Structure and membrane affinity of new amphiphilic siderophores produced by Ochrobactrum sp. SP18

Jessica D. Martin, Yusai Ito, Vanessa V. Homann, Margo G. Haygood, Alison Butler

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


The coastal α-proteobacterium Ochrobactrum sp. SP18 produces a suite of three citrate-derived, cell-associated amphiphilic siderophores, ochrobactins A-C. The ochrobactins are composed of a citric acid backbone amide-linked to two lysine residues. Each ε-amine of lysine is hydroxylated and acylated forming two hydroxamic acid moieties. One of the acylated appendages of each ochrobactin is (E)-2-decenoic acid. The other acylated appendages for ochrobactins A-C are (E)-2-octenoic acid, octanoic acid and (E)-2-decenoic acid, respectively. The ferric ochrobactin complexes are photoreactive in UV light, producing an oxidized ligand with loss of 46 mass units that can still coordinate Fe(III). The relative partitioning of the apo-ochrobactins, Fe(III) ochrobactins and Fe(III) photoproducts into 1,2-dimyristoyl-sn-glycero-3- phosphocholine vesicles is presented. The ochrobactins are the first example of aerobactin-based siderophores with two fatty acid appendages produced in a suite with varying acyl appendage lengths.

Original languageEnglish (US)
Pages (from-to)633-641
Number of pages9
JournalJournal of Biological Inorganic Chemistry
Issue number5
StatePublished - Jul 2006
Externally publishedYes


  • Ochrobactins
  • Photoreactive amphiphilic siderophore
  • α-Proteobacterium

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry


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