lin C.S., and Chen S.C. Biotransformation of cyanide to methane and ammonium by Klebsiella oxytoca. Chemosphere 50 (2003) 1055-1061
    • (2003) Chemosphere , vol.50 , pp. 1055-1061
    • Kao, C.M.1    Liu, J.K.2    Lou, H.R.3    Lin, C.S.4    Chen, S.C.5
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0002995454 scopus 로고
    • Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Beier H., and Cross H.J. Improved silver staining of plant-proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 69 (1987) 25-31
    • (1987) Electrophoresis , vol.69 , pp. 25-31
    • Blum, H.1    Beier, H.2    Cross, H.J.3
  • 16
    • 0035315481 scopus 로고    scopus 로고
    • Purification and characterization of black porgy muscle Cu/Zn superoxide dismutase
    • Lin C.T., Lee T.L., Duan K.J., and Su J.C. Purification and characterization of black porgy muscle Cu/Zn superoxide dismutase. Zoolog Stud 40 (2001) 84-90
    • (2001) Zoolog Stud , vol.40 , pp. 84-90
    • Lin, C.T.1    Lee, T.L.2    Duan, K.J.3    Su, J.C.4
  • 17
    • 12144289472 scopus 로고    scopus 로고
    • Discovery of superoxide reductase: an historical perspective
    • Niviere V., and Fontecave M. Discovery of superoxide reductase: an historical perspective. J Biol Inorg Chem 9 (2004) 119-123
    • (2004) J Biol Inorg Chem , vol.9 , pp. 119-123
    • Niviere, V.1    Fontecave, M.2
  • 18
    • 0028809394 scopus 로고
    • Pseudomonas aeruginosa sod A and sod B mutants defective in manganese-and iron-cofactored superoxide dismutase activity demonstrate the importance of the iron-cofactored form in aerobic metabolism
    • Hassett D.J., Schweizer H.P., and Ohman D.E. Pseudomonas aeruginosa sod A and sod B mutants defective in manganese-and iron-cofactored superoxide dismutase activity demonstrate the importance of the iron-cofactored form in aerobic metabolism. J Bacteriol 177 (1995) 6330-6337
    • (1995) J Bacteriol , vol.177 , pp. 6330-6337
    • Hassett, D.J.1    Schweizer, H.P.2    Ohman, D.E.3
  • 19
    • 33749423106 scopus 로고    scopus 로고
    • ase activity in bacteria exposed to acetamiprid
    • ase activity in bacteria exposed to acetamiprid. Biomed Environ Sci 19 (2006) 309-314
    • (2006) Biomed Environ Sci , vol.19 , pp. 309-314
    • Yao, X.H.1    Min, H.2    Lv, Z.M.3
  • 20
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: implication for classification of on-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferases: implication for classification of on-mammalian members of an ancient enzyme superfamily. Biochem J 360 (2001) 1-16
    • (2001) Biochem J , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 21
    • 10444278093 scopus 로고    scopus 로고
    • Favaloro B. Expression of glutathione S-transferase and peptide methionine sulphoxide reductase in Ochrobactrum anthropi is correlated to the production of reactive oxygen species caused by aromatic substances
    • Tamburro A., Robuffo I., Heipieper H.J., Allocati N., Rotilio D., and Di Ilio C. Favaloro B. Expression of glutathione S-transferase and peptide methionine sulphoxide reductase in Ochrobactrum anthropi is correlated to the production of reactive oxygen species caused by aromatic substances. FEMS Microbiol Lett 241 (2004) 151-156
    • (2004) FEMS Microbiol Lett , vol.241 , pp. 151-156
    • Tamburro, A.1    Robuffo, I.2    Heipieper, H.J.3    Allocati, N.4    Rotilio, D.5    Di Ilio, C.6
  • 22
    • 33846114358 scopus 로고    scopus 로고
    • Three distinct-type glutathione S-transferase from Escherichia coli important for defense against oxidative stress
    • Kanai T., Takahashi K., and Inoue H. Three distinct-type glutathione S-transferase from Escherichia coli important for defense against oxidative stress. J Biochem (Tokyo) 140 (2006) 703-711
    • (2006) J Biochem (Tokyo) , vol.140 , pp. 703-711
    • Kanai, T.1    Takahashi, K.2    Inoue, H.3
  • 23
    • 0038005094 scopus 로고    scopus 로고
    • Proteus mirabilis rglutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses
    • Allocati N., Favaloro B., Masulli M., Alexeyev M.F., and Ilio C.D. Proteus mirabilis rglutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses. Biochem J 373 (2003) 305-311
    • (2003) Biochem J , vol.373 , pp. 305-311
    • Allocati, N.1    Favaloro, B.2    Masulli, M.3    Alexeyev, M.F.4    Ilio, C.D.5
  • 24
    • 0026032524 scopus 로고
    • Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp
