| Literature DB >> 21288761 |
Poorna Subramanian1, Andria V Rodrigues, Sudipa Ghimire-Rijal, Timothy L Stemmler.
Abstract
Protein controlled iron homeostasis is essential for maintaining appropriate levels and availability of metal within cells. Recently, two iron chaperones have been discovered that direct metal within two unique pathways: (1) mitochondrial iron-sulfur (Fe-S) cluster assembly and (2) within the ferritin iron storage system. Although structural and functional details describing how these iron chaperones operate are emerging, both share similar iron binding affinities and metal-ligand site structures that enable them to bind and release Fe2+ to specific protein partners. Molecular details related to iron binding and delivery by these chaperones will be explored within this review.Entities:
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Year: 2011 PMID： 21288761 PMCID： PMC3366118 DOI： 10.1016/j.cbpa.2011.01.003
Source DB: PubMed Journal: Curr Opin Chem Biol ISSN： 1367-5931 Impact factor: 8.822