메뉴 건너뛰기




Volumn 2, Issue 4, 2007, Pages 387-395

Siderophores in fluorescent pseudomonads: New tricks from an old dog

Author keywords

(Thio)quinolobactin; 6 bis thiocarboxylic acid (PDTC); Biodegradation; Iron uptake; Pseudomonas; Pyridine 2; Siderophores

Indexed keywords

ABC TRANSPORTER; ANTIBIOTIC AGENT; IRON; MEMBRANE RECEPTOR; NATURAL PRODUCT; PYOCHELIN; PYOVERDINE; PYRIDINE 2,6 BISTHIOCARBOXYLIC ACID; PYRROLIDINE DITHIOCARBAMATE; QUINOLOBACTIN; SIDEROPHORE; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 34548452873     PISSN: 17460913     EISSN: None     Source Type: Journal    
DOI: 10.2217/17460913.2.4.387     Document Type: Review
Times cited : (23)

References (64)
  • 1
    • 0030861787 scopus 로고    scopus 로고
    • Avoidance of iron toxicity through regulation of bacterial iron transport
    • Braun V: Avoidance of iron toxicity through regulation of bacterial iron transport. Biol. Chem. 378, 779-786 (1997).
    • (1997) Biol. Chem , vol.378 , pp. 779-786
    • Braun, V.1
  • 2
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands JB: Siderophores: structure and function of microbial iron transport compounds. J. Biol. Chem. 270, 26723-26726 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 3
    • 0027945605 scopus 로고
    • Microbial iron transport
    • Guerinot ML: Microbial iron transport. Annu. Rev. Microbiol. 48, 743-772 (1994).
    • (1994) Annu. Rev. Microbiol , vol.48 , pp. 743-772
    • Guerinot, M.L.1
  • 4
  • 5
    • 0037317173 scopus 로고    scopus 로고
    • Acquisition of siderophores in Gram-negative bacteria
    • Faraldo-Gomez JD, Sansom MS: Acquisition of siderophores in Gram-negative bacteria. Nat. Rev. Mol. Cell Biol. 4, 105-116 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 105-116
    • Faraldo-Gomez, J.D.1    Sansom, M.S.2
  • 6
    • 34548442567 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle K, Kadner RJ: Touch and go: tying TonB to transport. Mol. Microbiol. 29, 673-684 (2003).
    • (2003) Mol. Microbiol , vol.29 , pp. 673-684
    • Postle, K.1    Kadner, R.J.2
  • 7
    • 0000803252 scopus 로고
    • Pseudomonadaceae
    • Krieg NR, Holt JG Eds, Williams and Wilkins, Baltimore, USA
    • Palleroni NJ: Pseudomonadaceae. In: Bergey's Manual of Systematic Bacteriology. Krieg NR, Holt JG (Eds). Williams and Wilkins, Baltimore, USA 141-199 (1984).
    • (1984) Bergey's Manual of Systematic Bacteriology , pp. 141-199
    • Palleroni, N.J.1
  • 8
    • 0031278030 scopus 로고    scopus 로고
    • Siderophores of fluorescent pseudomonads
    • Budzikiewicz H: Siderophores of fluorescent pseudomonads. Z. Naturforsch. 52c, 713-720 (1997).
    • (1997) Z. Naturforsch , vol.52 c , pp. 713-720
    • Budzikiewicz, H.1
  • 9
    • 0024095094 scopus 로고
    • Specificity of pyoverdine-mediated iron uptake among fluorescent Pseudomonas strains
    • Hohnadel D, Meyer JM: Specificity of pyoverdine-mediated iron uptake among fluorescent Pseudomonas strains. J. Bacteriol. 170, 4865-4873 (1988).
    • (1988) J. Bacteriol , vol.170 , pp. 4865-4873
    • Hohnadel, D.1    Meyer, J.M.2
  • 10
    • 0027154740 scopus 로고
    • Secondary metabolites from fluorescent pseudomonads
    • Budzikiewicz H: Secondary metabolites from fluorescent pseudomonads. FEMS Microbiol. Rev. 10, 209-228 (1993).
