High-Performance Liquid Chromatography Analyses of Pyoverdin Siderophores Differentiate among Phytopathogenic Fluorescent Pseudomonas Species (original) (raw)
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Brazilian Journal of Microbiology, 2012
Microbial siderophores confiscate the available ferric ions around the roots and trigger a reaction resulting in plant growth promotion. In our study, a high level of siderophore production was observed from a newly isolated Pseudomonas sp. from the rhizosphere of Chickpea plants. Under an iron depleted condition in Standard Succinic acid medium a 1000 µgmL-1 of siderophore production was achieved. Increasing the concentration of iron showed an inverse relationship between growth and siderophore production. Fourier Transform Infrared Spectroscopy (FTIR) analysis of the purified crystals, its UV spectral analysis and High Pressure Liquid Chromatography (HPLC) revealed the identity of the siderophore as similar to that of pyoverdin with distinctive characters. Electron spray ionization mass spectroscopy (ESIMS) shows presence of abundance of A 1 ions (419 m/z) and branching of amino acids from B 1-B 5. This pyoverdin contains a cyclic tetra peptide but Serine and Arginine are missing. Based on our analysis and deviations from the reported structure of pyoverdin it is suggested that this pseudomonas produces distinctly characterized pyoverdin siderophore.
The Pyoverdins of Pseudomonas syringae and Pseudomonas cichorii
Zeitschrift für Naturforschung C, 2004
The structure elucidation of the cyclic (lactonic) forms of the pyoverdins with a succinamide side chain originally produced by the closely related species Pseudomonas syringae and P. cichorii is reported. Mass spectrometry and nuclear magnetic resonance analyses as well as the determination of the configuration of the amino acids after degradation indicate that these two pyoverdins differ only by the replacement of the first in-chain serine by glycine. The pyoverdins of P. syringae and P. cichorii and the dihydropyoverdin of P. syringae can be used by both species as siderophores.
The Pyoverdins of Pseudomonas sp. 96-312 and 96-318
Zeitschrift für Naturforschung C, 2001
The structures of the pyoverdins isolated from the Pseudomonas spp. 96-312 and 96-318 were elucidated by spectroscopic and degradation techniques. As observed before for Pseudomonas spp. producing pyoverdins with a C-terminal cyclopeptidic substructure, the two strains can recognize to some extent structurally different pyoverdins as long as they have also a similar cyclopeptidic C-terminus.
Zeitschrift für Naturforschung. C, Journal of biosciences
The siderophores produced by Pseudomonas fluorescens G173 are unusual in several respects. So far all pyoverdins with a C-terminal cyclopeptidic substructure have in common that the epsilon-amino group of an in-chain Lys is bound amidically to the carboxyl group of a C-terminal Ser or Thr and that N5-formyl-N5-hydroxy Orn (FoOHOrn) is the next amino acid after Lys. FoOHOrn may (cyclotetrapeptidic structures) be or may not (cyclotripeptidic structures) be followed by a further amino acid. In the pyoverdin described here Orn instead of Lys is the amino acid forming the cycle, FoOHOrn is replaced by AcOHOrn which does not follow the branching Orn but is the penultimate amino acid and finally the last amino acid is Asp. The producing strain which had been classified as Pseudomonas fluorescens may well be a new species. Pyoverdins are frequently accompanied by ferribactins which are considered to be their biogenetic precursors. They always have the same amino acid chain as the co-occurri...
Structure Proposal for a New Pyoverdin from Pseudomonas sp. PS 6.10
Zeitschrift für Naturforschung C, 2006
From Pseudomonas sp. PS 6.10, when grown in a casamino acid medium, a pyoverdin was isolated whose primary structure could be deduced from its mass spectrometric fragmentation pattern and amino acid analysis. It belongs to the smallest representatives of this group of siderophores comprising only six amino acids in its peptide chain. When grown in a succinate minimal medium the corresponding ferribactin considered to be the biogenetic precursor of the pyoverdin was obtained as the major component.