메뉴 건너뛰기




Volumn 44, Issue 5, 2013, Pages 1267-1277

Fate of ferrisiderophores after import across bacterial outer membranes: Different iron release strategies are observed in the cytoplasm or periplasm depending on the siderophore pathways

Author keywords

ABC transporters; Iron homeostasis; Iron uptake; Siderophore; TonB dependent transporters

Indexed keywords

ABC TRANSPORTER; CEPABACTIN; CITRIC ACID; DEFEROXAMINE; DESFERRICHROME; ENTEROCHELIN; FERRISIDEROPHORE; MYCOBACTIN; PERMEASE; PROTEIN TONB; PYOCHELIN; PYOVERDINE; RHIZOFERRIN; SIDEROPHORE; UNCLASSIFIED DRUG; VIBRIOBACTIN; YERSINIABACTIN;

EID: 84876665028     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-013-1468-2     Document Type: Review
Times cited : (133)

References (83)
  • 1
    • 69849115536 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of trilactone siderophores: Where chiral recognition occurs in enterobactin and bacillibactin iron transport
    • 10.1021/ja903051q 19673474 10.1021/ja903051q 1:CAS:528: DC%2BD1MXps1yksr4%3D
    • Abergel RJ, Zawadzka AM, Hoette TM, Raymond KN (2009) Enzymatic hydrolysis of trilactone siderophores: where chiral recognition occurs in enterobactin and bacillibactin iron transport. J Am Chem Soc 131:12682-12692. doi: 10.1021/ja903051q
    • (2009) J Am Chem Soc , vol.131 , pp. 12682-12692
    • Abergel, R.J.1    Zawadzka, A.M.2    Hoette, T.M.3    Raymond, K.N.4
  • 2
    • 0031599719 scopus 로고    scopus 로고
    • Coordination chemistry of siderophores: Thermodynamics and kinetics of iron chelation and release
    • 1:CAS:528:DyaK1cXmsl2gsA%3D%3D
    • Albrecht-Gary AM, Crumbliss AL (1998) Coordination chemistry of siderophores: thermodynamics and kinetics of iron chelation and release. Metal Ions Biological Systems 35:239-327
    • (1998) Metal Ions Biological Systems , vol.35 , pp. 239-327
    • Albrecht-Gary, A.M.1    Crumbliss, A.L.2
  • 3
    • 0029766824 scopus 로고    scopus 로고
    • Extracellular iron reductase activity produced by Listeria monocytogenes
    • DOI 10.1007/s002030050354
    • Barchini E, Cowart RE (1996) Extracellular iron reductase activity produced by Listeria monocytogenes. Arch Microbiol 166:51-57 (Pubitemid 26291321)
    • (1996) Archives of Microbiology , vol.166 , Issue.1 , pp. 51-57
    • Barchini, E.1    Cowart, R.E.2
  • 4
    • 45649085030 scopus 로고    scopus 로고
    • Plant carbohydrate scavenging through tonb-dependent receptors: A feature shared by phytopathogenic and aquatic bacteria
    • 17311090 10.1371/journal.pone.0000224
    • Blanvillain S, Meyer D, Boulanger A, Lautier M, Guynet C, Denance N et al (2007) Plant carbohydrate scavenging through tonb-dependent receptors: a feature shared by phytopathogenic and aquatic bacteria. PLoS ONE 2:e224
    • (2007) PLoS ONE , vol.2 , pp. 224
    • Blanvillain, S.1    Meyer, D.2    Boulanger, A.3    Lautier, M.4    Guynet, C.5    Denance, N.6
  • 5
    • 0029017649 scopus 로고
    • The mobile ferrous iron pool in Escherichia coli is bound to a phosphorylated sugar derivative
    • 7647518 10.1007/BF00143380 1:STN:280:DyaK2MznsFCqsA%3D%3D
    • Bohnke R, Matzanke BF (1995) The mobile ferrous iron pool in Escherichia coli is bound to a phosphorylated sugar derivative. Biometals 8:223-230
    • (1995) Biometals , vol.8 , pp. 223-230
    • Bohnke, R.1    Matzanke, B.F.2
  • 7
    • 66149125265 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa pyochelin-iron uptake pathway and its metal specificity
    • 10.1128/JB.00010-09 10.1128/JB.00010-09
    • Braud A, Hannauer M, Mislin GLA, Schalk IJ (2009a) The Pseudomonas aeruginosa pyochelin-iron uptake pathway and its metal specificity. J Bacteriol 191:5317-5325. doi: 10.1128/JB.00010-09
    • (2009) J Bacteriol , vol.191 , pp. 5317-5325
    • Braud, A.1    Hannauer, M.2    Mislin, G.L.A.3    Schalk, I.J.4
  • 8
    • 65349127542 scopus 로고    scopus 로고
    • New insights into the metal specificity of the Pseudomonas aeruginosa pyoverdine-iron uptake pathway
    • 10.1111/j.1462-2920.2008.01838.x 19207567 10.1111/j.1462-2920.2008.01838. x 1:CAS:528:DC%2BD1MXmsVeqt7w%3D
    • Braud A, Hoegy F, Jezequel K, Lebeau T, Schalk IJ (2009b) New insights into the metal specificity of the Pseudomonas aeruginosa pyoverdine-iron uptake pathway. Environ Microbiol 11:1079-1091. doi: 10.1111/j.1462-2920.2008.01838.x
    • (2009) Environ Microbiol , vol.11 , pp. 1079-1091
    • Braud, A.1    Hoegy, F.2    Jezequel, K.3    Lebeau, T.4    Schalk, I.J.5
  • 9
    • 0031610907 scopus 로고    scopus 로고
    • Bacterial iron transport: Mechanisms, genetics, and regulation