    • (1993) FEMS Microbiol. Rev , vol.10 , pp. 209-228
    • Budzikiewicz, H.1
  • 12
    • 33749255145 scopus 로고    scopus 로고
    • Oxygen, cyanide and energy generation in the cystic fibrosis pathogen Pseudomonas aeruginosa
    • Williams HD, Zlosnik JE, Ryall B: Oxygen, cyanide and energy generation in the cystic fibrosis pathogen Pseudomonas aeruginosa. Adv. Microb. Physiol. 52, 1-71 (2007).
    • (2007) Adv. Microb. Physiol , vol.52 , pp. 1-71
    • Williams, H.D.1    Zlosnik, J.E.2    Ryall, B.3
  • 13
    • 0035352919 scopus 로고    scopus 로고
    • Siderotyping - a powerful tool for the characterization of pyoverdines
    • Fuchs R, Schafer M, Geoffroy VA, Meyer JM: Siderotyping - a powerful tool for the characterization of pyoverdines. Curr. Top. Med. Chem 1(1), 31-57 (2001).
    • (2001) Curr. Top. Med. Chem , vol.1 , Issue.1 , pp. 31-57
    • Fuchs, R.1    Schafer, M.2    Geoffroy, V.A.3    Meyer, J.M.4
  • 14
    • 0036268797 scopus 로고    scopus 로고
    • Siderophore typing, a powerful tool for the identification of fluorescent and non-fluorescent pseudomonads
    • Meyer JM, Geoffroy VA, Baida N et al.: Siderophore typing, a powerful tool for the identification of fluorescent and non-fluorescent pseudomonads. Appl. Environ. Microbiol. 68, 2745-2753 (2002).
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 2745-2753
    • Meyer, J.M.1    Geoffroy, V.A.2    Baida, N.3
  • 15
    • 0027203781 scopus 로고
    • Cloning and nucleotide sequence analysis of the ferripyoverdine receptor gene fpvA of Pseudomonas aeruginosa
    • Poole K, Neshat S, Krebes Y, Heinrichs DE: Cloning and nucleotide sequence analysis of the ferripyoverdine receptor gene fpvA of Pseudomonas aeruginosa. J. Bacteriol. 175, 4597-4604 (1993).
    • (1993) J. Bacteriol , vol.175 , pp. 4597-4604
    • Poole, K.1    Neshat, S.2    Krebes, Y.3    Heinrichs, D.E.4
  • 16
    • 14144255323 scopus 로고    scopus 로고
    • The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution
    • Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F: The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution. J. Mol. Biol. 347(1), 121-134 (2005).
    • (2005) J. Mol. Biol , vol.347 , Issue.1 , pp. 121-134
    • Cobessi, D.1    Celia, H.2    Folschweiller, N.3    Schalk, I.J.4    Abdallah, M.A.5    Pattus, F.6
  • 17
    • 33947600827 scopus 로고    scopus 로고
    • From the periplasmic signalling domain to the extracellular face of an outer membrane signal transducer of Pseudomonas aeruginosa: Crystal structure of the ferric pyoverdine outer membrane receptor
    • Wirth C, Meyer-Klaucke W, Patrus F, Cobessi D: From the periplasmic signalling domain to the extracellular face of an outer membrane signal transducer of Pseudomonas aeruginosa: crystal structure of the ferric pyoverdine outer membrane receptor. J. Mol. Biol. 368(2), 398-406 (2007).
    • (2007) J. Mol. Biol , vol.368 , Issue.2 , pp. 398-406
    • Wirth, C.1    Meyer-Klaucke, W.2    Patrus, F.3    Cobessi, D.4
  • 18
    • 3142716025 scopus 로고    scopus 로고
    • FpvB, an alternative type I ferripyoverdine receptor of Pseudomonas aeruginosa
    • Ghysels B, Dieu BT, Beatson SA et al.: FpvB, an alternative type I ferripyoverdine receptor of Pseudomonas aeruginosa. Microbiology 150, 1671-1680 (2004).
