| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10564892 | Current Opinion in Chemical Biology | 2011 | 7 Pages |
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Chemistry (General)
Authors
Poorna Subramanian, Andria V Rodrigues, Sudipa Ghimire-Rijal, Timothy L Stemmler,