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Stray Cu(II) may cause oxidative damage when coordinated to the -TESHHK- sequence derived from the C-terminal tail of histone H2A

  1. Author:
    Mylonas, M.
    Malandrinos, G.
    Plakatouras, J.
    Hadjiliadis, N.
    Kasprzak, K. S.
    Krezel, A.
    Bal, W.

  2. Author Address

    Univ Wroclaw, Fac Chem, PL-50383 Wroclaw, Poland. Univ Wroclaw, Fac Chem, PL-50383 Wroclaw, Poland. Univ Ioannina, Dept Chem, GR-45110 Ioannina, Greece. Natl Canc Inst, Comparat Carcinogenesis Lab, Frederick, MD 21702 USA. Polish Acad Sci, Inst Biochem & Biophys, Warsaw, Poland. Bal W Univ Wroclaw, Fac Chem, PL-50383 Wroclaw, Poland.
    1. Year: 2001
  2. Journal: Chemical Research in Toxicology
    1. 14
    2. 9
    3. Pages: 1177-1183
  4. Type of Article: Article
  1. Abstract:

    CH3CO-Thr-Glu-Ser-His-His-Lys-NH2, a hexapeptide representing the 120-125 sequence of histone H2A, coordinates Cu(II) ions efficiently. Monomeric complexes are formed. In the major complex at physiological pH, CuH-1L, Cu(II) is coordinated equatorially through the imidazole nitrogen of the His-4 residue and the amide nitrogens of the Ser-3 and His-4 residues, and axially through the imidazole nitrogen of the His-5 residue. This complex reacts with H2O2 and the resulting reactive oxygen intermediate efficiently oxidizes 2 ' - deoxyguanosine. The underlying mechanism involves the formation of Cu(III) and a metal-bound hydroxyl radical species.

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