Corpus ID: 22295171

Preferential binding of copper to the beta domain of metallothionein.

@article{Nielson1984PreferentialBO,
  title={Preferential binding of copper to the beta domain of metallothionein.},
  author={K. B. Nielson and D. Winge},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 8},
  pages={
          4941-6
        }
}
  • K. B. Nielson, D. Winge
  • Published 1984
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • Proteolytic studies of rat liver metallothionein reconstituted in vitro with Cu salts revealed that the 2 metal centers fill in an ordered fashion. The B cluster in the NH2-terminal beta domain fills prior to Cu binding in cluster A. This is in contradistinction to cluster formation induced by the binding of Cd or Zn ions in which cluster A is the center of initial binding. The formation of metal cluster B by Cu occurs in a cooperative fashion yielding a saturated cluster with approximately 6… CONTINUE READING
    107 Citations

    Figures, Tables, and Topics from this paper.

    Explore Further: Topics Discussed in This Paper

    Cooperative cluster formation in metallothionein.
    • J. Byrd, D. Winge
    • Chemistry, Medicine
    • Archives of biochemistry and biophysics
    • 1986
    • 17
    X-ray absorption studies of the copper-beta domain of rat liver metallothionein.
    • 27
    • PDF
    Cu+ distribution in metallothionein fragments.
    • 34
    Sequence and antigenicity of calf metallothionein II.
    • 5

    References

    Metal Ions in Biological Systems (Sigel, H., ed
    • 1983