On the conformation of cyclic iron-containing hexapeptides: The crystal and molecular structure of ferrichrysin (cas 18972-10-6)

Add time:07/19/2019    Source:sciencedirect.com

The three-dimensional molecular structure of the cyclic iron(III)-containing hexapeptide ferrichrysin, as elucidated from single crystal X-ray diffraction data, is described. The molecular conformation of this biologically active compound shows similarities with the one observed for the related ferrichrome A. As has been found in similar iron(III) compounds, the iron(III) ions are co-ordinated by three hydroxamate groups in an octahedral cis- Λ arrangement. In ferrichrysin all three ornithyl side chains are stabilized by intra-molecular hydrogen bonds. The fact that all ferrichromes that exhibit iron transport activities contain glycine in the same relative position in the peptide chain, suggests that the type II β-loop observed in both ferrichrysin and ferrichrome A is a biologically significant characteristic feature of the ferrichrome class of compounds.

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