Bajnóczi, Eva
- University of Szeged
Research article2014Peer reviewed
Csendes, Zita; Varga, Gabor; Schmehl, Hajnal; Timar, Zita; Carlson, Stefan; Canton, Sophie E.; Bajnoczi, Eva G.; Sebok, Daniel; Dekany, Imre; Elek, Gabor; Sipos, Pal; Palinko, Istvan
Covalently anchored Ni(II)-C-protected amino acid (L-histidine, L-cysteine, and L-cystine) complexes inspired by the active site of the Ni-superoxide dismutase enzyme were synthesised using chloropropylated silica gel as support. The structural features of the surface complexes were studied by the Kjeldahl method and ICP-MS, mid/far IR, UV-vis diffuse reflectance, and X-ray absorption spectroscopies. The enzyme-like activities of the materials were determined in a biochemical test reaction. Covalent grafting and building the complex onto the surface of the support were successful in all cases. It was found that in many instances the structures obtained and the coordinating groups substantially varied upon changing the conditions of the syntheses. All the covalently immobilised Ni(II)-complexes displayed enzyme-like activity. They also were active in the liquid-phase oxidation of cyclohexene, providing the epoxide with high selectivity. (C) 2014 Elsevier B.V. All rights reserved.
Biomimetic catalysis; Silica immobilised Ni(II)-complexes; XAS; Catalytic activities
Journal of Molecular Catalysis A: Chemical
2014, volume: 395, pages: 93-99
Publisher: ELSEVIER SCIENCE BV
Inorganic Chemistry
https://res.slu.se/id/publ/85898