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Interaction of copper(I) with nucleic acids.

W A Prütz1, J Butler, E J Land

  • 1Institut für Biophysik und Strahlenbiologie, Universität Freiburg, FRG.

International Journal of Radiation Biology
|August 1, 1990
PubMed
Summary

Copper(I) readily binds to DNA and poly(I), forming stable complexes. This binding influences DNA stability and reactivity, particularly in the presence of hydrogen peroxide, and can affect enzyme activity.

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Area of Science:

  • Biophysical Chemistry
  • Molecular Biology
  • Radiochemistry

Background:

  • Copper(I) ions (Cu(I)) are known to interact with nucleic acids.
  • The stability and reactivity of DNA-Cu(I) complexes are not fully understood.
  • Understanding these interactions is crucial for comprehending DNA damage and repair mechanisms.

Purpose of the Study:

  • To investigate the complex formation between Cu(I) and various nucleic acids, including DNA and synthetic polynucleotides.
  • To quantify the kinetics and thermodynamics of Cu(I) binding to DNA.
  • To elucidate the role of Cu(I)-DNA complexes in DNA degradation and their influence on enzyme activity.

Main Methods:

  • Pulse radiolysis was employed to generate Cu(I) ions.
  • UV-Vis spectroscopy was used to monitor complex formation and absorbance changes.
  • Kinetic studies measured association and dissociation rates, and stability constants were calculated.

Main Results:

  • Poly(dG-dC) and poly(I) form highly stable Cu(I) complexes.
  • A significant rate constant for Cu(I) association with native DNA was determined (~4 x 10^7 dm3 mol-1 s-1).
  • Cu(I)-DNA complexes are susceptible to degradation by hydrogen peroxide, with enhanced damage observed for specific DNA models.
  • DNA and poly(I) can inhibit copper-zinc superoxide dismutase (SOD) activity by complexing Cu(I).

Conclusions:

  • Cu(I) forms stable complexes with DNA, influencing its structural integrity and reactivity.
  • The DNA-Cu(I) complex is prone to oxidative damage mediated by hydrogen peroxide.
  • Nucleic acids can modulate copper-dependent enzyme activity through competitive Cu(I) binding.

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