    • (2004) Microbiology , vol.150 , pp. 1671-1680
    • Ghysels, B.1    Dieu, B.T.2    Beatson, S.A.3
  • 19
    • 0038076006 scopus 로고    scopus 로고
    • Identification of type II and type III pyoverdine receptors from Pseudomonas aeruginosa
    • de Chial M, Ghysels B, Beatson SA et al.: Identification of type II and type III pyoverdine receptors from Pseudomonas aeruginosa. Microbiology 149, 821-831 (2003).
    • (2003) Microbiology , vol.149 , pp. 821-831
    • de Chial, M.1    Ghysels, B.2    Beatson, S.A.3
  • 20
    • 33845951124 scopus 로고    scopus 로고
    • Pyoverdine siderophores: From biogenesis to biosignificance
    • Visca P, Imperi F, Lamont IL: Pyoverdine siderophores: from biogenesis to biosignificance. Trends Microbiol. 15(1), 22-30 (2007).
    • (2007) Trends Microbiol , vol.15 , Issue.1 , pp. 22-30
    • Visca, P.1    Imperi, F.2    Lamont, I.L.3
  • 21
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa JH, Walsh CT: Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Mol. Biol. Rev. 66, 223-249 (2002).
    • (2002) Microbiol. Mol. Biol. Rev , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 22
    • 33645116726 scopus 로고    scopus 로고
    • Chemoenzymatic and template-directed synthesis of bioactive macrocyclic peptides
    • Grunewald J, Marahiel MA: Chemoenzymatic and template-directed synthesis of bioactive macrocyclic peptides. Microbiol. Mol. Biol. Rev. 70, 121-146 (2006).
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 121-146
    • Grunewald, J.1    Marahiel, M.A.2
  • 23
    • 18644368300 scopus 로고    scopus 로고
    • Identification of new, conserved, non-ribosomal peptide synthetases from fluorescent pseudomonads involved in the biosynthesis of the siderophore pyoverdine
    • Mossialos D, Ochsner U, Baysse C et al.: Identification of new, conserved, non-ribosomal peptide synthetases from fluorescent pseudomonads involved in the biosynthesis of the siderophore pyoverdine. Mol. Microbiol. 45, 1673-1685 (2002).
    • (2002) Mol. Microbiol , vol.45 , pp. 1673-1685
    • Mossialos, D.1    Ochsner, U.2    Baysse, C.3
  • 24
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar L, Pérez-Martin J, de Lorenzo V: Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 181, 6223-6229 (1999).
    • (1999) J. Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Pérez-Martin, J.2    de Lorenzo, V.3
  • 25
    • 3042840984 scopus 로고    scopus 로고
    • Idnetification of tandem duplicate regulatory small RNAs in Pseudomonas aeruginosa involved in iron homeostasis
    • Wilderman PJ, Sowa NA, FitzGerald DJ et al.: Idnetification of tandem duplicate regulatory small RNAs in Pseudomonas aeruginosa involved in iron homeostasis. Proc. Natl. Acad. Sci. USA 101(26), 9792-9797 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.26 , pp. 9792-9797
    • Wilderman, P.J.1    Sowa, N.A.2    FitzGerald, D.J.3
  • 26
    • 34248669844 scopus 로고    scopus 로고
    • How we learnt about iron acquisition in Pseudomonas aeruginosa: A series of very fortunate events
    • Vasil ML: How we learnt about iron acquisition in Pseudomonas aeruginosa: a series of very fortunate events. Biometals 20(3-4), 587-601 (2007).
    • (2007) Biometals , vol.20 , Issue.3-4 , pp. 587-601
    • Vasil, M.L.1
  • 27
    • 0036046297 scopus 로고    scopus 로고
    • Iron transport and regulation, cell signalling and genomics: Lessons from Escherichia coli and Pseudomonas
    • Visca P, Leoni L, Wilson MJ, Lamont IL: Iron transport and regulation, cell signalling and genomics: lessons from Escherichia coli and Pseudomonas Mol. Microbiol. 45, 1177-1190 (2002).
