메뉴 건너뛰기




Volumn 29, Issue 2, 2013, Pages 267-273

Influence of metal ions on bioremediation activity of protocatechuate 3,4-dioxygenase from Stenotrophomonas maltophilia KB2

Author keywords

Aromatic compounds; Dioxygenases; Metal ions; Stenotrophomonas

Indexed keywords

AROMATIC COMPOUNDS; BENZOIC ACID; BIOREMEDIATION; BIOTECHNOLOGY; ENZYME ACTIVITY; ENZYME INHIBITION; METAL IONS; PHENOLS;

EID: 84874217080     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-012-1178-z     Document Type: Article
Times cited : (23)

References (47)
  • 1
    • 33847124805 scopus 로고    scopus 로고
    • Degradation of phenol by Acinetobacter strain isolated from aerobic granules
    • Adav SS, Chen M-Y, Lee D-J, Ren N-Q (2007) Degradation of phenol by Acinetobacter strain isolated from aerobic granules. Chemosphere 67: 1566-1572.
    • (2007) Chemosphere , vol.67 , pp. 1566-1572
    • Adav, S.S.1    Chen, M.-Y.2    Lee, D.-J.3    Ren, N.-Q.4
  • 2
    • 0034063357 scopus 로고    scopus 로고
    • Characterization of benzoate degradation via ortho-cleavage by Streptomyces setonii
    • An H-R, Park H-J, Kim E-S (2000) Characterization of benzoate degradation via ortho-cleavage by Streptomyces setonii. J Microbiol Biotechnol 10(1): 111-114.
    • (2000) J Microbiol Biotechnol , vol.10 , Issue.1 , pp. 111-114
    • An, H.-R.1    Park, H.-J.2    Kim, E.-S.3
  • 3
    • 33749534288 scopus 로고    scopus 로고
    • Mechanism of catechol ring cleavage by non-heme iron intradiol dioxygenases: a hybrid DFT study
    • Borowski T, Siegbahn EM (2006) Mechanism of catechol ring cleavage by non-heme iron intradiol dioxygenases: a hybrid DFT study. J Am Chem Soc 128: 12941-12953.
    • (2006) J Am Chem Soc , vol.128 , pp. 12941-12953
    • Borowski, T.1    Siegbahn, E.M.2
  • 4
    • 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 (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 7: 248-254.
    • (1976) Anal Biochem , vol.7 , pp. 248-254
    • Bradford, M.1
  • 5
    • 0033754309 scopus 로고    scopus 로고
    • Key aromatic-ring-cleaving enzyme, protocatechuate 3,4-dioxygenase, in the ecologically important marine Roseobacter lineage
    • Buchan A, Collier LS, Neidle EL, Moran MA (2000) Key aromatic-ring-cleaving enzyme, protocatechuate 3, 4-dioxygenase, in the ecologically important marine Roseobacter lineage. Appl Environ Microbiol 66(11): 4662-4672.
    • (2000) Appl Environ Microbiol , vol.66 , Issue.11 , pp. 4662-4672
    • Buchan, A.1    Collier, L.S.2    Neidle, E.L.3    Moran, M.A.4
  • 6
    • 0033763853 scopus 로고    scopus 로고
    • Characterization of the genes for two protocatechuate 3,4-dioxygenases from the 4-sulfocatechol-degrading bacterium Agrobacterium radiobacter strain S2
    • Contzen M, Stolz A (2000) Characterization of the genes for two protocatechuate 3, 4-dioxygenases from the 4-sulfocatechol-degrading bacterium Agrobacterium radiobacter strain S2. J Bacteriol 182(21): 6123-6129.
    • (2000) J Bacteriol , vol.182 , Issue.21 , pp. 6123-6129
    • Contzen, M.1    Stolz, A.2
  • 7
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates
    • Costas M, Mehn MP, Jensen MP, Que L (2004) Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem Rev 104: 939-986.
    • (2004) Chem Rev , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que, L.4
  • 8
    • 67249153511 scopus 로고    scopus 로고
    • Degradative plasmid and heave metal resistance plasmid naturally coexist in phenol and cyanide assimilating bacteria
    • Deeb BE, Altalhi AD (2009) Degradative plasmid and heave metal resistance plasmid naturally coexist in phenol and cyanide assimilating bacteria. Am J Biochem Biotechnol 5(2): 84-93.
