A Pyoverdin from the Antarctica Strain 51W of Pseudomonas fluorescens* Jessica Voss, Kambiz Taraz and Herbert Budzikiewicz

c Chimie Biologique Industrielle, Faculte´ Universitaire des Sciences agronomiques, Passage des De´porte´s, 2, B-5030 Gembloux, Belgium. * Author for correspondence and

A ferribactin having these structural characteristics is produced by the investigated strain, but it is accompanied by derivatives where the α -amino group of Glu is partially

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

Pseudomonas chlororaphis, Pyoverdin, Ferribactin By a feeding experiment with a 15 N-labelled precursor it is shown that ferribactins are transformed into pyover- dins and thus

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