Ferribactins as the Biosynthetic Precursors of the Pseudomonas Siderophores Pyoverdins§

So far all pyoverdins with a C-terminal cyclopeptidic substructure have in common that the ε -amino group of an in-chain Lys is bound amidically to the carboxyl group of a C-

From Pseudomonas fluorescens PL7 and PL8 structurally related pyoverdins were isolated and their primary structures were elucidated by spectroscopic methods and degradation reac-

a dihydroxyquinoline chromo- phore responsible for their fluorescence, a peptide chain comprising 6 to 12 amino acids bound to its carboxyl group, and a small dicarboxylic acid (or

producing pyoverdins with a C-terminal cyclopeptidic substructure, the two strains can recognize to some extent structurally different pyoverdins as long as they have also a

12 C scale; COSY, correlated spectroscopy; DEPT, distortionless enhancement by polarization transfer; HMBC, heteronuclear multiple bond correlation; HMQC, heteronuclear multiple

c Laboratoire de Microbiologie et de Ge´ne´tique, UPRES-A 7010 du CNRS, Universite´ Louis Pasteur, 28 rue Goethe, 67000 Strasbourg, France.. * Author for correspondence and

From a Pseudomonas strain obtained from a soil sample collected in Thailand a pyoverdin was obtained containing twelve amino acids in its peptide chain. The structure elucidation

By cross feeding studies structur- ally closely related pyoverdins containing a C-terminal cyclopeptidic substructure were tested regarding the mutual recognition by the