    • (2009) Am J Biochem Biotechnol , vol.5 , Issue.2 , pp. 84-93
    • Deeb, B.E.1    Altalhi, A.D.2
  • 9
    • 0030954878 scopus 로고    scopus 로고
    • Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate
    • Elgren TE, Orville AM, Kelly KA, Lipscomb JD, Ohlendorf DH, Que L (1997) Crystal structure and resonance Raman studies of protocatechuate 3, 4-dioxygenase complexed with 3, 4-dihydroxyphenylacetate. Biochemistry 36: 11504-11513.
    • (1997) Biochemistry , vol.36 , pp. 11504-11513
    • Elgren, T.E.1    Orville, A.M.2    Kelly, K.A.3    Lipscomb, J.D.4    Ohlendorf, D.H.5    Que, L.6
  • 10
    • 0141922977 scopus 로고    scopus 로고
    • Isolation and identification of a novel strain of the genus Ochrobactrum with phenol-degrading activity
    • El-Sayed WE, Ibrahim MK, Abu-Shady M, El-Beih F, Ohmura N, Saiki H, Ando A (2003) Isolation and identification of a novel strain of the genus Ochrobactrum with phenol-degrading activity. J Biosci Bioeng 96(3): 310-312.
    • (2003) J Biosci Bioeng , vol.96 , Issue.3 , pp. 310-312
    • El-Sayed, W.E.1    Ibrahim, M.K.2    Abu-Shady, M.3    El-Beih, F.4    Ohmura, N.5    Saiki, H.6    Ando, A.7
  • 11
    • 72149129190 scopus 로고    scopus 로고
    • Kinetics and metabolic versality of highly tolerant phenol degrading Alcaligenes strain TW1
    • Essam T, Amin MA, Tayeb OE, Mattiasson B, Guieysse B (2010) Kinetics and metabolic versality of highly tolerant phenol degrading Alcaligenes strain TW1. J Hazard Mater 173: 783-788.
    • (2010) J Hazard Mater , vol.173 , pp. 783-788
    • Essam, T.1    Amin, M.A.2    Tayeb, O.E.3    Mattiasson, B.4    Guieysse, B.5
  • 12
    • 11844304935 scopus 로고    scopus 로고
    • The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)
    • Gopal B, Madan LL, Betz SF, Kossiakoff AA (2005) The crystal structure of a quercetin 2, 3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s). Biochemistry 44: 193-201.
    • (2005) Biochemistry , vol.44 , pp. 193-201
    • Gopal, B.1    Madan, L.L.2    Betz, S.F.3    Kossiakoff, A.A.4
  • 13
    • 77951141722 scopus 로고    scopus 로고
    • Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin
    • Greń I, Wojcieszyńska D, Guzik U, Perkosz M, Hupert-Kocurek K (2010) Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin. World J Microbiol Biotechnol 26: 289-295.
    • (2010) World J Microbiol Biotechnol , vol.26 , pp. 289-295
    • Greń, I.1    Wojcieszyńska, D.2    Guzik, U.3    Perkosz, M.4    Hupert-Kocurek, K.5
  • 14
    • 69249137529 scopus 로고    scopus 로고
    • Isolation and characterization of a novel strain of Stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation
    • Guzik U, Greń I, Wojcieszyńska D, Łabużek S (2009) Isolation and characterization of a novel strain of Stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation. Braz J Microbiol 40: 285-291.
    • (2009) Braz J Microbiol , vol.40 , pp. 285-291
    • Guzik, U.1    Greń, I.2    Wojcieszyńska, D.3    Łabuzek, S.4
  • 15
    • 84862875187 scopus 로고    scopus 로고
    • Activity of catechol dioxygenases In the presence of some heavy metal ions: bioremediation of environment polluted with aromatic compounds
    • (in Polish)
    • Guzik U, Wojcieszyńska D, Greń I, Hupert-Kocurek K (2010) Activity of catechol dioxygenases In the presence of some heavy metal ions: bioremediation of environment polluted with aromatic compounds. Ochrona Srodowiska 32(1): 9-13 (in Polish).
