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Bacillibactin and enterobactin are hexadentate catecholate siderophores produced by bacteria upon iron limitation in order to scavenge ferric ion and is the ultimate siderophores of their Gram-positive and Gram-negative domains. The enzymes are stereospecific and the studies have helped in understanding the microbial iron transport mediated by these two siderophores, from initial recognition and transport to intracellular iron release.

Multidimensional Fourier transformation (MFT) method is used to obtain a three dimensional C[alpha]-coupled HNCO spectrum. The measured J coupling values have provided information about backbone torsion angles at early stages of protein structure determination and the technique can be used for determining various residual dipolar couplings and for resolving chemical shifts in partially unfolded proteins.

The incorporation of iron-binding moieties of 3,4-catecholamide into a siderophore is described as a bacterial strategy to evade the immune system. The studies have shown that while the insertion of 3,4-catecholamide subunits in the siderophore structure has not increased its affinity for ferric ion as compared to hydroxamates, it has promoted catalysis of iron removal from transferrin and evasion from siderocalin binding.