Struktur von Ferribactin aus Pseudomonas fluorescens ATCC 13525 [1] / The Structure of Ferribactin from Pseudomonasfluorescens ATCC 13525 [1]

Hohlneicher, U.; Hartmann, Rudolf; Taraz, K.; Budzikiewicz, H.

doi:10.1515/znb-1992-1119

Cited by 10 publications

(3 citation statements)

References 9 publications

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“…HPLC, gas chromatography, FAB-MS, analysis of the sequence characteristic ions in the ESI-MS spectrum after collisioninduced dissociation, one-and two-dimensional NMR. Indeed and unfortunately, such laborious and timeconsuming studies have resulted in the elucidation of already known pyoverdine structures, as in the case of P. aeruginosa pyoverdines (Briskot et al, 1989 ;Demange et al, 1990;Eng-Wilmot et af., 1990;Gipp et al, 1991;Tappe et af., 1993), or for some other pyoverdines and related compounds synthesized by various strains of P. chlororaphis, P. fluorescens and P. putida species or by undetermined fluorescent pseudomonad isolates (Demange et al, 1986;Persmark et al, 1990;Andriollo et al, 1992;Linget et al, 1992a, b ;Hohlneicher et al, 1992Hohlneicher et al, ,1995Glennon et al, 1994). To avoid such a waste of time and energy, any method which could allow a rapid recognition and comparison of a given pyoverdine with already known compounds would be of great interest for deciding whether or not a chemical investigation is required.…”

Section: Discussionmentioning

confidence: 99%

Siderotyping of fluorescent pseudomonads:characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica

et al. 1998

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Siderotyping of fluorescent pseudomonads t characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica J ea n-M a r ie M eyer, Al a in S t i ntz i, Va I& i e Cou I a ng es, S isi nt h y S h ivaj i * Jessica A. VossJ3 Kambiz Taraz3 and Herbert Budzikiewicz3 Five independent fluorescent pseudomonad isolates originating from Antarctica were analysed for their pyoverdine systems. A pyoverdine-related siderotyping, which involved pyoverdine-induced growth stimulation, pyoverdine-mediated iron uptake, pyoverdine analysis by electrophoresis and isoelectric focusing, revealed three different pyoverdine-related siderotypes among the five isolates. One siderotype, including Pseudomonas fluorescens 1W and P. fluorescens lOcW, was identical to that of P. fluorescens ATCC 13525. Two other strains, P. fluorescens 9AW and Pseudomonas putida 9BW, showed identical pyoverdine-related behaviour t o each other, whereas the fifth strain, P. fluorescens 5lW, had unique features compared to the other strains or t o a set of 12 fluorescent Pseudomonas strains used as comparison material. Elucidation of the structure of the pyoverdines produced by the Antarctic strains supported the accuracy of the siderotyping methodology by confirming that pyoverdines from strains 1W and 1OcW had the same structures as the P. fluorescens ATCC 13525 pyoverdine, whereas the 9AW and 9BW pyoverdines are probably identical with the pyoverdine of P. fluorescens strain 244. Pyoverdine from strain 51W appeared t o be a novel pyoverdine since i t s structure was different from all previously established pyoverdine structures. Together with the conclusion that the Antarctic Pseudomonas strains have no special features at the level of their pyoverdines and pyoverdine-mediated iron metabolism compared to worldwide strains, the present work demonstrates that siderotyping provides a rapid means of screening for novel pyoverdines.

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Section: Discussionmentioning

confidence: 99%

Siderotyping of fluorescent pseudomonads:characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica

et al. 1998

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“…Under iron deficient conditions Azotobacter vinelandii (strain D) secretes high amounts of a fluorescent siderophore called azotobactin, a chromopeptidic siderophore belonging to the class of pyoverdins, the peptidic siderophores of the fluorescent pseudomonads . Pyoverdins are constituted of a fluorescent chromophore derived from 2,3-diamino-6,7-dihydroxyquinoline, bound via a carboxylic acid group to the N terminus of an oligopeptide of 6−12 amino acids of various chirality and composition with a linear, − partially cyclic, − or fully cyclic backbone.…”