    • (2010) Ochrona Srodowiska , vol.32 , Issue.1 , pp. 9-13
    • Guzik, U.1    Wojcieszyńska, D.2    Greń, I.3    Hupert-Kocurek, K.4
  • 16
    • 79953107665 scopus 로고    scopus 로고
    • Catechol 1,2-dioxygenase from the new aromatic compounds-degrading Pseudomonas putida strain N6
    • Guzik U, Greń I, Hupert-Kocurek K, Wojcieszyńska D (2011) Catechol 1, 2-dioxygenase from the new aromatic compounds-degrading Pseudomonas putida strain N6. Int Biodeterior Biodegrad 65: 504-512.
    • (2011) Int Biodeterior Biodegrad , vol.65 , pp. 504-512
    • Guzik, U.1    Greń, I.2    Hupert-Kocurek, K.3    Wojcieszyńska, D.4
  • 17
    • 0034105384 scopus 로고    scopus 로고
    • Reaction characteristics of 4-methylcatechol 2,3-dioxygenase from Pseudomonas putida SU10
    • Ha YM, Jung YH, Kwon DY, Kim Y, Kim C-K, Min KH (2000) Reaction characteristics of 4-methylcatechol 2, 3-dioxygenase from Pseudomonas putida SU10. J Microbiol Biotechnol 10(1): 35-42.
    • (2000) J Microbiol Biotechnol , vol.10 , Issue.1 , pp. 35-42
    • Ha, Y.M.1    Jung, Y.H.2    Kwon, D.Y.3    Kim, Y.4    Kim, C.-K.5    Min, K.H.6
  • 18
    • 0017273546 scopus 로고
    • Protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus
    • Hou ChT, Lillard MO, Schwartz RD (1976) Protocatechuate 3, 4-dioxygenase from Acinetobacter calcoaceticus. Biochemistry 15(3): 582-588.
    • (1976) Biochemistry , vol.15 , Issue.3 , pp. 582-588
    • Hou, C.T.1    Lillard, M.O.2    Schwartz, R.D.3
  • 19
    • 0034087467 scopus 로고    scopus 로고
    • Characterization of the protocatechuic acid catabolic gene luster from Streptomyces sp. strain 2065
    • Iwagami SG, Yang K, Davies J (2000) Characterization of the protocatechuic acid catabolic gene luster from Streptomyces sp. strain 2065. Appl Environ Microbiol 66(4): 1499-1508.
    • (2000) Appl Environ Microbiol , vol.66 , Issue.4 , pp. 1499-1508
    • Iwagami, S.G.1    Yang, K.2    Davies, J.3
  • 20
    • 33749840732 scopus 로고    scopus 로고
    • Trigonal-bipyramidal geometry induced by an external water ligand in a sterically hindered iron salen complex, related to the active site of protocatechuate 3,4-dioxygenase
    • Kurahashi T, Oda K, Sugimoto M, Ogura T, Fujii H (2006) Trigonal-bipyramidal geometry induced by an external water ligand in a sterically hindered iron salen complex, related to the active site of protocatechuate 3, 4-dioxygenase. Inorg Chem 45(19): 7709-77021.
    • (2006) Inorg Chem , vol.45 , Issue.19 , pp. 7709-77021
    • Kurahashi, T.1    Oda, K.2    Sugimoto, M.3    Ogura, T.4    Fujii, H.5
  • 22
    • 77954406044 scopus 로고    scopus 로고
    • Quantification of catechol dioxygenase gene expression in soil during degradation of 2,4-dichlorophenol
    • Lillis L, Clipson N, Doyle E (2010) Quantification of catechol dioxygenase gene expression in soil during degradation of 2, 4-dichlorophenol. FEMS Microbiol Ecol 73: 363-369.
