Structure of the yellow-green fluorescent peptide produced by iron-deficient Azotobacter vinelandii strain O

Mapping of mutations in Pseudomonas aeruginosa defective in pyoverdin production

“…Pyoverdin from P. aeruginosa shares structural aspects with other bacterial yellow-green fluorescent peptides: pseudobactin from Pseudomonas strain B10 (37), pyoverdin from Pseudomonas fluorescens (28,32,33), pseudobactin 7SR1 from a plant-deleterious Pseudomonas strain (44), and azotobactin from A. vinelandii (5,15). The same dihydroxyquinoline derivative, responsible for the fluorescence of these compounds, is present in all these compounds with only minor structural differences.…”

“…This fluorescent siderophore produced by P. aeruginosa is a complex peptide containing two hydroxamate groups and a dihydroxyquinoline derivative (42) as its theorized chelating moieties. Yellow-green fluorescent peptides produced by other fluorescent Pseudomonas species and Azotobacter vinelandii (5,15,28,32,33,37,44) have similar spectral characteristics and extensive structural homology with pyoverdin.Recent investigations have suggested that iron acquisition by P. aeruginosa may play a role in its pathogenesis. The concentration of iron in culture medium has a significant effect on the production of the extracellular proteins, toxin A, alkaline protease, and elastase (3, 4).…”

“…This fluorescent siderophore produced by P. aeruginosa is a complex peptide containing two hydroxamate groups and a dihydroxyquinoline derivative (42) as its theorized chelating moieties. Yellow-green fluorescent peptides produced by other fluorescent Pseudomonas species and Azotobacter vinelandii (5,15,28,32,33,37,44) have similar spectral characteristics and extensive structural homology with pyoverdin.…”

Microbial Siderophores

“…Both of them are accompanied by compounds where the C-terminal Hse forms a g-lactone ring (azotobactin 87-II and d). An azotobactin O for which also a structure had been proposed (120) was shown later to be identical with azotobactin D (272). For secondary metabolites see protochelin and its constituents (Sect.…”

The presence of intracellular proteolytic enzyme activities in Azotobacter vinelandii strain O cultured in iron-deficient medium.

“…Fukasawa and Goto have previously reported the determination of the structure and biosynthesis of the yellow-green fluorescent peptide. 3,4) In the course of the culture of Azotobacter vinelandii in iron-deficient medium, the growth of cell populations was extremely reduced by comparison to that of iron-containing medium. In order to obtain information on the relationship between biosynthesis of the yellow-green fluorescent peptide and low cell numbers of Azotobacter vinelandii strain 0 in iron free media, the proteolytic activity with and without iron in the culture medium was determined in water soluble protein fraction of the bacteria.…”