Abstract
Copper(II) complexes of five peptide ligands containing at least three histidine residues have been tested as catalysts in catechol oxidation and superoxide dismutation. All systems exhibit considerable catechol oxidase-like activity, and the Michaelis–Menten enzyme kinetic model is applicable in all cases. Beside the Michaelis–Menten parameters, the effects of pH, catalyst and dioxygen concentration on the reaction rates are also reported. Considering the rather different sequences, the observed oxidase activity seems to be a general behavior of copper(II) complexes with multihistidine peptides. Interestingly, in all cases {Nim/2Nim,2N−} coordinated complexes are the pre-active species, the bound amide nitrogens were proposed to be an acid/base site for facilitating substrate binding. The studied copper(II)-peptide complexes are also able to effectively dismutate superoxide radical in the neutral pH range.
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Funding
This research was supported by National Research, Development and Innovation Office-NKFIH (Hungary) through projects GINOP-2.3.2-15-2016-00038, OTKA 101541 and TÉT_15-1-2016-0031.
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Dávid Árus—deceased September 28, 2015.
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Dancs, Á., Selmeczi, K., Árus, D. et al. Catechol Oxidase and SOD Mimicking by Copper(II) Complexes of Multihistidine Peptides. Int J Pept Res Ther 24, 571–575 (2018). https://doi.org/10.1007/s10989-017-9645-x
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DOI: https://doi.org/10.1007/s10989-017-9645-x