<jats:title>Abstract</jats:title> <jats:p> 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 <jats:sup>1</jats:sup>H-, <jats:sup>13</jats:sup>C-, and <jats:sup>15</jats:sup>N-resonances based on 2D-HOHAHA-, <jats:sup>1</jats:sup>H/<jats:sup>13</jats:sup>C-HMQC-, <jats:sup>1</jats:sup>H /<jats:sup>13</jats:sup>C-HMBC-, <jats:sup>1</jats:sup>H /<jats:sup>15</jats:sup>N-HMQC/TOCSY-, and <jats:sup>1</jats:sup>H/<jats:sup>15</jats:sup>N-HMBC-experiments are given as well as sequential information derived from <jats:sup>1</jats:sup>H/<jats:sup>1</jats:sup>H-NOESY-, <jats:sup>1</jats:sup>H /<jats:sup>13</jats:sup>C-HMBC-and <jats:sup>1</jats:sup>H/ <jats:sup>13</jats:sup>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<jats:sup>5</jats:sup>OH-N<jats:sup>5</jats:sup>-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<jats:sup>5</jats:sup>-hydroxyornithine and R-β-hydroxybutyric acid.