Chromopeptide siderophores (azotobactin 87-1 and -II) were isolated from an iron deficient culture medium of Azotobacter vinelandii ATCC 12837 (=DSM 87). Their structures were elu cidated by chemical degradation studies and spectroscopic methods, especially 2D-NMR-tech-niques. Total assignments of 1 H-, 13 C-, and 15 N-resonances based on 2D-HOHAHA-, 1 H/ 13 C-HMQC-, 1 H / 13 C-HMBC-, 1 H / 15 N-HMQC/TOCSY-, and 1 H/ 15 N-HMBC-experiments are given as well as sequential information derived from 1 H/ 1 H-NOESY-, 1 H / 13 C-HMBC-and 1 H/ 13 N-HMBC-experiments. Both Az 87-1 and Az 87-11 consist of a tetracyclic chromophore -(1S)8,9-dihydroxy-4-oxo-2,3,4,5-tetrahydro-1H,10cH-3a,5,10b-triazaacephenantrylene-1-carb-oxylic acid -and a decapeptide chain linked with the N-terminus to the carboxy group of the chromophore containing also modified, non-proteinogenic amino acids. The sequence L-Ser-D-Ser-L-Hse-Gly-D-threo-OHAsp-Hse-Hse-Hse-D-N 5 OH-N 5 -R-Hbu-Om-L-Hse was determined for Az 87-1, while Az 87-11 contains a C-terminal L-Hse-lactone instead. Iron is chelated by the catecholic group of the chromophore, the β-hydroxy aspartic acid, and the hydroxamate function formed by N 5 -hydroxyornithine and R-β-hydroxybutyric acid.