Iron-sulfur cluster biosynthesis: functional characterization of the N- and C-terminal domains of human NFU.

@article{Liu2009IronsulfurCB,
  title={Iron-sulfur cluster biosynthesis: functional characterization of the N- and C-terminal domains of human NFU.},
  author={Yushi Liu and Wenbin Qi and James Allan Cowan},
  journal={Biochemistry},
  year={2009},
  volume={48 5},
  pages={973-80}
}
Human NFU (also known as HIRIP5) has been implicated in cellular iron-sulfur cluster biosynthesis. Bacterial and yeast forms are smaller than the human protein and are homologous to the C-terminal domain of the latter. This C-terminal domain contains a pair of redox active cysteines and demonstrates thioredoxin-like activity by mediating persulfide bond cleavage of sulfur-loaded NifS (an IscS-type protein), the sulfide donor for [2Fe-2S] cluster assembly on ISU-type scaffold proteins. Herein… CONTINUE READING