    • 9444760 1:CAS:528:DyaK1cXmsl2hug%3D%3D
    • Braun V, Hantke K, Koster W (1998) Bacterial iron transport: mechanisms, genetics, and regulation. Met Ions Biol Syst 35:67-145
    • (1998) Met Ions Biol Syst , vol.35 , pp. 67-145
    • Braun, V.1    Hantke, K.2    Koster, W.3
  • 10
    • 0026724913 scopus 로고
    • Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex
    • 1534808 1:CAS:528:DyaK38Xlt1Ojsrc%3D
    • Brickman TJ, McIntosh MA (1992) Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. J Biol Chem 267:12350-12355
    • (1992) J Biol Chem , vol.267 , pp. 12350-12355
    • Brickman, T.J.1    McIntosh, M.A.2
  • 11
    • 80054736579 scopus 로고    scopus 로고
    • Pyochelin enantiomers and their outer membrane siderophore transporters in fluorescent Pseudomonads: Structural bases of a unique enantiospecific recognition
    • 10.1021/ja205504z 21902256 10.1021/ja205504z 1:CAS:528: DC%2BC3MXht1Wks7%2FE
    • Brillet K, Reimmann C, Mislin GLA, Noël S, Rognan D, Schalk IJ, Cobessi D (2011) Pyochelin enantiomers and their outer membrane siderophore transporters in fluorescent Pseudomonads: structural bases of a unique enantiospecific recognition. J Am Chem Soc 133:16503-16509. doi: 10.1021/ja205504z
    • (2011) J Am Chem Soc , vol.133 , pp. 16503-16509
    • Brillet, K.1    Reimmann, C.2    Mislin, G.L.A.3    Noël, S.4    Rognan, D.5    Schalk, I.J.6    Cobessi, D.7
  • 12
    • 84871564039 scopus 로고    scopus 로고
    • An ABC transporter with two periplasmic binding proteins involved in iron acquisition in Pseudomonas aeruginosa
    • in press
    • Brillet K, Ruffenach F, Adams H, Journet L, Gasser V, Hoegy F et al (2012) An ABC transporter with two periplasmic binding proteins involved in iron acquisition in Pseudomonas aeruginosa. ACS Chem Biol, in press
    • (2012) ACS Chem Biol
    • Brillet, K.1    Ruffenach, F.2    Adams, H.3    Journet, L.4    Gasser, V.5    Hoegy, F.6
  • 13
    • 0027983767 scopus 로고
    • Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae
    • Butterton JR, Calderwood SB (1994) Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae. J Bacteriol 176:5631-5638 (Pubitemid 24280495)
    • (1994) Journal of Bacteriology , vol.176 , Issue.18 , pp. 5631-5638
    • Butterton, J.R.1    Calderwood, S.B.2
  • 16
    • 0036889483 scopus 로고    scopus 로고
    • Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides
    • DOI 10.1128/JB.184.23.6434-6436.2002
    • Cheng Q, Park JT (2002) Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J Bacteriol 184:6434-6436 (Pubitemid 35332545)
    • (2002) Journal of Bacteriology , vol.184 , Issue.23 , pp. 6434-6436
    • Cheng, Q.1    Park, J.T.2
  • 17
    • 78651359481 scopus 로고    scopus 로고
    • A structural and functional analysis of type III periplasmic and substrate binding proteins: Their role in bacterial siderophore and heme transport
    • 10.1515/BC.2011.012 21194366 10.1515/bc.2011.012 1:CAS:528: DC%2BC3MXkvFCrsLk%3D
    • Chu BC, Vogel HJ (2011) A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport. Biol Chem 392:39-52. doi: 10.1515/BC.2011.012
    • (2011) Biol Chem , vol.392 , pp. 39-52
    • Chu, B.C.1    Vogel, H.J.2
  • 18
    • 0034127329 scopus 로고    scopus 로고
    • The structure of the ferric siderophore binding protein FhuD complexed with gallichrome
    • DOI 10.1038/74048
    • Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW (2000) The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat Struct Biol 7:287-291 (Pubitemid 30194451)
    • (2000) Nature Structural Biology , vol.7 , Issue.4 , pp. 287-291
    • Clarke, T.E.1    Ku, S.-Y.2    Dougan, D.R.3    Vogel, H.J.4    Tari, L.W.5
  • 19
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • DOI 10.1074/jbc.M109385200
    • Clarke TE, Braun V, Winkelmann G, Tari LW, Vogel HJ (2002) X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin. J Biol Chem 277:13966-13972 (Pubitemid 34968004)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 20
    • 33845556505 scopus 로고
    • The complexities of ascorbate as a reducing agent
    • 10.1021/ic50226a088 1:CAS:528:DyaL3MXmtVCgsb0%3D
    • Creutz C (1981) The complexities of ascorbate as a reducing agent. Inorg Chem 20:4449-4452
    • (1981) Inorg Chem , vol.20 , pp. 4449-4452
    • Creutz, C.1
  • 21
    • 2442485987 scopus 로고    scopus 로고
    • Identification of rhtX and fptX, Novel Genes Encoding Proteins That Show Homology and Function in the Utilization of the Siderophores Rhizobactin 1021 by Sinorhizobium meliloti and Pyochelin by Pseudomonas aeruginosa, Respectively