    • (2010) FEMS Microbiol Ecol , vol.73 , pp. 363-369
    • Lillis, L.1    Clipson, N.2    Doyle, E.3
  • 23
    • 0037007542 scopus 로고    scopus 로고
    • Ortho pathway of benzoate degradation in Pseudomonas putida: induction of meta pathway at high substrate concentration
    • Loh K-C, Chua S-S (2002) Ortho pathway of benzoate degradation in Pseudomonas putida: induction of meta pathway at high substrate concentration. Enzyme Microb Technol 30: 620-626.
    • (2002) Enzyme Microb Technol , vol.30 , pp. 620-626
    • Loh, K.-C.1    Chua, S.-S.2
  • 24
    • 0021679083 scopus 로고
    • Characterization of crystals of protocatechuate 3,4-dioxygenase from Pseudomonas cepacia
    • Ludwig ML, Weber LD, Ballou DP (1984) Characterization of crystals of protocatechuate 3, 4-dioxygenase from Pseudomonas cepacia. J Biol Chem 259(23): 14840-14842.
    • (1984) J Biol Chem , vol.259 , Issue.23 , pp. 14840-14842
    • Ludwig, M.L.1    Weber, L.D.2    Ballou, D.P.3
  • 25
    • 84874195185 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of protocatechuate 3,4-dioxygenase in Burkholderia sp. NCIMB 10467
    • Luo S, Zhang J-J, Zhou N-Y (2008) Molecular cloning and biochemical characterization of protocatechuate 3, 4-dioxygenase in Burkholderia sp. NCIMB 10467. Microbiology 35(5): 712-719.
    • (2008) Microbiology , vol.35 , Issue.5 , pp. 712-719
    • Luo, S.1    Zhang, J.-J.2    Zhou, N.-Y.3
  • 26
    • 45849123846 scopus 로고    scopus 로고
    • Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans: crystal structure of a pelicular ring-cleaving dioxygenase
    • Matera I, Ferraroni M, Bürger S, Scozzafava A, Stolz A, Briganti F (2008) Salicylate 1, 2-dioxygenase from Pseudoaminobacter salicylatoxidans: crystal structure of a pelicular ring-cleaving dioxygenase. J Mol Biol 380: 856-868.
    • (2008) J Mol Biol , vol.380 , pp. 856-868
    • Matera, I.1    Ferraroni, M.2    Bürger, S.3    Scozzafava, A.4    Stolz, A.5    Briganti, F.6
  • 27
    • 77957680207 scopus 로고    scopus 로고
    • Novel square pyramidal iron(III) coplex of linear tetradentate bis(phenolate) ligands as structural and reactive models dor intradiol-cleaving 3,4-PCD enzymes: quinine formation vs. intradiol cleavage
    • Mayilmurugan R, Sankaralingam M, Suresh E, Palaniandavar M (2010) Novel square pyramidal iron(III) coplex of linear tetradentate bis(phenolate) ligands as structural and reactive models dor intradiol-cleaving 3, 4-PCD enzymes: quinine formation vs. intradiol cleavage. Dalton Trans 39: 9611-9625.
    • (2010) Dalton Trans , vol.39 , pp. 9611-9625
    • Mayilmurugan, R.1    Sankaralingam, M.2    Suresh, E.3    Palaniandavar, M.4
  • 28
    • 2942702300 scopus 로고    scopus 로고
    • Biodegradation of natural phenolic compounds as a single and mixed substrates by Fusarium flocciferum
    • Mendonça E, Martins A, Anselmo M (2004) Biodegradation of natural phenolic compounds as a single and mixed substrates by Fusarium flocciferum. Electron J Biotechnol 7(1): 30-37.
    • (2004) Electron J Biotechnol , vol.7 , Issue.1 , pp. 30-37
    • Mendonça, E.1    Martins, A.2    Anselmo, M.3
  • 29
    • 72949085723 scopus 로고    scopus 로고
    • Biodegradation kinetics of benzoic and anthranilic acids by Micrococcus sp
    • Muthukumar K, Bharath Ch, Pugalenthi V, Velan M (2009) Biodegradation kinetics of benzoic and anthranilic acids by Micrococcus sp. J Sci Ind Res 68: 900-903.
