Ni(II) specifically cleaves the C-terminal tail of the major variant of histone H2A and forms an oxidative damage-mediating complex with the cleaved-off octapeptide.

@article{Bal2000NiIISC,
  title={Ni(II) specifically cleaves the C-terminal tail of the major variant of histone H2A and forms an oxidative damage-mediating complex with the cleaved-off octapeptide.},
  author={Wojciech Bal and Ruifeng Liang and Jan Lukszo and Seon Hwa Lee and Miral Dizdaroğlu and Kazimierz S. Kasprzak},
  journal={Chemical research in toxicology},
  year={2000},
  volume={13 7},
  pages={616-24}
}
The acetyl-TESHHK-amide peptide, modeling a part of the C-terminal "tail" of histone H2A, was found previously by us to undergo at pH 7. 4 a Ni(II)-assisted hydrolysis of the E-S peptide bond with formation of a stronger Ni(II) complex with the SHHK-amide product [Bal, W., et al. (1998) Chem. Res. Toxicol. 11, 1014-1023]. To further characterize the hydrolysis and test the resulting Ni(II) complex for redox activity, bovine histone H2A and three peptides were investigated: acetyl… CONTINUE READING

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