    • DOI 10.1128/JB.186.10.2996-3005.2004
    • Cuiv PO, Clarke P, Lynch D, O'Connell M (2004) Identification of rhtX and fptX, novel genes encoding proteins that show homology and function in the utilization of the siderophores rhizobactin 1021 by Sinorhizobium meliloti and pyochelin by Pseudomonas aeruginosa, respectively. J Bacteriol 186:2996-3005 (Pubitemid 38612853)
    • (2004) Journal of Bacteriology , vol.186 , Issue.10 , pp. 2996-3005
    • Cuiv, P.O.1    Clarke, P.2    Lynch, D.3    O'Connell, M.4
  • 24
    • 0024436779 scopus 로고
    • Nucleotide sequence and regulation of the Escherichia coli gene for ferrienterobactin transport protein FepB
    • Elkins MF, Earhart CF (1989) Nucleotide sequence and regulation of the Escherichia coli gene for ferrienterobactin transport protein FepB. J Bacteriol 171:5443-5451 (Pubitemid 19252429)
    • (1989) Journal of Bacteriology , vol.171 , Issue.10 , pp. 5443-5451
    • Elkins, M.F.1    Earhart, C.F.2
  • 25
    • 80052080449 scopus 로고    scopus 로고
    • The structural biology of beta-barrel membrane proteins: A summary of recent reports
    • 10.1016/j.sbi.2011.05.005 21719274 10.1016/j.sbi.2011.05.005 1:CAS:528:DC%2BC3MXhtV2qu7rL
    • Fairman JW, Noinaj N, Buchanan SK (2011) The structural biology of beta-barrel membrane proteins: a summary of recent reports. Curr Opin Struct Biol 21:523-531. doi: 10.1016/j.sbi.2011.05.005
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 523-531
    • Fairman, J.W.1    Noinaj, N.2    Buchanan, S.K.3
  • 26
    • 0034079929 scopus 로고    scopus 로고
    • Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
    • Ferguson AD, Braun V, Fiedler HP, Coulton JW, Diederichs K, Welte W (2000) Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci 9:956-963 (Pubitemid 30353337)
    • (2000) Protein Science , vol.9 , Issue.5 , pp. 956-963
    • Ferguson, A.D.1    Braun, V.2    Fiedler, H.-P.3    Coulton, J.W.4    Diederichs, K.5    Welte, W.6
  • 27
    • 0032921490 scopus 로고    scopus 로고
    • YbtP and YbtQ: Two ABC transporters required for iron uptake in Yersinia pestis
    • Fetherston JD, Bertolino VJ, Perry RD (1999) YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis. Mol Microbiol 32:289-299 (Pubitemid 29178696)
    • (1999) Molecular Microbiology , vol.32 , Issue.2 , pp. 289-299
    • Fetherston, J.D.1    Bertolino, V.J.2    Perry, R.D.3
  • 28
    • 0035352919 scopus 로고    scopus 로고
    • Siderotyping: A powerful tool for the characterization of pyoverdines
    • 11895292 10.2174/1568026013395542 1:CAS:528:DC%2BD3MXjsVyisLc%3D
    • Fuchs R, Schafer M, Geoffroy V, Meyer JM (2001) Siderotyping: a powerful tool for the characterization of pyoverdines. Curr Top Med Chem 1:31-57
    • (2001) Curr Top Med Chem , vol.1 , pp. 31-57
    • Fuchs, R.1    Schafer, M.2    Geoffroy, V.3    Meyer, J.M.4
  • 29
    • 34047268399 scopus 로고    scopus 로고
    • Real time fluorescent resonance energy transfer visualization of ferric pyoverdine uptake in Pseudomonas aeruginosa: A role for ferrous iron
    • DOI 10.1074/jbc.M609238200
    • Greenwald J, Hoegy F, Nader M, Journet L, Mislin GLA, Graumann PL, Schalk IJ (2007) Real-time FRET visualization of ferric-pyoverdine uptake in Pseudomonas aeruginosa: a role for ferrous iron. J Biol Chem 282:2987-2995 (Pubitemid 47084339)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 2987-2995
    • Greenwald, J.1    Hoegy, F.2    Nader, M.3    Journet, L.4    Mislin, G.L.A.5    Graumann, P.L.6    Schalk, I.J.7
  • 30
    • 65949102784 scopus 로고    scopus 로고
    • FpvA bound to non-cognate pyoverdines: Molecular basis of siderophore recognition by an iron transporter
    • 19504741 10.1111/j.1365-2958.2009.06721.x 1:CAS:528:DC%2BD1MXnsVSrsLg%3D
    • Greenwald J, Nader M, Celia H, Gruffaz C, Geoffroy V, Meyer JM et al (2009) FpvA bound to non-cognate pyoverdines: molecular basis of siderophore recognition by an iron transporter. Mol Microbiol 72:1246-1259
    • (2009) Mol Microbiol , vol.72 , pp. 1246-1259
    • Greenwald, J.1    Nader, M.2    Celia, H.3    Gruffaz, C.4    Geoffroy, V.5    Meyer, J.M.6
  • 31
    • 0041042405 scopus 로고
    • Studies of the reactions of ferric iron with gluthatione and some related thiols
    • 10.1016/S0020-1693(00)86480-4 1:CAS:528:DyaL3sXps1Cmsw%3D%3D
    • Hamed MY, Silver J, Wilson MT (1983) Studies of the reactions of ferric iron with gluthatione and some related thiols. Inorg Chem Acta 78:1-11
    • (1983) Inorg Chem Acta , vol.78 , pp. 1-11
    • Hamed, M.Y.1    Silver, J.2    Wilson, M.T.3
