Characterization of the chromophores of pyoverdins and related siderophores by electrospray tandem mass spectrometry

Budzikiewicz, H.; Schäfer, Matthias; Fernández, Diana Urı́a; Matthijs, Sandra; Cornélis, Pierre

doi:10.1007/s10534-006-9021-3

Cited by 54 publications

(42 citation statements)

References 18 publications

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“…Mature PVDI is then secreted to the surrounding environment by PvdRT-OpmQ and by an as-yet-unidentified transporter. Immature precursors, such as ferribactin (42) and PVDIq (this study), have also been found in the secreted fraction of fluorescent pseudomonads, indicating that these precursors can also be secreted into the extracellular medium (dashed lines). Once in the medium, PVDI binds iron, forming the PVDI-Fe complex, which can be taken up by the cell, where further steps are conducted.…”

Section: Figsupporting

confidence: 52%

PvdP Is a Tyrosinase That Drives Maturation of the Pyoverdine Chromophore in Pseudomonas aeruginosa

et al. 2014

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eThe iron binding siderophore pyoverdine constitutes a major adaptive factor contributing to both virulence and survival in fluorescent pseudomonads. For decades, pyoverdine production has allowed the identification and classification of fluorescent and nonfluorescent pseudomonads. Here, we demonstrate that PvdP, a periplasmic enzyme of previously unknown function, is a tyrosinase required for the maturation of the pyoverdine chromophore in Pseudomonas aeruginosa. PvdP converts the nonfluorescent ferribactin, containing two iron binding groups, into a fluorescent pyoverdine, forming a strong hexadentate complex with ferrous iron, by three consecutive oxidation steps. PvdP represents the first characterized member of a small family of tyrosinases present in fluorescent pseudomonads that are required for siderophore maturation and are capable of acting on large peptidic substrates.

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Section: Figsupporting

confidence: 52%

PvdP Is a Tyrosinase That Drives Maturation of the Pyoverdine Chromophore in Pseudomonas aeruginosa

et al. 2014

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“…The masses of the newly identified azotobactin derivatives match the masses of putative azotobactin precursors, which are characterized by modifications of the chromophore with a glutamic acid side chain. These structures have been suggested to occur in the following oxidative cascade in pseudomonads: ferribactin ¡ hydroxyl-ferribactin ¡ dihydropyoverdine ¡ pyoverdine ¡ azotobactin (36)(37)(38) (Fig. 4D).…”

Section: Figmentioning

confidence: 95%

The Siderophore Metabolome of Azotobacter vinelandii

Baars

Zhang

Morel

et al. 2016

Appl Environ Microbiol

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In this study, we performed a detailed characterization of the siderophore metabolome, or "chelome," of the agriculturally important and widely studied model organism Azotobacter vinelandii. Using a new high-resolution liquid chromatography-mass spectrometry (LC-MS) approach, we found over 35 metal-binding secondary metabolites, indicative of a vast chelome in A. vinelandii. These include vibrioferrin, a siderophore previously observed only in marine bacteria. Quantitative analyses of siderophore production during diazotrophic growth with different sources and availabilities of Fe showed that, under all tested conditions, vibrioferrin was present at the highest concentration of all siderophores and suggested new roles for vibrioferrin in the soil environment. Bioinformatic searches confirmed the capacity for vibrioferrin production in Azotobacter spp. and other bacteria spanning multiple phyla, habitats, and lifestyles. Moreover, our studies revealed a large number of previously unreported derivatives of all known A. vinelandii siderophores and rationalized their origins based on genomic analyses, with implications for siderophore diversity and evolution. Together, these insights provide clues as to why A. vinelandii harbors multiple siderophore biosynthesis gene clusters. Coupled with the growing evidence for alternative functions of siderophores, the vast chelome in A. vinelandii may be explained by multiple, disparate evolutionary pressures that act on siderophore production.

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“…A detailed study of the electrospray mass spectra (Budzikiewicz et al 2007) allows to present the amino acid sequence of the pyoverdine: Ala-AcOHOrn-Gly-(a)Thr-(a)Thr-Gln-Gly-SercOHOrn. Two isoforms were observed, for one of them with a succinamide (Suca) residue attached to the chromophore (Chr) the typical pattern for a Suca-ChrAla N-terminus was obtained by collision induced fragmentation of [M ?…”

Section: P Thivervalensis Lmg 21626mentioning

confidence: 99%

Pyoverdine and histicorrugatin-mediated iron acquisition in Pseudomonas thivervalensis

Matthijs¹,

Brandt²,

Ongena

et al. 2016

Biometals

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The genome of Pseudomonas thivervalensis LMG 21626T has been sequenced and a genomic, genetic and structural analysis of the siderophore mediated iron acquisition was undertaken. Pseudomonas thivervalensis produces two structurally new siderophores, pyoverdine PYO thi which is typical for P. thivervalensis strains and a closely related strain, and the lipopeptidic siderophore histicorrugatin which is also detected in P. lini. Histicorrugatin consists out of an eight amino acid long peptide which is linked to octanoic acid. It is structurally related to the siderophores corrugatin and ornicorrugatin.

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Characterization of the chromophores of pyoverdins and related siderophores by electrospray tandem mass spectrometry

Cited by 54 publications

References 18 publications

PvdP Is a Tyrosinase That Drives Maturation of the Pyoverdine Chromophore in Pseudomonas aeruginosa

PvdP Is a Tyrosinase That Drives Maturation of the Pyoverdine Chromophore in Pseudomonas aeruginosa

The Siderophore Metabolome of Azotobacter vinelandii

Pyoverdine and histicorrugatin-mediated iron acquisition in Pseudomonas thivervalensis

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