title: Human frataxin: iron and ferrochelatase binding surface.
abstract: The coordinated iron structure and ferrochelatase binding surface of human frataxin have been characterized to provide insight into the protein's ability to serve as the iron chaperone during heme biosynthesis.
authors.affiliation: Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, MI 49201, USA. tstemmle@med.wayne.edu
authors.forename: Krisztina Z
authors.initials: KZ
authors.lastname: Bencze
authors.forename: Taejin
authors.initials: T
authors.lastname: Yoon
authors.forename: César
authors.initials: C
authors.lastname: Millán-Pacheco
authors.forename: Patrick B
authors.initials: PB
authors.lastname: Bradley
authors.forename: Nina
authors.initials: N
authors.lastname: Pastor
authors.forename: J A
authors.initials: JA
authors.lastname: Cowan
authors.forename: Timothy L
authors.initials: TL
authors.lastname: Stemmler
mesh_terms: D018360:Crystallography, X-Ray; D005294:Ferrochelatase / Q000378:metabolism*; D006418:Heme / Q000096:biosynthesis; D006801:Humans; D007501:Iron / Q000378:metabolism*; D033862:Iron-Binding Proteins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D018832:Molecular Chaperones / Q000378:metabolism; D013499:Surface Properties; D000096923:Frataxin
chemical_list: D005294:Ferrochelatase; D006418:Heme; D007501:Iron; D033862:Iron-Binding Proteins; D018832:Molecular Chaperones; D000096923:Frataxin