    • (2002) Mol. Microbiol , vol.45 , pp. 1177-1190
    • Visca, P.1    Leoni, L.2    Wilson, M.J.3    Lamont, I.L.4
  • 28
    • 0037221477 scopus 로고    scopus 로고
    • Siderophore-mediated cell signaling in Pseudomonas aeruginosa: Divergent pathways regulate virulence factor production and siderophore receptor synthesis
    • Beare PA, For RJ, Martin LW, Lamont IL: Siderophore-mediated cell signaling in Pseudomonas aeruginosa: divergent pathways regulate virulence factor production and siderophore receptor synthesis. Mol. Microbiol. 47, 195-207 (2003).
    • (2003) Mol. Microbiol , vol.47 , pp. 195-207
    • Beare, P.A.1    For, R.J.2    Martin, L.W.3    Lamont, I.L.4
  • 29
    • 0037076382 scopus 로고    scopus 로고
    • Siderophore-mediated signalling regulates virulence factor production in Pseudomonas aeruginosa
    • Lamont IL, Beare PA, Ochsner U, Vasil AI, Vasil ML: Siderophore-mediated signalling regulates virulence factor production in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 99, 7072-7077 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7072-7077
    • Lamont, I.L.1    Beare, P.A.2    Ochsner, U.3    Vasil, A.I.4    Vasil, M.L.5
  • 30
    • 23644456000 scopus 로고    scopus 로고
    • FpvIR control of fpvA ferric pyoverdine gene expression in Pseudomonas aeruginosa: Demonstration of an interaction between FpvI and FpvR and identification of mutations in each compromising this interaction
    • Redly GA, Poole K: FpvIR control of fpvA ferric pyoverdine gene expression in Pseudomonas aeruginosa: demonstration of an interaction between FpvI and FpvR and identification of mutations in each compromising this interaction. J. Bacteriol. 187, 5648-5657 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 5648-5657
    • Redly, G.A.1    Poole, K.2
  • 31
    • 33644777983 scopus 로고    scopus 로고
    • The heterologous siderophores ferrioxamine B and ferrichrome activate signalling pathways in Pseudomonas aeruginosa
    • Llmas MA, Sparrius M, Kloet R, Jimenez CR, Vandenbroucke-Grauls C, Bitter W: The heterologous siderophores ferrioxamine B and ferrichrome activate signalling pathways in Pseudomonas aeruginosa. J. Bacteriol. 188, 1882-1891 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 1882-1891
    • Llmas, M.A.1    Sparrius, M.2    Kloet, R.3    Jimenez, C.R.4    Vandenbroucke-Grauls, C.5    Bitter, W.6
  • 32
    • 0346636767 scopus 로고    scopus 로고
    • Iron acquisition and its control in Pseudomonas aeruginosa: Many roads lead to Rome
    • Poole K, McKay GA. Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome. Front Biosci. 8, d661-d686 (2003).
    • (2003) Front Biosci , vol.8
    • Poole, K.1    McKay, G.A.2
  • 33
    • 0031026577 scopus 로고    scopus 로고
    • Augmentation of oxidant injury to human pulmonary epithelial cells by the Pseudomonas aeruginosa siderophore pyochelin
    • Britigan BE, Rasmussen GT, Cox CD: Augmentation of oxidant injury to human pulmonary epithelial cells by the Pseudomonas aeruginosa siderophore pyochelin. Infect. Immun. 65, 1071-1076 (1997).
