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Biochem. Biophys. Res. Commun. · Mar 2004
Effect on ribonucleotide reductase of novel lipophilic iron chelators: the desferri-exochelins.
- Yvonne K Hodges, William E Antholine, and Lawrence D Horwitz.
- University of Colorado, Health Sciences Center, Department of Medicine, Division of Cardiology, Box B130, 4200 E. 9th Ave., Denver, CO 80262, USA. yvonne.hodges@uchsc.edu
- Biochem. Biophys. Res. Commun. 2004 Mar 12; 315 (3): 595-8.
AbstractDesferri-exochelins are siderophores secreted by Mycobacterium tuberculosis that are both lipid- and water-soluble and have a high binding affinity for iron. Desferri-exochelin 772SM inhibits DNA replication and ribonucleotide reductase activity at 10-fold less concentration than the lipid-insoluble iron chelator deferoxamine, which is currently in clinical use. Neither chelator can extract iron directly from ribonucleotide reductase. However, because of its lipid-solubility and high binding affinity, desferri-exochelin is able to enter cells rapidly and access intracellular iron, while deferoxamine has limited capacity to cross the cell membrane.
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