Human frataxin: iron and ferrochelatase binding surface.
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.
Bencze
Krisztina Z
KZ
Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, MI 49201, USA. tstemmle@med.wayne.edu
Yoon
Taejin
T
Millán-Pacheco
César
C
Bradley
Patrick B
PB
Pastor
Nina
N
Cowan
J A
JA
Stemmler
Timothy L
TL
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
D005294:Ferrochelatase; D006418:Heme; D007501:Iron; D033862:Iron-Binding Proteins; D018832:Molecular Chaperones; D000096923:Frataxin