Bacterial siderophores: the structure of a desferriferribactin produced by pseudomonas fluorescens ATCC 13525

✍ Scribed by Caroline Linget; Despina G. Stylianou; Anne Dell; Robert E. Wolff; Yves Piémont; Mohamed A. Abdallah

• Publisher: Elsevier Science
• Year: 1992
• Tongue: French
• Weight: 295 KB
• Volume: 33
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(00)74802-7

✦ Synopsis

The structure of a desferriferribaciin a postulated precursor of pyowrdins produced in iron-deficient cultures of i'seudomonasj7uorescens ATCC 13525 was elucidated using FAB-MS and 20 NMR techniques. II is a partly cyclic pe4xide containing a thirteen-membered ring, as well as an amkiine trpp amino-acid built up on tyrosine

and

2,4

dir minobutyric acid. Whet! Pseudomonasfluorescens ATCC 13525 grows in iron deficient conditions, it excretes a large number of pyo\ erdins l1 possessing the same type of fluorescent chromophore derived from 2,3-diamino-6,7-dihydro>:yquinoline, together with a desferriferribactin which does not have a chromophore but which also chelates iron(II1). Maurer er a1.2 proposed a peptide structure of ten amino acids [Ser(2), Lys(3), N6 -OHOm( ?), Tyr( I), Gly( l), Glu( I)] and two acetyl groups for the desferrifenibactin molecule. After reaction of the pepttde with dinitrofluorobenzene and hydrolysis, they characterized only DNP-glutamic acid and the NHE DNP-delivative from only one lysine molecule, and concluded that desfeniferribactin was cyclic.