title: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Wayne State University, 540 E. Canfield Ave., Detroit, MI 48201, USA.
authors.forename: Poorna
authors.initials: P
authors.lastname: Subramanian
authors.forename: Andria V
authors.initials: AV
authors.lastname: Rodrigues
authors.forename: Sudipa
authors.initials: S
authors.lastname: Ghimire-Rijal
authors.forename: Timothy L
authors.initials: TL
authors.lastname: Stemmler
mesh_terms: D000818:Animals; D005293:Ferritins / Q000378:metabolism*; D006801:Humans; D007501:Iron / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*
chemical_list: D007506:Iron-Sulfur Proteins; D018832:Molecular Chaperones; D005293:Ferritins; D007501:Iron