Section: Introductionmentioning

confidence: 99%

Bacterial Iron Transport: Coordination Properties of Azotobactin, the Highly Fluorescent Siderophore ofAzotobacter vinelandii

et al. 2003

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Azotobacter vinelandii, a nitrogen-fixing soil bacterium, secretes in iron deficiency azotobactin delta, a highly fluorescent pyoverdin-like chromopeptidic hexadentate siderophore. The chromophore, derived from 2,3-diamino-6,7 dihydroxyquinoline, is bound to a peptide chain of 10 amino acids: (L)-Asp-(D)-Ser-(L)-Hse-Gly-(D)-beta-threo-HOAsp-(L)-Ser-(D)-Cit-(L)-Hse-(L)-Hse lactone-(D)-N(delta)-Acetyl, N(delta)-HOOrn. Azotobactin delta has three different iron(III) binding sites which are one hydroxamate group at the C-terminal end of the peptidic chain (N(delta)-Acetyl, N(delta)-HOOrn), one alpha-hydroxycarboxylic function in the middle of the chain (beta-threo-hydroxyaspartic acid), and one catechol group on the chromophore. The coordination properties of its iron(III) and iron(II) complexes were measured by spectrophotometry, potentiometry, and voltammetry after the determination of the acid-base functions of the uncomplexed free siderophore. Strongly negatively charged ferric species were observed at neutral p[H]'s corresponding to a predominant absolute configuration Lambda of the ferric complex in solution as deduced from CD measurements. The presence of an alpha-hydroxycarboxylic chelating group does not decrease the stability of the iron(III) complex when compared to the main trishydroxamate siderophores or to pyoverdins. The value of the redox potential of ferric azotobactin is highly consistent with a reductive step by physiological reductants for the iron release. Formation and dissociation kinetics of the azotobactin delta ferric complex point out that both ends of this long siderophore chain get coordinated to Fe(III) before the middle. The most striking result provided by fluorescence measurements is the lasting quenching of the fluorophore in the course of the protonation of the ferric azotobactin delta complex. Despite the release of the hydroxyacid and of the catechol, the fluorescence remains indeed quenched, when iron(III) is bound only to the hydroxamic acid, suggesting a folded conformation at this stage, around the metal ion, in contrast to the unfolded species observed for other siderophores such as ferrioxamine or pyoverdin PaA.

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“…Azoverdin is a chromopeptide very closely related in structure to pyoverdins, the peptidic siderophores of the fluorescent Pseudomonas (9). Pyoverdins are composed of a fluorescent chromophore derived from 2,3-diamino-6,7dihydroxyquinoline, bound via a carboxylic acid group to the N-terminus of an oligopeptide of 6-12 amino acids of varying chirality and composition with a linear (10)(11)(12)(13)(14)(15)(16)(17), partially cyclic (18)(19)(20)(21)(22)(23)(24)(25)(26), or fully cyclic (27) backbone.…”

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confidence: 99%

The Three-Dimensional Structure of the Gallium Complex of Azoverdin, a Siderophore of Azomonas macrocytogenes ATCC 12334, Determined by NMR Using Residual Dipolar Coupling Constants

Wasielewski¹,

Atkinson²,

Abdallah³

et al. 2002

Biochemistry

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In iron-deficient conditions, Azomonas macrocytogenes ATCC 12334 excretes a fluorescent siderophore called azoverdin, which is composed of a six-amino-acid peptide chain linked to a chromophore. Azoverdin chelates iron(III) very strongly, solubilizing it and transporting it back into the cells using an outer-membrane receptor. This compound is related to the pyoverdins, the peptidic siderophores of Pseudomonas, but differs in the site on the chromophore at which the peptide is covalently linked. This feature identifies azoverdin as a member of a new class of pyoverdins: the isopyoverdins. We report the three-dimensional structure of azoverdin-Ga(III) in solution. The use of orientational constraints obtained from the measurement of residual dipolar couplings using samples dissolved in a liquid crystalline medium allowed us to define the absolute configuration of the metal complex, which is Delta. The structure is characterized by a U-shape adopted by the peptide chain, with the N(delta)-acetyl-N(delta)-hydroxyornithine side chains adopting extended conformations in order to chelate the gallium ion. This conformation leaves a large open space permitting access to the gallium ion. The structural consequences of the particular isopyoverdin chemical structure are discussed in the context of the three-dimensional structures of other pyoverdins.

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Struktur von Ferribactin aus Pseudomonas fluorescens ATCC 13525 [1] / The Structure of Ferribactin from Pseudomonasfluorescens ATCC 13525 [1]

Cited by 10 publications

References 9 publications

Siderotyping of fluorescent pseudomonads:characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica

Siderotyping of fluorescent pseudomonads:characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica

Bacterial Iron Transport: Coordination Properties of Azotobactin, the Highly Fluorescent Siderophore ofAzotobacter vinelandii

The Three-Dimensional Structure of the Gallium Complex of Azoverdin, a Siderophore of Azomonas macrocytogenes ATCC 12334, Determined by NMR Using Residual Dipolar Coupling Constants

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