Ni-S(uper)O(xide)D(ismutase) Inspired Ni(II)-Amino Acid Complexes Covalently Grafted onto Merrifield’s Resin - Synthesis, Structure and Catalytic Activity
In this work the syntheses of covalently grafted Ni(II)-complexes formed with various N- or C-protected amino acid ligands (L-histidine, L-tyrosine, L-cysteine and L-cystine) inspired by the active site of the Ni-SOD enzyme are presented. Merrifield’s resin was used as support to mimic the proteomic skeleton of the enzyme. Conditions of the syntheses were altered and the structural features of the substances obtained were studied by infrared spectroscopy. It was found that the preparation of covalently anchored Ni(II)−amino acid complexes was successful in all cases. In many cases the structures of the anchored complexes and the coordinating groups substantially varied upon changing the conditions of the syntheses. The obtained materials were studied by energy dispersive X-ray fluorescence coupled to scanning electron microscope (SEM−EDX). All the covalently anchored materials displayed superoxide dismutase (SOD) activity and some proved to be exceptionally efficient in the biochemical test reaction.
Ana Maria Pires Pinto and António Sérgio Pouzada
Z. Csendes et al., "Ni-S(uper)O(xide)D(ismutase) Inspired Ni(II)-Amino Acid Complexes Covalently Grafted onto Merrifield’s Resin - Synthesis, Structure and Catalytic Activity", Materials Science Forum, Vols. 730-732, pp. 1012-1017, 2013