    • Xing R.Y., and Whitman W.B. Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp. J Bacteriol 173 (1991) 2086-2092
    • (1991) J Bacteriol , vol.173 , pp. 2086-2092
    • Xing, R.Y.1    Whitman, W.B.2
  • 25
    • 0027165156 scopus 로고
    • The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
    • Flint D.H., Emptage M.H., Finnegan M.G., Fu W., and Johnson M.K. The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. J Biol Chem 268 (1993) 14732-14742
    • (1993) J Biol Chem , vol.268 , pp. 14732-14742
    • Flint, D.H.1    Emptage, M.H.2    Finnegan, M.G.3    Fu, W.4    Johnson, M.K.5
  • 26
    • 0029010808 scopus 로고
    • Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress
    • Brown O.R., Smyk-Randal lE, Draczynska-Lusiak B., and Fee J.A. Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress. Arch Biochem Biophys 319 (1995) 10-22
    • (1995) Arch Biochem Biophys , vol.319 , pp. 10-22
    • Brown, O.R.1    Smyk-Randal lE2    Draczynska-Lusiak, B.3    Fee, J.A.4
  • 27
    • 33751539540 scopus 로고    scopus 로고
    • Complete decolorization of the anthraquinone dye Reactive blue 5 by the concerted action of two peroxidases from Thanatephorus cucumeris Dec 1
    • Sugano Y., Matsushima Y., and Shoda M. Complete decolorization of the anthraquinone dye Reactive blue 5 by the concerted action of two peroxidases from Thanatephorus cucumeris Dec 1. Appl Microbiol Biotechnol 73 (2006) 862-871
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 862-871
    • Sugano, Y.1    Matsushima, Y.2    Shoda, M.3
  • 28
    • 0034973791 scopus 로고    scopus 로고
    • Accumulation of manganese in Neisseria gonorrhoeae correlations with resistance to oxidative killing by superoxide anion is independent of superoxide dismutase activity
    • Tseng H.J., Strikhanta Y., McEwan A.G., and Jennings M.P. Accumulation of manganese in Neisseria gonorrhoeae correlations with resistance to oxidative killing by superoxide anion is independent of superoxide dismutase activity. Mol Microbiol 40 (2001) 1175-1186
    • (2001) Mol Microbiol , vol.40 , pp. 1175-1186
    • Tseng, H.J.1    Strikhanta, Y.2    McEwan, A.G.3    Jennings, M.P.4
  • 29
    • 0036178058 scopus 로고    scopus 로고
    • Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress
    • Tseng H.J., McEwan A.G., Paton J.C., and Jennings M.P. Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress. Infect Immun 70 (2002) 1635-1639
    • (2002) Infect Immun , vol.70 , pp. 1635-1639
    • Tseng, H.J.1    McEwan, A.G.2    Paton, J.C.3    Jennings, M.P.4
  • 30
    • 4644305043 scopus 로고    scopus 로고
    • Lipoprotein PsaA in virulence of Streptococcus pneumoniae: surface accessibility and role in protection from superoxide
    • Johnston J.W., Myers L.E., Ochs Jr. M.M., Benjamin W.H.D., Briles E., and Kollingshead S.K. Lipoprotein PsaA in virulence of Streptococcus pneumoniae: surface accessibility and role in protection from superoxide. Infect Immun 72 (2004) 5858-5867
    • (2004) Infect Immun , vol.72 , pp. 5858-5867
    • Johnston, J.W.1    Myers, L.E.2    Ochs Jr., M.M.3    Benjamin, W.H.D.4    Briles, E.5    Kollingshead, S.K.6
  • 32
    • 34248589261 scopus 로고    scopus 로고
    • The cyanotrophic bacterium Pseudomonas pseudoalcaligenes CECT5344 responds to cyanide by defense mechanisms against iron deprivation, oxidative damage and nitrogen stress
    • Lugue-Almagro V.M., Huertas M.J., Roldan M.D., Moreno-Vivian C., Martinez-Luque M., Blasco R., et al. The cyanotrophic bacterium Pseudomonas pseudoalcaligenes CECT5344 responds to cyanide by defense mechanisms against iron deprivation, oxidative damage and nitrogen stress. Environ Microbiol 9 (2007) 1541-1549
    • (2007) Environ Microbiol , vol.9 , pp. 1541-1549
    • Lugue-Almagro, V.M.1    Huertas, M.J.2    Roldan, M.D.3    Moreno-Vivian, C.4    Martinez-Luque, M.5    Blasco, R.6
  • 33
    • 4444316792 scopus 로고    scopus 로고
    • Insights into Pseudomonas putida KT2440 response to phenol-induced stress by quantitative proteomics
    • Santos P.M., Benndorf D., and Sa-Correia I. Insights into Pseudomonas putida KT2440 response to phenol-induced stress by quantitative proteomics. Proteomics 9 (2004) 2640-2652
    • (2004) Proteomics , vol.9 , pp. 2640-2652
    • Santos, P.M.1    Benndorf, D.2    Sa-Correia, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.