    • (1997) Infect. Immun , vol.65 , pp. 1071-1076
    • Britigan, B.E.1    Rasmussen, G.T.2    Cox, C.D.3
  • 34
    • 0031020825 scopus 로고    scopus 로고
    • Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron regulated pchDCBA operon in Pseudomonas aeruginosa
    • Serino L, Reimmann C, Visca P, Beyeler M, Della Chiesa V, Haas D: Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron regulated pchDCBA operon in Pseudomonas aeruginosa. J. Bacteriol. 179, 248-257 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 248-257
    • Serino, L.1    Reimmann, C.2    Visca, P.3    Beyeler, M.4    Della Chiesa, V.5    Haas, D.6
  • 35
    • 0031736408 scopus 로고    scopus 로고
    • Dihydroaeruginoic acid synthetase and pyochelin synthetase, products of the pchEF genes, are induced by extracellular pyochelin in Pseudomonas aeruginosa
    • Reimmann C, Serino L, Beyeler M, Haas D: Dihydroaeruginoic acid synthetase and pyochelin synthetase, products of the pchEF genes, are induced by extracellular pyochelin in Pseudomonas aeruginosa. Microbiology 144, 3135-3148 (1998).
    • (1998) Microbiology , vol.144 , pp. 3135-3148
    • Reimmann, C.1    Serino, L.2    Beyeler, M.3    Haas, D.4
  • 36
    • 0035151726 scopus 로고    scopus 로고
    • Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa
    • Reimmann C, Patel HM, Serino L, Barone M, Walsh CT, Haas D: Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa. J. Bacteriol. 183, 813-820 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 813-820
    • Reimmann, C.1    Patel, H.M.2    Serino, L.3    Barone, M.4    Walsh, C.T.5    Haas, D.6
  • 37
    • 0026686089 scopus 로고
    • Cloning of the outer membrane high-affinity Fe (III)-pyochelin receptor of Pseudomonas aeruginosa
    • Ankenbauer RG: Cloning of the outer membrane high-affinity Fe (III)-pyochelin receptor of Pseudomonas aeruginosa. J. Bacteriol. 174, 4401-4409 (1992).
    • (1992) J. Bacteriol , vol.174 , pp. 4401-4409
    • Ankenbauer, R.G.1
  • 38
    • 0029914952 scopus 로고    scopus 로고
    • PchR, a regulator of ferripyochelin receptor gene (fpt.A) expression in Pseudomonas aeruginosa, functions both as an activator and as a repressor
    • Heinrichs D, Poole K: PchR, a regulator of ferripyochelin receptor gene (fpt.A) expression in Pseudomonas aeruginosa, functions both as an activator and as a repressor. J. Bacteriol. 178, 2586-2592 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 2586-2592
    • Heinrichs, D.1    Poole, K.2
  • 39
    • 24644432870 scopus 로고    scopus 로고
    • Crystal structure at high resolution of ferricpyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
    • Cobessi D, Celia H, Pattus F: Crystal structure at high resolution of ferricpyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J. Mol. Biol. 352(4), 893-904 (2005).
    • (2005) J. Mol. Biol , vol.352 , Issue.4 , pp. 893-904
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 40
    • 0037077213 scopus 로고    scopus 로고
    • Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities
    • Gaille C, Kast P, Haas D: Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities. J. Biol. Chem. 277, 21768-21775 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 21768-21775
    • Gaille, C.1    Kast, P.2    Haas, D.3
  • 41
    • 0038268151 scopus 로고    scopus 로고
    • Isochorismate synthase (PchA), the first and rate-limiting enzyme in salicylate biosynthesis of Pseudomoans aeruginosa
    • Gaille C, Reimmann C, Haas D: Isochorismate synthase (PchA), the first and rate-limiting enzyme in salicylate biosynthesis of Pseudomoans aeruginosa. J. Biol. Chem. 278, 16893-16898 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 16893-16898
    • Gaille, C.1    Reimmann, C.2    Haas, D.3
  • 42
    • 0033539471 scopus 로고    scopus 로고
    • Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitutiçon of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE and PchF
    • Quadri LE, Keating TA, Patel HM, Walsh CT: Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: in vitro reconstitutiçon of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE and PchF. Biochemistry 38, 14941-14954 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14941-14954
    • Quadri, L.E.1    Keating, T.A.2    Patel, H.M.3    Walsh, C.T.4
  • 43
    • 4544326782 scopus 로고    scopus 로고
    • PchC thioesterase optimises nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa
    • Reimmann C, Patel HM, Walsh CT, Haas D: PchC thioesterase optimises nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa. J. Bacteriol. 186, 6367-6373 (2004).
