The ability of the NiSOD binding loop to chelate zinc(ii): The role of the terminal amino group in the enzymatic functions
| Autor: | Tamás Gajda, Imre Sóvágó, Norbert Lihi, Giuseppe Pappalardo, Katalin Várnagy, András Kolozsi, Gizella Csire, István Fábián |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Stereochemistry
chemistry.chemical_element Peptide Zinc metal complexes 010402 general chemistry Ligands 01 natural sciences Inorganic Chemistry Deprotonation Coordination Complexes Nickel Side chain Chelation Amino Acid Sequence Binding site Amines Amino Acids Peptide sequence Chelating Agents chemistry.chemical_classification Binding Sites Molecular Structure 010405 organic chemistry Hydrogen-Ion Concentration 0104 chemical sciences stability constants chemistry peptides Thermodynamics Protein Binding |
| Zdroj: | Dalton transactions (2003. Print) 48 (2019): 6217–6227. doi:10.1039/c9dt01015g info:cnr-pdr/source/autori:Csire G.; Kolozsi A.; Gajda T.; Pappalardo G.; Varnagy K.; Sovago I.; Fabian I.; Lihi N./titolo:The ability of the NiSOD binding loop to chelate zinc(ii): The role of the terminal amino group in the enzymatic functions/doi:10.1039%2Fc9dt01015g/rivista:Dalton transactions (2003. Print)/anno:2019/pagina_da:6217/pagina_a:6227/intervallo_pagine:6217–6227/volume:48 |
| DOI: | 10.1039/c9dt01015g |
| Popis: | 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 of L1 (HCDLPCGVY-NH2), L2 (Ac-HCDLPCGVY-NH2) and L3 (HCDLACGVY-NH2) and the nickel(ii) and zinc(ii) complexes of L4 (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. L2 complexes 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. |
| Databáze: | OpenAIRE |
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