DNA hydrolysis and oxidative cleavage by metal-binding peptides tethered to rhodium intercalators.

@article{Copeland2002DNAHA,
  title={DNA hydrolysis and oxidative cleavage by metal-binding peptides tethered to rhodium intercalators.},
  author={Kimberly D Copeland and Marilena P. Fitzsimons and Robert P. Houser and Jacqueline K Barton},
  journal={Biochemistry},
  year={2002},
  volume={41 1},
  pages={343-56}
}
With the goal of developing artificial nucleases for DNA hydrolysis, metal-coordinating peptides have been tethered to a DNA-intercalating rhodium complex to deliver metal ions to the sugar-phosphate backbone. The intercalator, [Rh(phi)(2)bpy']Cl(3) [phi = 9,10-phenanthrenequinone diimine; bpy' = 4-(butyric acid)-4'-methyl-2,2'-bipyridine], provides DNA binding affinity, and a metal-binding peptide contributes reactivity. This strategy for DNA hydrolysis is a general one, and zinc(II)-promoted… CONTINUE READING