Abstract
p-azidobenzoyloxy desferriferricrocin (AF) 2, a photoactivatable analog of ferrichrome, was prepared by selective acylation of the serine group of ferricrocin 1 in two steps: transesterification of ferricrocin followed by demetallation. A model compound, (L) 2-benzyloxycarbonylamino-3-p-azidobenzoyloxy N-isopropyl propionamide 8, was separately synthesized in order to set up optimal transesterification conditions to avoid α, β-elimination or epimerization of serine. Binding of iron-loaded AF (FeAF) to the FhuA outer membrane receptor protein of Escherichia coli AB2847 was demonstrated by inhibition of ferrichrome transport, interference with the infection by the bacteriophage φ80 and with killing of cells by albomycin and colicin M. FeAF transported iron only weakly which indicates that the photoaffinity moiety is incompatible with transport or intracellular iron release from the siderophore.
Similar content being viewed by others
References
Anderson GW, Zimmerman JE, Callahan FM. 1964 The use of esters of N-hydroxysuccinimide in peptide synthesis. J Am Chem Soc 86, 1839-1842.
Bailey CT, Kime-Hunt EM, Carrano CJ, Huschka HG, Winkelmann G. 1986 A photoaffinity label for the siderophore-mediated iron transport system in Neurospora crassa. Biochim Biophys Acta 883, 299-305.
Boos W, Shuman H, 1998 Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microb Mol Biol Rev 62, 204-229.
Boulanger P, Le Maire M, Bonhivers M, Dubois S, Desmadril M, Letellier L. 1996 Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Biochemistry 35, 14216-14224.
Braun V, Hantke K. 1997 Receptor-mediated bacterial iron transport. In: Winkelmann G, Carrano CJ, eds. Transition Metals in Microbial Metabolism. Amsterdam, Harwood Academic Publishers, 81-116.
Braun V, Schaller K, Wolff H. 1973 A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli. Biochem Biophys Acta 323, 87-97.
Braun V, Hantke K, Köster W. 1998 Bacterial iron transport: mechanisms, genetics and regulation. In: Sigel A, Sigel S, eds. Metal Ions in Biological Systems. Iron Transport and Storage in Microorganisms, Plants and Animals. New York, Marcel Dekker, 67-145.
Carmel G, Hellstern D, Henning D, Coulton JW. 1990 Insertion mutagenesis of the gene encoding the ferrichrome-iron receptor of Escherichia coli. J Bacteriol 172, 1861-1869.
Coulton JW, Naegeli HU, Braun, V. 1979 Iron supply of Escherichia coli with polymer-bound ferricrocin. Eur J Biochem 99, 39-47.
Galardy RE, Craig LC, Jamieson JD, Printz MP. 1974 Photoaffinity labeling of peptide hormone binding sites. J Biol Chem 249, 3510-3518.
Keller-Schierlein W, Deer A. 1963 Zur Konstitution von Ferrichrysin und Ferricrocin. Helv Chem Acta 46, 1907-1920.
Killmann H, Braun V. 1992 An aspartate deletion mutation defines a binding site of the multifunctional FhuA outer membrane receptor of Escherichia coli. J Bacteriol 174, 3479-3486.
Killmann H, Braun V. 1993 Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli. EMBO J 12, 3007-3016.
Killmann H, Herrmann C, Wolff H, Braun V. 1998 Identification of a new site for ferrichrome transport by comparison of the FhuA proteins of Escherichia coli, Salmonella paratyphi B, Salmonella typhimurium, and Pantoea agglomerans. J Bacteriol 180, 3845-3852.
Koebnik R, Braun V. 1993 Insertion derivatives containing segments of up to 16 amino acids identify surface-and periplasm-exposed regions of the FhuA outer membrane receptor of Escherichia coli. J Bacteriol 175, 828-839.
Köster W, Braun V. 1990 Iron(III) hydroxamate transport into Escherichia coli. Substrate binding to the periplasmic FhuD protein. J Biol Chem 265, 21407-21410.
Locher KP, Rosenbusch JP. 1997. Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes. Eur J Biochem 247, 770-775.
Neilands JB. 1982. Microbial envelope proteins related to iron. Annu Rev Microbiol 36, 285-309.
Nelson M, Carrano CJ, Szaniszlo PJ. 1992. Identification of the ferrioxamine B receptor FoxB in Escherichia coli. BioMetals 5, 37-46.
Nikaido H, Vaara M. 1985 Molecular basis of bacterial outer-membrane permeability. Microbiol Rev 45, 1-32.
Ocaktan A, Schalk I, Hennard C, Linget-Morice C, Kyslik P, Smith AW, Lambert PA, Abdallah MA. 1996 Specific photoaffinity labeling of a ferripyoverdin outer-membrane receptor of Pseudomonas aeruginosa. FEBS Lett 396, 243-247.
Rohrbach MR, Braun V, Köster W. 1995 Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB. J Bacteriol 177, 7186-7193.
Salah El Din AM, Kyslik P, Stephan D, Abdallah MA. 1997 Bacterial siderophores: Structure elucidation and 1H, 13C, 15N two-dimensional NMR assignments of pyoverdin G4R and related siderophores synthesized by a nitrogen-fixing strain of Pseudomonas putida. Tetrahedron 53, 12539-12552.
Schluter DN, Mamantov G, Vercellotti J. 1974. Reactivity of Nacetyl-3-O-p-tolylsulfonyl-D,L-serine methyl ester: nucleophilic displacement by water at C-3 versus elimination. Carbohydrate Res 38, 333-338.
Schneider E, Hunke S. 1998 ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol Rev 22, 2-20.
Wong GB, Kapel MJ, Raymond KN, Matzanke B, Winkelmann G. 1983 Coordination chemistry of microbial iron-transport compounds: 24. Cheracterization of coprogen and ferricrocin, two ferric hydroxamate siderophores. J Am Chem Soc 105, 810-815.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Salah El Din, A.L.M., Braun, V. & Abdallah, M.A. Synthesis and activity of p-azidobenzoyloxyferricrocin, a photoactivatable analog of ferrichrome. Biometals 12, 151–160 (1999). https://doi.org/10.1023/A:1009225811420
Issue Date:
DOI: https://doi.org/10.1023/A:1009225811420