    • (2009) J Sci Ind Res , vol.68 , pp. 900-903
    • Muthukumar, K.1    Bharath, C.2    Pugalenthi, V.3    Velan, M.4
  • 30
    • 0032977236 scopus 로고    scopus 로고
    • Microbial heavy-metal resistance
    • Nies DH (1999) Microbial heavy-metal resistance. Appl Microbiol Biotechnol 51: 730-750.
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 730-750
    • Nies, D.H.1
  • 31
    • 0034167536 scopus 로고    scopus 로고
    • Heavy metal-resistant bacteria as extremophiles: molecular physiology and biotechnological use of Ralstonia sp. CH34
    • Nies DH (2000) Heavy metal-resistant bacteria as extremophiles: molecular physiology and biotechnological use of Ralstonia sp. CH34. Extremophiles 4: 77-82.
    • (2000) Extremophiles , vol.4 , pp. 77-82
    • Nies, D.H.1
  • 32
    • 0014429573 scopus 로고
    • Metapyrocatechase. The role of iron and sulfhydryl groups
    • Nozaki M, Ono K, Nakazawa T, Kotani S, Hayaishi O (1968) Metapyrocatechase. The role of iron and sulfhydryl groups. J Biol Chem 243(10): 2682-2690.
    • (1968) J Biol Chem , vol.243 , Issue.10 , pp. 2682-2690
    • Nozaki, M.1    Ono, K.2    Nakazawa, T.3    Kotani, S.4    Hayaishi, O.5
  • 33
    • 33847267249 scopus 로고    scopus 로고
    • Spectroscopic and electronic structure study of the enzyme-substrate complex of intradiol dioxygenases: substrate activation by a high-spin ferric non-heme iron site
    • Pau MYM, Davis MI, Orville AM, Lipscomb JD, Solomon EI (2005) Spectroscopic and electronic structure study of the enzyme-substrate complex of intradiol dioxygenases: substrate activation by a high-spin ferric non-heme iron site. J Am Chem Soc 129: 1944-1958.
    • (2005) J Am Chem Soc , vol.129 , pp. 1944-1958
    • Pau, M.Y.M.1    Davis, M.I.2    Orville, A.M.3    Lipscomb, J.D.4    Solomon, E.I.5
  • 35
    • 0024618763 scopus 로고
    • Occurrence of two different forms of protocatechuate 3,4-dioxygenase in a Moraxella sp
    • Sterjiades R, Pelmont J (1989) Occurrence of two different forms of protocatechuate 3, 4-dioxygenase in a Moraxella sp. Appl Environ Microbiol 55(2): 340-347.
    • (1989) Appl Environ Microbiol , vol.55 , Issue.2 , pp. 340-347
    • Sterjiades, R.1    Pelmont, J.2
  • 36
    • 80051938045 scopus 로고    scopus 로고
    • New approaches concerning the utilization of natural amendments in cadmium phytoremediation
    • Stingu A, Volf I, Popa VI, Gostin I (2012) New approaches concerning the utilization of natural amendments in cadmium phytoremediation. J Crop Prod 35: 53-60.
    • (2012) J Crop Prod , vol.35 , pp. 53-60
    • Stingu, A.1    Volf, I.2    Popa, V.I.3    Gostin, I.4
  • 37
    • 78651157011 scopus 로고
    • A description of some lignanolytic soil bacteria and their ability to oxidize simple phenolic compounds
    • Sundman V (1964) A description of some lignanolytic soil bacteria and their ability to oxidize simple phenolic compounds. J Gen Microbiol 36: 171-183.
    • (1964) J Gen Microbiol , vol.36 , pp. 171-183
    • Sundman, V.1
  • 39
    • 33847126079 scopus 로고    scopus 로고
    • Purification and characterization of a catechol 1,2-dioxygenase from a phenol degrading Candida albicans TL3
    • Tsai S-Ch, Li Y-K (2007) Purification and characterization of a catechol 1, 2-dioxygenase from a phenol degrading Candida albicans TL3. Arch Microbiol 187: 199-206.
