Cobalt(2+) binding to human and tomato copper chaperone for superoxide dismutase: implications for the metal ion transfer mechanism.

@article{Zhu2000Cobalt2BT,
  title={Cobalt(2+) binding to human and tomato copper chaperone for superoxide dismutase: implications for the metal ion transfer mechanism.},
  author={Hui Zhu and Elizabeth A Shipp and Raylene J. Sanchez and Amir Liba and Jeffrey Emmett Stine and P John Hart and Edith Butler Gralla and Aram M. Nersissian and Joan Selverstone Valentine},
  journal={Biochemistry},
  year={2000},
  volume={39 18},
  pages={
          5413-21
        }
}
The copper chaperone for superoxide dismutase (CCS) gene encodes a protein that is believed to deliver copper ions specifically to copper-zinc superoxide dismutase (CuZnSOD). CCS proteins from different organisms share high sequence homology and consist of three distinct domains; a CuZnSOD-like central domain 2 flanked by domains 1 and 3, which contain putative metal-binding motifs. We report deduced protein sequences from tomato and Arabidopsis, the first functional homologues of CCS… CONTINUE READING
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