An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo.

@article{Emerson2003AnET,
  title={An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo.},
  author={Joseph P Emerson and Diane E. Cabelli and Donald M Kurtz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 7},
  pages={3802-7}
}
Superoxide reductases (SORs) contain a characteristic square-pyramidal [Fe(NHis)(4)(SCys)] active site that catalyzes reduction of superoxide to hydrogen peroxide in several anaerobic bacteria and archaea. Some SORs, referred to as two-iron SORs (2Fe-SORs), also contain a lower-potential [Fe(SCys)(4)] site that is presumed to have an electron transfer function. However, the intra- and inter-subunit distances between [Fe(SCys)(4)] and [Fe(NHis)(4)(SCys)] iron centers within the 2Fe-SOR homodimer… CONTINUE READING