    • (2004) J. Bacteriol , vol.186 , pp. 6367-6373
    • Reimmann, C.1    Patel, H.M.2    Walsh, C.T.3    Haas, D.4
  • 44
    • 26944468295 scopus 로고    scopus 로고
    • PchR-box recognition by the AraC-type regulator PchR of Pseudomonas aeruginosa requires the siderophore pyochelin as an effector
    • Michel L, Gonzalez N, Jagdeep S, Nguyen-Ngoc T, Reimmann C: PchR-box recognition by the AraC-type regulator PchR of Pseudomonas aeruginosa requires the siderophore pyochelin as an effector. Mol. Microbiol. 58, 495-509 (2005).
    • (2005) Mol. Microbiol , vol.58 , pp. 495-509
    • Michel, L.1    Gonzalez, N.2    Jagdeep, S.3    Nguyen-Ngoc, T.4    Reimmann, C.5
  • 45
    • 0026697628 scopus 로고
    • Stability, frequency and multiplicity of transposon insertions in the pyoverdine region in the chromosomes of different fluorescent pseudomonads
    • Cornelis P, Anjaiah V, Koedam N et al.: Stability, frequency and multiplicity of transposon insertions in the pyoverdine region in the chromosomes of different fluorescent pseudomonads. J. Gen. Microbiol. 138, 1337-1343 (1992).
    • (1992) J. Gen. Microbiol , vol.138 , pp. 1337-1343
    • Cornelis, P.1    Anjaiah, V.2    Koedam, N.3
  • 46
    • 0033952910 scopus 로고    scopus 로고
    • Quinolobactin, a new siderophore of Pseudomonas fluorescens ATCC 17400, the production of which is repressed by the cognate pyoverdine
    • Mossialos D, Meyer JM, Budzikiewicz H et al.: Quinolobactin, a new siderophore of Pseudomonas fluorescens ATCC 17400, the production of which is repressed by the cognate pyoverdine. Appl. Environ. Microbiol. 66, 487-492 (2000).
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 487-492
    • Mossialos, D.1    Meyer, J.M.2    Budzikiewicz, H.3
  • 47
    • 18444392091 scopus 로고    scopus 로고
    • Synthesis and iron-binding properties of quinolobactin, a siderophore from a pyoverdine-deficient Pseudomonas fluorescens
    • du Moulinet d'Hardemare A, Serratrice G, Pierre JL: Synthesis and iron-binding properties of quinolobactin, a siderophore from a pyoverdine-deficient Pseudomonas fluorescens. Biometals 17, 691-697. (2004).
    • (2004) Biometals , vol.17 , pp. 691-697
    • du Moulinet d'Hardemare, A.1    Serratrice, G.2    Pierre, J.L.3
  • 48
    • 11144357935 scopus 로고    scopus 로고
    • The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic acid, an intermediate of the kynurenine pathway
    • Matthis S, Baysse C, Koedam N et al.: The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic acid, an intermediate of the kynurenine pathway. Mol. Microbiol. 52, 371-384 (2004).
