The structure of the pyoverdin isolated from various Pseudomonas syringae pathovars.
From seven different pathovars of Pseudomonas syringae representing various genetic subgroups, and one strain of Pseudomonas viridiflava the same pyoverdin siderophore (1) was isolated, probably identical with the pyoverdin whose amino acid composition (but not their sequence) had been reported before. 1 is the first pyoverdin where two of the ligands for Fe3+ are beta-hydroxy Asp units. Its remarkably high complexing constant for Fe3+ at pH 5 as compared with other pyoverdins offers a definite advantage in plant infection. The structure elucidation of 1 will be described and the taxonomical implications regarding pyoverdins with different structures ascribed previously to P. syringae strains will be discussed.
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Institut für Organische Chemie der Universität zu Köln, Germany. aco88@uni-koeln.de
Taraz
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K
Budzikiewicz
H
H
Geoffroy
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V
Meyer
J M
JM
Gardan
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L
D000595:Amino Acid Sequence; D001692:Biological Transport; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D007501:Iron / Q000378:metabolism; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D010446:Peptide Fragments / Q000737:chemistry; D010860:Pigments, Biological / Q000737:chemistry* / Q000302:isolation & purification; D011549:Pseudomonas / Q000378:metabolism*; D017262:Siderophores / Q000737:chemistry
D008024:Ligands; D009842:Oligopeptides; D010446:Peptide Fragments; D010860:Pigments, Biological; D017262:Siderophores; C042453:pyoverdin; D007501:Iron