BACTERIAL IRON TRANSPORT - STRUCTURE ELUCIDATION BY FAB-MS AND BY 2D NMR (H-1, C-13, N-15) OF PYOVERDIN G4R, A PEPTIDIC SIDEROPHORE PRODUCED BY A NITROGEN-FIXING STRAIN OF PSEUDOMONAS-PUTIDA
Alms. Eldin et al., BACTERIAL IRON TRANSPORT - STRUCTURE ELUCIDATION BY FAB-MS AND BY 2D NMR (H-1, C-13, N-15) OF PYOVERDIN G4R, A PEPTIDIC SIDEROPHORE PRODUCED BY A NITROGEN-FIXING STRAIN OF PSEUDOMONAS-PUTIDA, Tetrahedron, 53(37), 1997, pp. 12539-12552
The structures of the pyoverdins excreted in iron-deficient conditions
by Pseudomonas putida G4R, a nitrogen-fixing Pseudomonas have been es
tablished using FAB-MS and 2D H-1, C-13 & N-15 NMR on both the unlabel
led and the N-15-labelled molecules. They are chromopeptides possessin
g the following linear heptapeptide: beta-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) beta-threo-hydroxyaspartic aci
d and one mole of (L) 2,4-diaminobutyric acid forming a tetrahydropyri
midine ring. (C) 1997 Elsevier Science Ltd.