  • 32
    • 77749270483 scopus 로고    scopus 로고
    • The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechansim with acylation of the siderophore and a recycling of the modified desferrichrome
    • 10.1128/JB.01539-09 20047910 10.1128/JB.01539-09 1:CAS:528: DC%2BC3cXivVSgu78%3D
    • Hannauer M, Barda Y, Mislin GL, Shanzer A, Schalk IJ (2010) The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechansim with acylation of the siderophore and a recycling of the modified desferrichrome. J Bacteriol 192:1212-1220. doi: 10.1128/JB.01539-09
    • (2010) J Bacteriol , vol.192 , pp. 1212-1220
    • Hannauer, M.1    Barda, Y.2    Mislin, G.L.3    Shanzer, A.4    Schalk, I.J.5
  • 33
    • 84863192539 scopus 로고    scopus 로고
    • The PvdRT-OpmQ efflux pump controls the metal selectivity of the iron uptake pathway mediated by the siderophore pyoverdine in Pseudomonas aeruginosa
    • 10.1111/j.1462-2920.2011.02674 22187978 10.1111/j.1462-2920.2011.02674.x 1:CAS:528:DC%2BC38Xhtleht7zK
    • Hannauer M, Braud A, Hoegy F, Ronot P, Boos A, Schalk IJ (2012) The PvdRT-OpmQ efflux pump controls the metal selectivity of the iron uptake pathway mediated by the siderophore pyoverdine in Pseudomonas aeruginosa. Environ Microbiol 14:1696-1708. doi: 10.1111/j.1462-2920.2011.02674
    • (2012) Environ Microbiol , vol.14 , pp. 1696-1708
    • Hannauer, M.1    Braud, A.2    Hoegy, F.3    Ronot, P.4    Boos, A.5    Schalk, I.J.6
  • 35
    • 67651207865 scopus 로고    scopus 로고
    • The redox hypothesis in siderophore-mediated iron uptake
    • 10.1007/s10534-009-9233-4 19357971 10.1007/s10534-009-9233-4 1:CAS:528:DC%2BD1MXotFCisrs%3D
    • Harrington JM, Crumbliss AL (2009) The redox hypothesis in siderophore-mediated iron uptake. Biometals 22:679-689. doi: 10.1007/s10534-009-9233-4
    • (2009) Biometals , vol.22 , pp. 679-689
    • Harrington, J.M.1    Crumbliss, A.L.2
  • 36
    • 0015765566 scopus 로고
    • Facilitation of Fe(II) autoxidation by Fe(II) complexing agents
    • 4206209 10.1016/0304-4165(73)90019-6 1:CAS:528:DyaE2cXht12msrw%3D
    • Harris DC, Aisen P (1973) Facilitation of Fe(II) autoxidation by Fe(II) complexing agents. Biochim Biophys Acta 329:156-158
    • (1973) Biochim Biophys Acta , vol.329 , pp. 156-158
    • Harris, D.C.1    Aisen, P.2
  • 37
    • 0019306798 scopus 로고
    • Iron transport in Escherichia coli: Uptake and modification of ferrichrome
    • Hartman A, Braun V (1980) Iron transport in Escherichia coli: uptake and modification of ferrichrome. J Bacteriol 143:246-255 (Pubitemid 10019653)
    • (1980) Journal of Bacteriology , vol.143 , Issue.1 , pp. 246-255
    • Hartmann, A.1    Braun, V.2
  • 38
    • 77951981537 scopus 로고    scopus 로고
    • Chemistry and biology of siderophores
    • 10.1039/b906679a 10.1039/b906679a
    • Hider RC, Kong X (2011a) Chemistry and biology of siderophores. Nat Prod Rep 27:637-657. doi: 10.1039/b906679a
    • (2011) Nat Prod Rep , vol.27 , pp. 637-657
    • Hider, R.C.1    Kong, X.2
  • 39
    • 83555173402 scopus 로고    scopus 로고
    • Glutathione: A key component of the cytoplasmic labile iron pool
    • 10.1007/s10534-011-9476-8 21769609 10.1007/s10534-011-9476-8 1:CAS:528:DC%2BC3MXhsVKhsrbL
    • Hider RC, Kong XL (2011b) Glutathione: a key component of the cytoplasmic labile iron pool. Biometals 24:1179-1187. doi: 10.1007/s10534-011-9476-8
    • (2011) Biometals , vol.24 , pp. 1179-1187
    • Hider, R.C.1    Kong, X.L.2
  • 40
    • 67649304833 scopus 로고    scopus 로고
    • Stereospecificity of the siderophore pyochelin outer membrane transporters in fluorescent Pseudomonads
    • 10.1074/jbc.M900606200 19297329 10.1074/jbc.M900606200 1:CAS:528:DC%2BD1MXmtlChtb8%3D
    • Hoegy F, Lee X, Noël S, Mislin GL, Rognan D, Reimmann C, Schalk IJ (2009) Stereospecificity of the siderophore pyochelin outer membrane transporters in fluorescent Pseudomonads. J Biol Chem 284:14949-14957. doi: 10.1074/jbc.M900606200
    • (2009) J Biol Chem , vol.284 , pp. 14949-14957
    • Hoegy, F.1    Lee, X.2    Noël, S.3    Mislin, G.L.4    Rognan, D.5    Reimmann, C.6    Schalk, I.J.7
  • 41
    • 77955879883 scopus 로고    scopus 로고
    • Susceptibility of Pseudomonas aeruginosa to catechol-substituted cephalosporin is unrelated to the pyochelin-Fe transporter FptA
    • 10.1007/s00726-009-0353-5 19777323 10.1007/s00726-009-0353-5 1:CAS:528:DC%2BC3cXlt1Omtbw%3D
    • Hoegy F, Gwynn MN, Schalk IJ (2010) Susceptibility of Pseudomonas aeruginosa to catechol-substituted cephalosporin is unrelated to the pyochelin-Fe transporter FptA. Amino Acids 38:1627-1629. doi: 10.1007/s00726-009-0353-5
