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Iron chaperones for mitochondrial Fe-S cluster biosynthesis and ferritin iron storage.

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.

SUBMITTER: Subramanian P

PROVIDER: S-EPMC3366118 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Iron chaperones for mitochondrial Fe-S cluster biosynthesis and ferritin iron storage.

Subramanian Poorna P Rodrigues Andria V AV Ghimire-Rijal Sudipa S Stemmler Timothy L TL

Current opinion in chemical biology 20110131 2

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 structure ...[more]

PMID: 21288761

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