Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity

@article{Fox2018ZincIIBO,
  title={Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity},
  author={N. Fox and A. Martelli and J. F. Nabhan and J. Janz and O. Borkowska and C. Bulawa and W. Yue},
  journal={Biochimie},
  year={2018},
  volume={152},
  pages={211 - 218}
}
Human de novo iron-sulfur (Fe-S) assembly complex consists of cysteine desulfurase NFS1, accessory protein ISD11, acyl carrier protein ACP, scaffold protein ISCU, and allosteric activator frataxin (FXN). FXN binds the NFS1-ISD11-ACP-ISCU complex (SDAU), to activate the desulfurase activity and Fe-S cluster biosynthesis. In the absence of FXN, the NFS1-ISD11-ACP (SDA) complex was reportedly inhibited by binding of recombinant ISCU. Recent studies also reported a substitution at position Met141… Expand
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