    • (2010) Amino Acids , vol.38 , pp. 1627-1629
    • Hoegy, F.1    Gwynn, M.N.2    Schalk, I.J.3
  • 42
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter - Binding protein complex BtuCD-BtuF
    • DOI 10.1126/science.1145950
    • Hvorup RN, Goetz BA, Niederer M, Hollenstein K, Perozo E, Locher KP (2007) Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317:1387-1390 (Pubitemid 47417478)
    • (2007) Science , vol.317 , Issue.5843 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 43
    • 73949146114 scopus 로고    scopus 로고
    • Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa
    • 10.1073/pnas.0908760106 19906986 10.1073/pnas.0908760106 1:CAS:528:DC%2BC3cXjtFWisw%3D%3D
    • Imperi F, Tiburzi F, Visca P (2009) Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa. Proc Natl Acad Sci USA 106:20440-20445. doi: 10.1073/pnas.0908760106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20440-20445
    • Imperi, F.1    Tiburzi, F.2    Visca, P.3
  • 44
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction
    • Jacobs C, Huang LJ, Bartowsky E, Normark S, Park JT (1994) Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction. EMBO J 13:4684-4694 (Pubitemid 24310220)
    • (1994) EMBO Journal , vol.13 , Issue.19 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.-J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 45
    • 50049089034 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake
    • 17916327 10.1016/j.bbamem.2007.07.026 1:CAS:528:DC%2BD1cXhtVKnt77E
    • Krewulak KD, Vogel HJ (2008) Structural biology of bacterial iron uptake. Biochim Biophys Acta 1778:1781-1804
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1781-1804
    • Krewulak, K.D.1    Vogel, H.J.2
  • 46
    • 84855431538 scopus 로고    scopus 로고
    • An evolutionary mechanism for diversity in siderophore-producing bacteria
    • 10.1111/j.1461-0248.2011.01717 22151214 10.1111/j.1461-0248.2011.01717.x
    • Lee W, van Baalen M, Jansen VA (2012) An evolutionary mechanism for diversity in siderophore-producing bacteria. Ecol Lett 15:119-125. doi: 10.1111/j.1461-0248.2011.01717
    • (2012) Ecol Lett , vol.15 , pp. 119-125
    • Lee, W.1    Van Baalen, M.2    Jansen, V.A.3
  • 47
    • 23744479843 scopus 로고    scopus 로고
    • In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes
    • DOI 10.1021/ja0522027
    • Lin H, Fischbach MA, Liu DR, Walsh CT (2005) In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J Am Chem Soc 127:11075-11084 (Pubitemid 41129884)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.31 , pp. 11075-11084
    • Lin, H.1    Fischbach, M.A.2    Liu, D.R.3    Walsh, C.T.4
  • 48
    • 33644777983 scopus 로고    scopus 로고
    • The heterologous siderophores ferrioxamine B and ferrichrome activate signaling pathways in Pseudomonas aeruginosa
    • DOI 10.1128/JB.188.5.1882-1891.2006
    • Llamas MA, Sparrius M, Kloet R, Jimenez CR, Vandenbroucke-Grauls C, Bitter W (2006) The heterologous siderophores ferrioxamine B and ferrichrome activate signaling pathways in Pseudomonas aeruginosa. J Bacteriol 188:1882-1891 (Pubitemid 43346867)
    • (2006) Journal of Bacteriology , vol.188 , Issue.5 , pp. 1882-1891
    • Llamas, M.A.1    Sparrius, M.2    Kloet, R.3    Jimenez, C.R.4    Vandenbroucke-Grauls, C.5    Bitter, W.6
  • 49
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • DOI 10.1126/science.1071142
    • Locher KP, Lee AT, Rees DC (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296:1793-1800 (Pubitemid 34517120)
    • (2002) Science , vol.296 , Issue.5570 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 50
    • 33751500166 scopus 로고
    • Solution equilibria of enterobactin complexes
    • 10.1021/ic00005a008 1:CAS:528:DyaK3MXhtFOisrs%3D
    • Loomis L, Raymond KN (1991) Solution equilibria of enterobactin complexes. Inorg Chem 30:906-911
    • (1991) Inorg Chem , vol.30 , pp. 906-911
    • Loomis, L.1    Raymond, K.N.2
  • 51
    • 0031923708 scopus 로고    scopus 로고
    • Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake
    • DOI 10.1007/s004380050718
    • Mademidis A, Koster W (1998) Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake. Mol Gen Genet 258:156-165 (Pubitemid 28223181)
    • (1998) Molecular and General Genetics , vol.258 , Issue.1-2 , pp. 156-165
    • Mademidis, A.1    Koster, W.2
  • 52
    • 0030662644 scopus 로고    scopus 로고
    • ATP-dependent ferric hydroxamate transport system in Escherichia coli: Periplasmic FhuD interacts with a periplasmic and with a transmembrane/ cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping
