Classical Cys2His2 zinc finger peptides are rapidly oxidized by either H2O2 or O2 irrespective of metal coordination

Seung Jae Lee, Jamie L. Michalek, Angelique N. Besold, Steven E. Rokita, Sarah L.J. Michel

Research output: Contribution to journalArticlepeer-review


ZIF268, a member of the classical zinc finger protein family, contains three Cys2His2 zinc binding domains that together recognize the DNA sequence 5′-AGCGTGGGCGT-3′. These domains can be fused to an endonuclease to make a chimeric protein to target and cleave specific DNA sequences. A peptide corresponding to these domains, named ZIF268-3D, has been prepared to determine if the zinc finger domain itself can promote DNA cleavage when a redox active metal ion, Fe(II), is coordinated. The UV-vis absorption spectrum of Fe(II)-ZIF268-3D is indicative of Fe(II) coordination. Using fluorescence anisotropy, we demonstrate that Fe(II)-ZIF268-3D binds selectively to its target DNA in the same manner as Zn(II)-ZIF268-3D. In the presence of added oxidant, H2O2 or O2, DNA cleavage is not observed by Fe(II)-ZIF268-3D. Instead, the peptide itself is rapidly oxidized. Similarly, Zn(II)-ZIF268-3D and apo-ZIF268-3D are rapidly oxidized by H2O2 or O 2, and we propose that ZIF268-3D is highly susceptible to oxidation.

Original languageEnglish (US)
Pages (from-to)5442-5450
Number of pages9
JournalInorganic Chemistry
Issue number12
StatePublished - Jun 20 2011
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry


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