Cargando…
Human Frataxin Activates Fe–S Cluster Biosynthesis by Facilitating Sulfur Transfer Chemistry
[Image: see text] Iron–sulfur clusters are ubiquitous protein cofactors with critical cellular functions. The mitochondrial Fe–S assembly complex, which consists of the cysteine desulfurase NFS1 and its accessory protein (ISD11), the Fe–S assembly protein (ISCU2), and frataxin (FXN), converts substr...
Autores principales: | Bridwell-Rabb, Jennifer, Fox, Nicholas G., Tsai, Chi-Lin, Winn, Andrew M., Barondeau, David P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4215901/ https://www.ncbi.nlm.nih.gov/pubmed/24971490 http://dx.doi.org/10.1021/bi500532e |
Ejemplares similares
-
Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin
por: Gervason, Sylvain, et al.
Publicado: (2019) -
In vivo overexpression of frataxin causes toxicity mediated by iron-sulfur cluster deficiency
por: Huichalaf, Claudia, et al.
Publicado: (2022) -
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism
por: Fox, Nicholas G., et al.
Publicado: (2019) -
Mitochondrial Fe-S cluster biogenesis, frataxin and the modulation of susceptibility to drug-induced cardiomyopathy
por: Sack, Michael N.
Publicado: (2010) -
Molecular Details of the Frataxin–Scaffold Interaction during Mitochondrial Fe–S Cluster Assembly
por: Campbell, Courtney J., et al.
Publicado: (2021)