ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013
Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Differences in Siderophore Production During the Growth of Phytoplankton in Southern Ocean Incubation Experiments Under High- and Low-Iron Conditions.Environmental microbiology · 2026Article
- Modulating backbone flexibility in hydroxamate siderophores for improved iron chelation and peptide nucleic acid delivery into bacteria.The Biochemical journal · 2026Article
- Tistrellabactins A and B Are PhotoreactiveJournal of natural products · 2023Article
- Design, Synthesis, and Biological Evaluation of Novel Hydroxamic Acid-Based Organoselenium Hybrids.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Chemistry and Biology of Siderophores from Marine Microbes.Marine drugs · 2019Review
- Vibrio Iron Transport: Evolutionary Adaptation to Life in Multiple Environments.Microbiology and molecular biology reviews : MMBR · 2016Review
- Structural characterization of amphiphilic siderophores produced by a soda lake isolate, Halomonas sp. SL01, reveals cysteine-, phenylalanine- and proline-containing head groups.Extremophiles : life under extreme conditions · 2015Article
- Microbial tailoring of acyl peptidic siderophores.Biochemistry · 2014Article
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2 authors at 1 institution in 1 country.
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Abstract
In response to iron-depleted aerobic conditions, bacteria often secrete low molecular weight, high-affinity iron(III)-complexing ligands, siderophores, to solubilize and sequester iron(III). Many marine siderophores are amphiphilic and are produced in suites, wherein each member within a particular suite has the same iron(III)-binding polar head group which is appended by one or two fatty acids of differing length, degree of unsaturation, and degree of hydroxylation, establishing the suite composition. We report the isolation and structural characterization of a suite of siderophores from marine bacterial isolate Vibrio sp. Nt1. On the basis of structural analysis, this suite of siderophores, the moanachelins, is amphiphilic and composed of two N-acetyl-N-hydroxy-D-ornithines, one N-acetyl-N-hydroxy-L-ornithine, and either a glycine or an L-alanine, appended with various saturated and unsaturated fatty acid tails. The variation in the small side-chain amino acid is the first occurrence of variation in the peptidic head group structure of a set of siderophores produced by a single bacterium.
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