    • (2004) Mol. Microbiol , vol.52 , pp. 371-384
    • Matthis, S.1    Baysse, C.2    Koedam, N.3
  • 49
    • 33846062870 scopus 로고    scopus 로고
    • Thioquinolobactin, a Pseudomonas siderophore with antifungal and anti-Pythium activity
    • Matthis S, Tehrani KA, Laus G et al.: Thioquinolobactin, a Pseudomonas siderophore with antifungal and anti-Pythium activity. Environ. Microbiol. 9(2), 22-30 (2007)
    • (2007) Environ. Microbiol , vol.9 , Issue.2 , pp. 22-30
    • Matthis, S.1    Tehrani, K.A.2    Laus, G.3
  • 50
    • 34147162110 scopus 로고    scopus 로고
    • Biosynthesis of the thioquinolobactin siderophore: An interesting variation on sulphur transfer
    • Godert AM, Jin M, McLafferty FW et al.: Biosynthesis of the thioquinolobactin siderophore: an interesting variation on sulphur transfer. J. Bacteriol. 189, 2941-2944 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 2941-2944
    • Godert, A.M.1    Jin, M.2    McLafferty, F.W.3
  • 51
    • 0033546561 scopus 로고    scopus 로고
    • Identification of an extracellular catalyst of carbon tetrachloride dehalogenation from Pseudomonas stutzeri KC as pyridine-2, 6-bis (thiocarboxylate)
    • Lee CH, Lewis TA, Paszczynski A, Crawford RL: Identification of an extracellular catalyst of carbon tetrachloride dehalogenation from Pseudomonas stutzeri KC as pyridine-2, 6-bis (thiocarboxylate). Biochm. Biophys. Res. Commun. 261, 562-566 (1999).
    • (1999) Biochm. Biophys. Res. Commun , vol.261 , pp. 562-566
    • Lee, C.H.1    Lewis, T.A.2    Paszczynski, A.3    Crawford, R.L.4
  • 52
    • 0035545131 scopus 로고    scopus 로고
    • Metal binding by pyridine-2, 6-bis (monothiocarboxylic acid), a biochelator produced by Pseudomonas stutzeri and Pseudomonas putida
    • Stolworthy JC, Paszczynski A, Korus RA, Crawford RL: Metal binding by pyridine-2, 6-bis (monothiocarboxylic acid), a biochelator produced by Pseudomonas stutzeri and Pseudomonas putida. Biodegradation 12, 411-418 (2001).
    • (2001) Biodegradation , vol.12 , pp. 411-418
    • Stolworthy, J.C.1    Paszczynski, A.2    Korus, R.A.3    Crawford, R.L.4
  • 53
    • 0036264590 scopus 로고    scopus 로고
    • Metal chelating properties of pyridine-2, 6-bis (thiocarboxylic acid) produced by Pseudomonas spp. and the biological activities of the formed complexes
    • Cortese M, Paszczynski A, Lewis TA, Sebat J, Crawford RL: Metal chelating properties of pyridine-2, 6-bis (thiocarboxylic acid) produced by Pseudomonas spp. and the biological activities of the formed complexes. Biometals 15, 103-120 (2002).
    • (2002) Biometals , vol.15 , pp. 103-120
    • Cortese, M.1    Paszczynski, A.2    Lewis, T.A.3    Sebat, J.4    Crawford, R.L.5
  • 55
    • 0036187139 scopus 로고    scopus 로고
    • Analysis of regulatory elements and genes required for carbon tetrachloride degradation in Pseudomonas stutzeri strain KC
    • Sepulveda-Torres LDC, Huang A, Kim H, Criddle CS: Analysis of regulatory elements and genes required for carbon tetrachloride degradation in Pseudomonas stutzeri strain KC. J. Mol. Microbiol. Biotechnol. 4, 151-161 (2002).
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 151-161
    • Sepulveda-Torres, L.D.C.1    Huang, A.2    Kim, H.3    Criddle, C.S.4
  • 56
    • 1142293848 scopus 로고    scopus 로고
    • Physiological and molecular genetic evaluation of the dechlorination agent, pyridine-2, 6-bis (monothiocarboxylic acid) (PDTC) as a secondary siderophore of Pseudomonas
    • Lewis TA, Leach L, Morales S et al.: Physiological and molecular genetic evaluation of the dechlorination agent, pyridine-2, 6-bis (monothiocarboxylic acid) (PDTC) as a secondary siderophore of Pseudomonas. Environ. Microbiol. 6, 159-169 (2004).