    • Mademidis A, Killmann H, Kraas W, Flechsler I, Jung G, Braun V et al (1997) ATP-dependent ferric hydroxamate transport system in Escherichia coli: periplasmic FhuD interacts with a periplasmic and with a transmembrane/ cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping. Mol Microbiol 26:1109-1123 (Pubitemid 27507893)
    • (1997) Molecular Microbiology , vol.26 , Issue.5 , pp. 1109-1123
    • Mademidis, A.1    Killmann, H.2    Kraas, W.3    Flechsler, I.4    Jung, G.5    Braun, V.6
  • 54
    • 0036084292 scopus 로고    scopus 로고
    • Identification of the Vibrio cholerae enterobactin receptors VctA and IrgA: IrgA is not required for virulence
    • DOI 10.1128/IAI.70.7.3419-3426.2002
    • Mey AR, Wyckoff EE, Oglesby AG, Rab E, Taylor RK, Payne SM (2002) Identification of the Vibrio cholerae enterobactin receptors VctA and IrgA: IrgA is not required for virulence. Infect Immun 70:3419-3426 (Pubitemid 34665978)
    • (2002) Infection and Immunity , vol.70 , Issue.7 , pp. 3419-3426
    • Mey, A.R.1    Wyckoff, E.E.2    Oglesby, A.G.3    Rab, E.4    Taylor, R.K.5    Payne, S.M.6
  • 55
    • 34249294573 scopus 로고    scopus 로고
    • Ferripyochelin uptake genes are involved in pyochelin-mediated signalling in Pseudomonas aeruginosa
    • DOI 10.1099/mic.0.2006/002915-0
    • Michel L, Bachelard A, Reimmann C (2007) Ferripyochelin uptake genes are involved in pyochelin-mediated signalling in Pseudomonas aeruginosa. Microbiology 153:1508-1518 (Pubitemid 46804321)
    • (2007) Microbiology , vol.153 , Issue.5 , pp. 1508-1518
    • Michel, L.1    Bachelard, A.2    Reimmann, C.3
  • 56
    • 33646950666 scopus 로고    scopus 로고
    • Ternary complex formation facilitates a redox mechanism for iron release from a siderophore
    • DOI 10.1007/s10534-005-4342-1, Special Issue on Microbial Iron Transport, Storage and Metabolism
    • Mies KA, Wirgau JI, Crumbliss AL (2006) Ternary complex formation facilitates a redox mechanism for iron release from a siderophore. Biometals 19:115-126 (Pubitemid 43794822)
    • (2006) BioMetals , vol.19 , Issue.2 , pp. 115-126
    • Mies, K.A.1    Wirgau, J.I.2    Crumbliss, A.L.3
  • 57
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • DOI 10.1128/MMBR.00012-07
    • Miethke M, Marahiel MA (2007) Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol Rev 71:413-451 (Pubitemid 47429279)
    • (2007) Microbiology and Molecular Biology Reviews , vol.71 , Issue.3 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 59
    • 83455262902 scopus 로고    scopus 로고
    • The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli
    • 10.1021/bi201517h 22098718 10.1021/bi201517h 1:CAS:528:DC%2BC3MXhsVyrs7rK
    • Miethke M, Hou J, Marahiel MA (2011) The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli. Biochemistry 50:10951-10964. doi: 10.1021/bi201517h
    • (2011) Biochemistry , vol.50 , pp. 10951-10964
    • Miethke, M.1    Hou, J.2    Marahiel, M.A.3
  • 60
    • 33751386342 scopus 로고
    • Oxidation/reduction potential of glutathione
    • 10.1021/jo00067a060 1:CAS:528:DyaK3sXksVektrk%3D
    • Millis KK, Weaver KH, Rabenstein DL (1993) Oxidation/reduction potential of glutathione. J Org Chem 58:4144-4146
    • (1993) J Org Chem , vol.58 , pp. 4144-4146
    • Millis, K.K.1    Weaver, K.H.2    Rabenstein, D.L.3
  • 61
    • 33645055640 scopus 로고    scopus 로고
    • Binding properties of pyochelin and structurally related molecules to FptA of Pseudomonas aeruginosa
    • 16499928 10.1016/j.jmb.2006.01.080 1:CAS:528:DC%2BD28XivVGqtrs%3D
    • Mislin GLA, Hoegy F, Cobessi D, Poole K, Rognan D, Schalk IJ (2006) Binding properties of pyochelin and structurally related molecules to FptA of Pseudomonas aeruginosa. J Mol Biol 357:1437-1448
    • (2006) J Mol Biol , vol.357 , pp. 1437-1448
    • Mislin, G.L.A.1    Hoegy, F.2    Cobessi, D.3    Poole, K.4    Rognan, D.5    Schalk, I.J.6
  • 62
    • 0021016161 scopus 로고
    • Identification of the iron chelate in hepatocyte cytosol
    • Morley CG, Bezkorovainy A (1983) Identification of the iron chelate in hepatocyte cytosol. IRCS Med Sci 11:1106-1107 (Pubitemid 14202540)
    • (1983) IRCS Medical Science , vol.11 , Issue.12 , pp. 1106-1107
    • Morley, C.G.D.1    Bezkorovainy, A.2
  • 63
    • 33747327461 scopus 로고    scopus 로고
    • An [{Fe(mecam)}2]6- bridge in the crystal structure of a ferric enterobactin binding protein
    • 16927323 10.1002/anie.200601198
