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  • siderophore  (4)
  • Chemistry  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    S, S-rhizoferrin (enantio-rhizoferrin) – a siderophore of Ralstonia (Pseudomonas) pickettii DSM 6297 – the optical antipode of R, R-rhizoferrin isolated from fungi (1999)
    Springer
    BioMetals 12 (1999), S. 189-193 
    Details
    ISSN: 1572-8773
    Keywords: Ralstonia pickettii ; rhizoferrin ; siderophore ; iron transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract From the culture medium of Ralstonia (formerly Burkholderia or Pseudomonas) pickettii DSM 6297 grown under iron-limited conditions an iron complexing compound (siderophore) could be isolated. The structure of the isolated polycarboxylate siderophore was determined by spectroscopic methods as S,S-rhizoferrin, the enantiomer of R,R-rhizoferrin produced by fungi (Zygomycetes). Transport experiments with radiolabelled iron using S,S- and R,R-rhizoferrin showd no differences in the bacterial Ralstonia strain, while transport of R,R-rhizoferrin was superior in the producing fungal Rhizopus strain, suggesting stereoselective recognition in the fungus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009259118034
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  • 2
    Electronic Resource
    Electronic Resource
    A pyoverdine from Pseudomonas putida CFML 90-51 with a Lys ε-amino link in the peptide chain (2000)
    Springer
    BioMetals 13 (2000), S. 147-152 
    Details
    ISSN: 1572-8773
    Keywords: Pseudomonas putida ; pyoverdin ; siderophore
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract From Pseudomonas putida CFML 90-51 – a hospital isolate – a pyoverdine was obtained which is characterized by the unusual linkage by the ε-rather than the α-amino group of Lys in the peptide chain. The structure elucidation by spectroscopic methods and degradation reactions is reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009212729408
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  • 3
    Electronic Resource
    Electronic Resource
    Ornibactin production and transport properties in strains of Burkholderia vietnamiensis and Burkholderia cepacia (formerly Pseudomonas cepacia) (1995)
    Springer
    BioMetals 8 (1995), S. 309-317 
    Details
    ISSN: 1572-8773
    Keywords: Burkholderia ; Pseudomonas ; ornibactin ; siderophore ; iron metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Several strains of Burkholderia vietnamiensis, isolated from the rhizosphere of rice plants, and four strains formerly known as Pseudomonas cepacia including two collection strains and two clinical isolates were compared for siderophore production and iron uptake. The B. vietnamiensis (TVV strains) as well as the B. cepacia strains (ATCC 25416 and ATCC 17759) and the clinical isolates K132 and LMG 6999 were all found to produce ornibactins under iron starvation. The two ATCC strains of B. cepacia additionally produced the previously described siderophores, pyochelin and cepabactin. Analysis of the ratio of isolated ornibactins (C4, C6 and C8) by HPLC revealed nearly identical profiles. Supplementation of the production medium with ornithine (20 mm) resulted in a 2.5-fold increase in ornibactin synthesis. Ornibactin-mediated iron uptake was independent of the length of the acyl side chain and was observed with all strains of B. vietnamiensis and B. cepacia, but was absent with strains of Pseudomonas aeruginosa, Pseudomonas fluorescens and Pseudomonas stutzeri, known to produce pyoverdines or desferriferrioxamines as siderophores. These results suggest that ornibactin production is a common feature of all Burkholderia strains and that these strains develop an ornibactin-specific iron transport system which is distinct from the pyoverdine-specific transport in Pseudomonas strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00141604
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  • 4
    Electronic Resource
    Electronic Resource
    The structure of a pyoverdine from Pseudomonas sp. CFML 96.188 and its relation to other pyoverdines with a cyclic C-terminus (2000)
    Springer
    BioMetals 13 (2000), S. 301-309 
    Details
    ISSN: 1572-8773
    Keywords: Pseudomonas ; iron uptake ; pyoverdine ; siderophore
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract From Pseudomonas sp. CFML 96.188 a pyoverdine was isolated and its primary structure was elucidated by spectroscopic methods and degradation reactions. This strain is of interest as it accepts the structurally different pyoverdines from several other Pseudomonas strains. They all have in common as a specific structural feature a C-terminal cyclic substructure, the importance of which for the recognition of a pyoverdine at the cell surface of a given strain will be discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009235421503
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  • 5
    Electronic Resource
    Electronic Resource
    Solution structure of salmon calcitonin (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 233-241 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Salmon calcitonin, a 32-residue peptide with a 1-7 disulfide bridge, was synthesized by standard solid-phase techniques, and studied by CD and two-dimensional NMR experiments. The peptide was dissolved in pure trifluoroethanol (TFE) and in aqueous solutions containing various amounts of TFE. CD studies in pure TFE indicated the presence of an α-helical structure comprising 40% of the constituent amino acids. This was fully confirmed by nmr. A detailed analysis was performed with the peptide in a 9 : 1 deuterated TFE/H2O mixture. A total of 365 nuclear Overhauser enhancements (154 intraresidual, 112 sequential and 99 long range) were compiled from the nuclear Overhauser enhancement spectroscopy spectra and used in the distance geometry calculations. The core of the peptide between residues 8 and 22 assumes an α-helix like structure. The Cys 1-Cys 7 ring is well defined and in close association with the helix, while the C-terminal decapeptide folds back toward the core, forming a loose loop.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310210
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  • 6
    Electronic Resource
    Electronic Resource
    Structure Elucidation of the Gallium-Ornibactin Complex by 2D-NMR Spectroscopy (1993)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1993 (1993), S. 43-48 
    Details
    ISSN: 0170-2041
    Keywords: Ornibactin ; Siderophore ; Iron complex ; Gallium complex ; Pseudomonas strain TVV 69 ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: From a Pseudomonas strain novel hydroxamate/carboxylate siderophores were isolated which were named ornibactins representing the modified tetrapeptide L-Orn1(Nδ-OH,Nδ-acyl)-D-threo-Asp(β-OH)-L-Ser-L-Orn4(Nδ-OH,N δ-formyl)-1,4-diaminobutane. The side-chain amino function of Orn1(Nδ-OH,Nδ-acyl) is acylated by 3-hydroxyoctanoic acid in the most lipophilic component of the microheterogeneous siderophore mixture. The structure elucidation was based on GC amino acid analysis, GC-MS and electrospray mass spectrometry of the iron complex. The 3-hydroxyoctanoic acid and the primary sequence were established on the basis of 1H and inverse detected 13C two-dimensional NMR spectra (COSY, TOCSY, NOESY, HMQC, HMBC) of the gallium-ornibactin-F complex which allowed the complete assignment of all 1H and 13C signals.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jlac.199319930108
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