    • (2004) Environ. Microbiol , vol.6 , pp. 159-169
    • Lewis, T.A.1    Leach, L.2    Morales, S.3
  • 57
    • 33751006455 scopus 로고    scopus 로고
    • Transcriptional regulation of the ptd gene cluster of Pseudomonas stutzeri KC involves an AraC/XylS family transcriptional activator (PdtC) and the cognate siderophore pyridine-2, 6-bis (thiocarboxylic acid)
    • Morales S, Lewis TA: Transcriptional regulation of the ptd gene cluster of Pseudomonas stutzeri KC involves an AraC/XylS family transcriptional activator (PdtC) and the cognate siderophore pyridine-2, 6-bis (thiocarboxylic acid). Appl. Environ. Mircobiol. 72, 6994-7002 (2006).
    • (2006) Appl. Environ. Mircobiol , vol.72 , pp. 6994-7002
    • Morales, S.1    Lewis, T.A.2
  • 58
    • 0038464967 scopus 로고    scopus 로고
    • Heteroaromatic monothiocarboxylic acids from Pseudomonas spp
    • Budzikiewicz H: Heteroaromatic monothiocarboxylic acids from Pseudomonas spp. Biodegradation 14, 65-72 (2003).
    • (2003) Biodegradation , vol.14 , pp. 65-72
    • Budzikiewicz, H.1
  • 60
    • 7544230473 scopus 로고    scopus 로고
    • Organotin compounds: Toxicokinetic aspects
    • Appel KE: Organotin compounds: toxicokinetic aspects. Drugs Metab. Rev. 36, 763-786 (2004).
    • (2004) Drugs Metab. Rev , vol.36 , pp. 763-786
    • Appel, K.E.1
  • 61
    • 0037313821 scopus 로고    scopus 로고
    • Tin-carbon cleavage of organotin compounds by pyoverdine from Pseudomonas chlororaphis
    • Inoue H, Takimura O, Kawaguchi K et al.: Tin-carbon cleavage of organotin compounds by pyoverdine from Pseudomonas chlororaphis. Appl. Environ. Microbiol. 69, 878-883 (2003).
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 878-883
    • Inoue, H.1    Takimura, O.2    Kawaguchi, K.3
  • 62
    • 33748795338 scopus 로고    scopus 로고
    • Organotin decomposition by pyochelin, secreted by Pseudomonas aeruginosa even in an iron-sufficient environment
    • Sun GX, Zhou WQ, Zhong JJ: Organotin decomposition by pyochelin, secreted by Pseudomonas aeruginosa even in an iron-sufficient environment. Appl. Environ. Microbiol. 72, 6411-6413 (2006).
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 6411-6413
    • Sun, G.X.1    Zhou, W.Q.2    Zhong, J.J.3
  • 63
    • 33750994052 scopus 로고    scopus 로고
    • Mechanism of augmentation of organotin decomposition by ferripyochelin: Formation of hydroxyl radical and organotin-pyochelin-iron ternary complex
    • Sun GX, Zhong JJ: Mechanism of augmentation of organotin decomposition by ferripyochelin: formation of hydroxyl radical and organotin-pyochelin-iron ternary complex. Appl. Environ. Microbiol. 72, 7264-7269 (2006).
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 7264-7269
    • Sun, G.X.1    Zhong, J.J.2
  • 64
    • 33747097895 scopus 로고    scopus 로고
    • Siderophore production by using free and immobilized cells of two Pseudomonads cultivated in a medium enriched with Fe and/or toxic metals (cr, Hg, Pb)
    • Brand A, Jezequel K, Leger MA, Lebeau T: Siderophore production by using free and immobilized cells of two Pseudomonads cultivated in a medium enriched with Fe and/or toxic metals (cr, Hg, Pb). Biotechnol. Bioeng. 94, 1080-1088 (2006).
    • (2006) Biotechnol. Bioeng , vol.94 , pp. 1080-1088
    • Brand, A.1    Jezequel, K.2    Leger, M.A.3    Lebeau, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.