    • Muller A, Wilkinson AJ, Wilson KS, Duhme-Klair AK (2006) An [{Fe(mecam)}2]6- bridge in the crystal structure of a ferric enterobactin binding protein. Angew Chem Int Ed Engl 45:5132-5136
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5132-5136
    • Muller, A.1    Wilkinson, A.J.2    Wilson, K.S.3    Duhme-Klair, A.K.4
  • 64
    • 79960837602 scopus 로고    scopus 로고
    • Yersiniabactin iron uptake: Mechanisms and role in Yersinia pestis pathogenesis
    • 10.1016/j.micinf.2011.04.008 21609780 10.1016/j.micinf.2011.04.008 1:CAS:528:DC%2BC3MXpslKrsbw%3D
    • Perry RD, Fetherston JD (2011) Yersiniabactin iron uptake: mechanisms and role in Yersinia pestis pathogenesis. Microbes Infect 13:808-817. doi: 10.1016/j.micinf.2011.04.008
    • (2011) Microbes Infect , vol.13 , pp. 808-817
    • Perry, R.D.1    Fetherston, J.D.2
  • 65
    • 0346636767 scopus 로고    scopus 로고
    • Iron acquisition and its control in Pseudomonas aeruginosa: Many roads lead to Rome
    • 12700066 10.2741/1051 1:CAS:528:DC%2BD3sXjvVWksb0%3D
    • Poole K, McKay GA (2003) Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome. Front Biosci 8:d661-d686
    • (2003) Front Biosci , vol.8
    • Poole, K.1    McKay, G.A.2
  • 67
    • 84860539117 scopus 로고    scopus 로고
    • Inner-membrane transporters for the siderophores pyochelin in Pseudomonas aeruginosa and enantio-pyochelin in Pseudomonas fluorescens display different enantioselectivities
    • 10.1099/mic.0.057430-0 22343350 10.1099/mic.0.057430-0 1:CAS:528:DC%2BC38XptFemsLc%3D
    • Reimmann C (2012) Inner-membrane transporters for the siderophores pyochelin in Pseudomonas aeruginosa and enantio-pyochelin in Pseudomonas fluorescens display different enantioselectivities. Microbiology 158:1317-1324. doi: 10.1099/mic.0.057430-0
    • (2012) Microbiology , vol.158 , pp. 1317-1324
    • Reimmann, C.1
  • 68
    • 41949113530 scopus 로고    scopus 로고
    • Metal trafficking via siderophores in Gram-negative bacteria: Specificities and characteristics of the pyoverdine pathway
    • 10.1016/j.jinorgbio.2007.11.017 10.1016/j.jinorgbio.2007.11.017 1:CAS:528:DC%2BD1cXkvVyjsb4%3D
    • Schalk IJ (2008) Metal trafficking via siderophores in Gram-negative bacteria: specificities and characteristics of the pyoverdine pathway. J Inorg Biochemi 102:1159-1169. doi: 10.1016/j.jinorgbio.2007.11.017
    • (2008) J Inorg Biochemi , vol.102 , pp. 1159-1169
    • Schalk, I.J.1
  • 69
    • 84873448278 scopus 로고    scopus 로고
    • Innovation and originalities in the strategies developed by bacteria to get access to iron
    • doi: 10.1002/cbic.201200738
    • Schalk IJ (2013) Innovation and originalities in the strategies developed by bacteria to get access to iron. Chembiochem 14:293-294. doi: 10.1002/cbic.201200738
    • (2013) Chembiochem , vol.14 , pp. 293-294
    • Schalk, I.J.1
  • 70
    • 0037022174 scopus 로고    scopus 로고
    • Recycling of pyoverdin on the FpvA receptor after ferric pyoverdin uptake and dissociation in Pseudomonas aeruginosa
    • DOI 10.1021/bi0157767
    • Schalk IJ, Abdallah MA, Pattus F (2002) Recycling of pyoverdin on the FpvA receptor after ferric pyoverdin uptake and dissociation in Pseudomonas aeruginosa. Biochemistry 41:1663-1671 (Pubitemid 34112757)
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1663-1671
    • Schalk, I.J.1    Abdallah, M.A.2    Pattus, F.3
  • 71
    • 80055065227 scopus 로고    scopus 로고
    • New roles for bacterial siderophores in metal transport and tolerance
    • 10.1111/j.1462-2920.2011.02556 21883800 10.1111/j.1462-2920.2011.02556.x 1:CAS:528:DC%2BC3MXhs1emtbbF
    • Schalk IJ, Hannauer M, Braud A (2011) New roles for bacterial siderophores in metal transport and tolerance. Environ Microbiol 13:2844-2854. doi: 10.1111/j.1462-2920.2011.02556
    • (2011) Environ Microbiol , vol.13 , pp. 2844-2854
    • Schalk, I.J.1    Hannauer, M.2    Braud, A.3
  • 72
    • 84867155796 scopus 로고    scopus 로고
    • Structure, function and binding selectivity and stereoselectivity of siderophore-iron outer membrane transporters
    • 10.1016/B978-0-12-394390-3.00002-1 23046646 10.1016/B978-0-12-394390-3. 00002-1
    • Schalk IJ, Mislin GL, Brillet K (2012) Structure, function and binding selectivity and stereoselectivity of siderophore-iron outer membrane transporters. Curr Top Membr 69:37-66. doi: 10.1016/B978-0-12-394390-3.00002-1
    • (2012) Curr Top Membr , vol.69 , pp. 37-66
    • Schalk, I.J.1    Mislin, G.L.2    Brillet, K.3
  • 73
    • 46149094595 scopus 로고    scopus 로고
    • New substrates for TonB-dependent transport: Do we only see the 'tip of the iceberg'?
