Conserved residues modulate copper release in human copper chaperone Atox1.

@article{Hussain2008ConservedRM,
  title={Conserved residues modulate copper release in human copper chaperone Atox1.},
  author={Faiza Hussain and John S Olson and Pernilla Wittung-Stafshede},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 32},
  pages={11158-63}
}
It is unclear how the human copper (Cu) chaperone Atox1 delivers Cu to metal-binding domains of Wilson and Menkes disease proteins in the cytoplasm. To begin to address this problem, we have characterized Cu(I) release from wild-type Atox1 and two point mutants (Met(10)Ala and Lys(60)Ala). The dynamics of Cu(I) displacement from holo-Atox1 were measured by using the Cu(I) chelator bicinchonic acid (BCA) as a metal acceptor. BCA removes Cu(I) from Atox1 in a three-step process involving the… CONTINUE READING
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