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The ability of the NiSOD binding loop to chelate zinc(ii): the role of the terminal amino group in the enzymatic functions

Csire, Gizella

Dalton transactions: an international journal of inorganic chemistry. Volume 48:Issue 18 (2019); pp 6217-6227 -- Royal Society of Chemistry

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  • Title:
    The ability of the NiSOD binding loop to chelate zinc(ii): the role of the terminal amino group in the enzymatic functions
  • Author: Csire, Gizella;
    Kolozsi, András;
    Gajda, Tamás;
    Pappalardo, Giuseppe;
    Várnagy, Katalin;
    Sóvágó, Imre;
    Fábián, István;
    Lihi, Norbert
  • Found In: Dalton transactions: an international journal of inorganic chemistry. Volume 48:Issue 18 (2019); pp 6217-6227
  • Journal Title: Dalton transactions: an international journal of inorganic chemistry
  • Subjects: Chemistry, Inorganic--Periodicals; Chemistry, Physical and theoretical--Periodicals; Dewey: 546.05
  • Rights: legaldeposit
  • Publication Details: Royal Society of Chemistry
  • Abstract: Abstract :

    Equilibrium and spectroscopic characterization of zinc(ii) complexes with NiSOD related peptides highlights the crucial role of terminal amino groups in the enzymatic function.

    Abstract :

    Equilibrium and detailed spectroscopic characterization of zinc(ii) complexes with NiSOD binding loop and their related model fragments are reported in the whole investigated pH-range. The zinc(ii) complexes ofL1(HCDLPCGVY-NH2), L2(Ac-HCDLPCGVY-NH2) andL3(HCDLACGVY-NH2) and the nickel(ii) and zinc(ii) complexes ofL4(HCDLPCG-NH2) were studied by pH-potentiometric and several spectroscopic methods. The results indicated that the macrochelate coordinated zinc(ii) complexes are dominant in a whole pH-range and the side chain donors of the peptides are involved in the metal binding. Therefore, the deprotonation and coordination of the peptide backbone occur only in a strongly alkaline solution. The acetylation of the peptide amino terminus (L2) significantly enhances the zinc(ii) binding ability compared to the corresponding nickel(ii) complexes.L2complexes of zinc(ii) are 2 or 3 orders of magnitude more stable than the corresponding nickel(ii) complexes. This effect clearly shows the crucial role of the terminal amino group in the nickel binding for the NiSOD enzyme.


  • Identifier: System Number: LDEAvdc_100083805238.0x000001; Journal ISSN: 1477-9226; 10.1039/c9dt01015g
  • Publication Date: 2019
  • Physical Description: Electronic
  • Shelfmark(s): ELD Digital store

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