    • 10.1016/j.tibs.2008.04.012 18539464 10.1016/j.tibs.2008.04.012 1:CAS:528:DC%2BD1cXotlaitbg%3D
    • Schauer K, Rodionov DA, de Reuse H (2008) New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'? Trends Biochem Sci 33:330-338. doi: 10.1016/j.tibs.2008.04.012
    • (2008) Trends Biochem Sci , vol.33 , pp. 330-338
    • Schauer, K.1    Rodionov, D.A.2    De Reuse, H.3
  • 74
    • 0025915699 scopus 로고
    • Nucleotide sequence and genetic organization of the ferric enterobactin transport system: Homology to other periplasmic binding protein-dependent systems in Escherichia coli
    • Shea CM, McIntosh MA (1991) Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli. Mol Microbiol 5:1415-1428 (Pubitemid 21896168)
    • (1991) Molecular Microbiology , vol.5 , Issue.6 , pp. 1415-1428
    • Shea, C.M.1    McIntosh, M.A.2
  • 75
    • 0035123718 scopus 로고    scopus 로고
    • Aqueous solution speciation of Fe(III) complexes with dihydroxamate siderophores alcaligin and rhodotorulic acid and synthetic analogues using electrospray ionization mass spectrometry
    • DOI 10.1021/ic991390x
    • Spasojevic I, Boukhalfa H, Stevens RD, Crumbliss AL (2001) Aqueous solution speciation of Fe(III) complexes with dihydroxamate siderophores alcaligin and rhodotorulic acid and synthetic analogues using electrospray ionization mass spectrometry. Inorg Chem 40:49-58 (Pubitemid 32183283)
    • (2001) Inorganic Chemistry , vol.40 , Issue.1 , pp. 49-58
    • Spasojevic, I.1    Boukhalfa, H.2    Stevens, R.D.3    Crumbliss, A.L.4
  • 76
    • 0029100970 scopus 로고
    • Escherichia coli periplasmic protein FepB binds ferrienterobactin
    • 7551033 10.1099/13500872-141-7-1647 1:CAS:528:DyaK2MXntFGgu7Y%3D
    • Stephens DL, Choe MD, Earhart CF (1995) Escherichia coli periplasmic protein FepB binds ferrienterobactin. Microbiology 141(Pt 7):1647-1654
    • (1995) Microbiology , vol.141 , Issue.PART 7 , pp. 1647-1654
    • Stephens, D.L.1    Choe, M.D.2    Earhart, C.F.3
  • 77
    • 84970583204 scopus 로고
    • Outer-sphere electron-transfer reactions of ascorbate anions
    • 10.1071/CH9821133 1:CAS:528:DyaL38Xlt1Kkur8%3D
    • Williams KE, Yandel JK (1982) Outer-sphere electron-transfer reactions of ascorbate anions. Aust J Chem 35:1133-1144
    • (1982) Aust J Chem , vol.35 , pp. 1133-1144
    • Williams, K.E.1    Yandel, J.K.2
  • 78
    • 84870817080 scopus 로고    scopus 로고
    • X-ray structure of the Yersinia pestis heme transporter HmuUV
    • 10.1038/nsmb.2417 23142986
    • Woo JS, Zeltina A, Goetz BA, Locher KP (2012) X-ray structure of the Yersinia pestis heme transporter HmuUV. Nat Struct Mol Biol. doi: 10.1038/nsmb.2417
    • (2012) Nat Struct Mol Biol
    • Woo, J.S.1    Zeltina, A.2    Goetz, B.A.3    Locher, K.P.4
  • 79
    • 80052743066 scopus 로고    scopus 로고
    • The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand
    • 21790806 10.1111/j.1365-2958.2011.07775.x 1:CAS:528:DC%2BC3MXht1CgsL%2FF
    • Wyckoff EE, Payne SM (2011) The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand. Mol Microbiol 81:1446-1458
    • (2011) Mol Microbiol , vol.81 , pp. 1446-1458
    • Wyckoff, E.E.1    Payne, S.M.2
  • 80
    • 34248669292 scopus 로고    scopus 로고
    • Iron acquisition in Vibrio cholerae
    • DOI 10.1007/s10534-006-9073-4, Biometals: function and transport in bacteria, fungi, and humans
    • Wyckoff EE, Mey AR, Payne SM (2007) Iron acquisition in Vibrio cholerae. Biometals 20:405-416 (Pubitemid 46776587)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 405-416
    • Wyckoff, E.E.1    Mey, A.R.2    Payne, S.M.3
  • 81
    • 78649645704 scopus 로고    scopus 로고
    • An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa
    • 10.1016/j.febslet.2010.10.051 10.1111/j.1758-2229.2009.00115.x 1:CAS:528:DC%2BC3cXot1ersbs%3D
    • Yeterian E, Martin LW, Lamont IL, Schalk IJ (2010) An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa. Environ Microbiol Report 2:412-418. doi: 10.1016/j.febslet.2010.10.051
    • (2010) Environ Microbiol Report , vol.2 , pp. 412-418
    • Yeterian, E.1    Martin, L.W.2    Lamont, I.L.3    Schalk, I.J.4
  • 82
    • 37249020818 scopus 로고    scopus 로고
    • Pseudomonas fluorescens CHA0 produces enantio-pyochelin, the optical antipode of the pseudomonas aeruginosa siderophore pyochelin
    • DOI 10.1074/jbc.M707039200
    • Youard ZA, Mislin GL, Majcherczyk PA, Schalk IJ, Reimmann C (2007) Pseudomonas fluorescens CHA0 produces enantio-pyochelin, the optical antipode of the Pseudomonas aeruginosa siderophore pyochelin. J Biol Chem 282:35546-35553 (Pubitemid 350277122)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35546-35553
    • Youard, Z.A.1    Mislin, G.L.A.2    Majcherczyk, P.A.3    Schalk, I.J.4    Reimmann, C.5
  • 83
    • 22144439383 scopus 로고    scopus 로고
    • Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization
    • DOI 10.1099/mic.0.27888-0
    • Zhu M, Valdebenito M, Winkelmann G, Hantke K (2005) Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization. Microbiology 151:2363-2372 (Pubitemid 40984309)
    • (2005) Microbiology , vol.151 , Issue.7 , pp. 2363-2372
    • Zhu, M.1    Valdebenito, M.2    Winkelmann, G.3    Hantke, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.