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Updated: Jun 4, 2026

Assessing Iron Deposition in the Brains of 5xFAD Mice by Perls'/DAB Staining
Published on: May 23, 2025
Iron chaperones for mitochondrial Fe-S cluster biosynthesis and ferritin iron storage
Poorna Subramanian1, Andria V Rodrigues, Sudipa Ghimire-Rijal
1Department of Biochemistry and Molecular Biology, Wayne State University, 540 E. Canfield Ave., Detroit, MI 48201, USA.
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.
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