ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2018
β-Hydroxyaspartic acid in siderophores: biosynthesis and reactivity.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Lipid interactions couple turnercyclamycin antibacterial activity with carbohydrate-active enzyme packaging in membrane vesicles.RSC chemical biology · 2026Article
- Iron starvation induced by vacidobactin A impairs the growth of pyoverdine-deficientMicrobiology spectrum · 2026Article
- Comparative metabolomic profiling ofFrontiers in chemistry · 2023Article
- Nonribosomal Peptide Synthesis Definitely Working Out of the Rules.Microorganisms · 2022Review
- Alison Butler: papers in celebration of her 2018 ACS Alfred Bader Award in Bioorganic or Bioinorganic Chemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- The Desotamide Family of Antibiotics.Antibiotics (Basel, Switzerland) · 2020Review
- Potashchelins, a Suite of Lipid Siderophores Bearing Both L-Frontiers in chemistry · 2020Article
- Genomic analysis of siderophore β-hydroxylases reveals divergent stereocontrol and expands the condensation domain family.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A reevaluation of iron binding by Mycobactin J.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
A growing number of siderophores are found to contain β-hydroxyaspartic acid (β-OH-Asp) as a functional group for Fe(III) coordination, along with the more common catechol and hydroxamic acid groups. This review covers the structures, biosynthesis, and reactions of peptidic β-OH-Asp siderophores. Hydroxylation of Asp in siderophore biosynthesis is predicted to be carried out either through discrete aspartyl β-hydroxylating enzymes or through hydroxylating domains within non-ribosomal peptide synthetases, both of which display sequence homology to known non-heme iron(II), α-ketoglutarate-dependent dioxygenases. Ferric complexes of β-OH-Asp siderophores are photoreactive, resulting in reduction of Fe(III) and oxidative cleavage of the siderophore to yield distinct types of photoproducts. Probing the photoreactivity of synthetic Fe(III)-α-hydroxycarboxylate clusters yields mechanistic insights into the different photoproducts observed for β-OH-Asp and other α-hydroxycarboxylate siderophore Fe(III) complexes.
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