    • (2007) Arch Microbiol , vol.187 , pp. 199-206
    • Tsai, S.C.1    Li, Y.K.2
  • 40
    • 59449092996 scopus 로고    scopus 로고
    • The pollution characteristics of odor, volatile organochlorinated compounds and polycyclic aromatic hydrocarbons emitted from plastic waste recycling plants
    • Tsai ChJ, Chen ML, Chang KF, Chang FK, Mao IF (2009) The pollution characteristics of odor, volatile organochlorinated compounds and polycyclic aromatic hydrocarbons emitted from plastic waste recycling plants. Chemosphere 74: 1104-1110.
    • (2009) Chemosphere , vol.74 , pp. 1104-1110
    • Tsai, C.J.1    Chen, M.L.2    Chang, K.F.3    Chang, F.K.4    Mao, I.F.5
  • 42
    • 0034636805 scopus 로고    scopus 로고
    • Structure of Acinetobacter strain ADP1 protocatechuate 3,4-dioxygenase at 2.2 Å resolution: implication for the mechanism of an intradiol dioxygenase
    • Vetting MW, D'Argenio DA, Ornston LN, Ohlendorf DH (2000) Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2. 2 Å resolution: implication for the mechanism of an intradiol dioxygenase. Biochemistry 39: 7943-7955.
    • (2000) Biochemistry , vol.39 , pp. 7943-7955
    • Vetting, M.W.1    D'Argenio, D.A.2    Ornston, L.N.3    Ohlendorf, D.H.4
  • 43
    • 33646540690 scopus 로고    scopus 로고
    • Purification and characterization of a novel catechol 1,2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source
    • Wang ChL, You SL, Wang S-L (2006) Purification and characterization of a novel catechol 1, 2-dioxygenase from Pseudomonas aeruginosa with benzoic acid as a carbon source. Process Biochem 41: 1594-1601.
    • (2006) Process Biochem , vol.41 , pp. 1594-1601
    • Wang, C.L.1    You, S.L.2    Wang, S.L.3
  • 44
    • 79952572933 scopus 로고    scopus 로고
    • Induction of aromatic ring-cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems
    • Wojcieszyńska D, Guzik U, Greń I, Perkosz M, Hupert-Kocurek K (2011a) Induction of aromatic ring-cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems. World J Microbiol Biotechnol 27: 805-811.
    • (2011) World J Microbiol Biotechnol , vol.27 , pp. 805-811
    • Wojcieszyńska, D.1    Guzik, U.2    Greń, I.3    Perkosz, M.4    Hupert-Kocurek, K.5
  • 45
    • 79961208826 scopus 로고    scopus 로고
    • High activity catechol 2,3-dioxygenase from the cresols-degrading Stenotrophomonas maltophilia strain KB2
    • Wojcieszyńska D, Hupert-Kocurek K, Greń I, Guzik U (2011b) High activity catechol 2, 3-dioxygenase from the cresols-degrading Stenotrophomonas maltophilia strain KB2. Int Biodeterior Biodegrad 65: 853-858.
    • (2011) Int Biodeterior Biodegrad , vol.65 , pp. 853-858
    • Wojcieszyńska, D.1    Hupert-Kocurek, K.2    Greń, I.3    Guzik, U.4
  • 46
    • 40849142100 scopus 로고    scopus 로고
    • Influence of metal ions on folding pathway and conformational stability of bovine serum albumin
    • Wu L-Z, Ma B-L, Zou D-W, Tie Z-X, Wang J, Wang W (2008) Influence of metal ions on folding pathway and conformational stability of bovine serum albumin. J Mol Struct 877: 44-49.
    • (2008) J Mol Struct , vol.877 , pp. 44-49
    • Wu, L.-Z.1    Ma, B.-L.2    Zou, D.-W.3    Tie, Z.-X.4    Wang, J.5    Wang, W.6
  • 47
    • 3142605206 scopus 로고    scopus 로고
    • Overcoming the inhibition effects of metal ions in the degradation of benzene and toluene by Alcaligenes xylosoxidans Y234
    • Yeom SH, Yoo YJ (1997) Overcoming the inhibition effects of metal ions in the degradation of benzene and toluene by Alcaligenes xylosoxidans Y234. Korean J Chem Eng 14(3): 204-208.
    • (1997) Korean J Chem Eng , vol.14 , Issue.3 , pp. 204-208
    • Yeom, S.H.1    Yoo, Y.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.