The pyoverdine from Pseudomonas chlororaphis D-TR133 showing mutual acceptance with the pyoverdine of Pseudomonas fluorescens CHAO.
From Pseudomonas chlororaphis D-TR 133 a pyoverdine was isolated and its primary structure were elucidated by spectroscopic methods and degradation reactions. Despite some structural differences, its Fe(III) complex and that of the pyoverdine from Pseudomonas fluorescens CHA0 were taken up by either strain with a high rate. This is explained by a structural similarity between the two pyoverdines which were shown to differ in their structures only by the replacement of Lys by Ala in the C-terminal part of the molecules. An unexpected feature is that the main pyoverdine of P. chlororaphis D-TR133 is accompanied by a minor one where specifically one Ala is replaced by Gly. So far amino acid variations in the peptide chain of pyoverdines produced by a given strain had not been observed amongst the producers of the about fifty pyoverdines reported in the literature.
Barelmann
Insa
I
Institut für Organische Chemie der Universität zu Köln, Greinstr. 4, 50939 Köln, Germany.
Fernández
Diana Uría
DU
Budzikiewicz
Herbert
H
Meyer
Jean-Marie
JM
D015373:Bacterial Typing Techniques; D007501:Iron / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D015394:Molecular Structure; D009842:Oligopeptides; D010860:Pigments, Biological / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D011549:Pseudomonas / Q000737:chemistry*; D011551:Pseudomonas fluorescens / Q000737:chemistry*; D020539:Sequence Analysis, Protein
D009842:Oligopeptides; D010860:Pigments, Biological; C042453:pyoverdin; D007501:Iron