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Bacterial iron transport: Structure elucidation by FAB-MS and by 2D NMR (1H, 13C, 15N) of pyoverdin G4R, a peptidic siderophore produced by a nitrogen-fixing strain of Pseudomonas putida

✍ Scribed by Abdel Latif M. Salah El Din; Pavel Kyslík; Danielle Stephan; Mohamed A. Abdallah


Publisher
Elsevier Science
Year
1997
Tongue
French
Weight
911 KB
Volume
53
Category
Article
ISSN
0040-4020

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✦ Synopsis


The structures of the pyoverdins excreted in iron-deficient conditions by Pseudomonas putida G4R, a nitrogen-fixing Pseudomonas have been established using FAB-MS and 2D 111, 13C & 15N NMR on both the unlabelled and the 15Nlabelled molecules. They are chromopeptides possessing the following linear heptapeptide: (L)-Asp-(L)-Orn-(D)-threo-fl-OHAsp-(L)-CTHPMD-Gly-(L)-Ser-(L)cyclo-OHOrn, bearing a new natural amino acid which is the result of the condensation of one mole of (D) fl-threo-hydroxyaspartic acid and one mole of (L)

2, 4--diaminobuOeric acid forming a tetrahydropyrimidine ring.