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  Superoxide dismutase inspired immobilised Ni(II)-protected amino acid catalysts - Synthesis, characterisation, and catalytic activity.

Csendes, Z., Varga, G., Schmehl, H., Timar, Z., Carlson, S., Canton, S. E., et al. (2014). Superoxide dismutase inspired immobilised Ni(II)-protected amino acid catalysts - Synthesis, characterisation, and catalytic activity. Journal of Molecular Catalysis A: Chemical, 395, 93-99. doi:10.1016/j.molcata.2014.07.033.

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Csendes, Z., Autor
Varga, G., Autor
Schmehl, H., Autor
Timar, Z., Autor
Carlson, S., Autor
Canton, S. E.1, Autor           
Bajnoczi, E. G., Autor
Sebok, D., Autor
Dekany, I., Autor
Elek, G., Autor
Sipos, P., Autor
Palinko, I., Autor
Affiliations:
1Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society, ou_578564              

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Schlagwörter: Biomimetic catalysis; Silica immobilised Ni(II)-complexes; XAS; Catalytic activities
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2014-08-132014-12
 Publikationsstatus: Erschienen
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 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/j.molcata.2014.07.033
 Art des Abschluß: -

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Titel: Journal of Molecular Catalysis A: Chemical
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 395 Artikelnummer: - Start- / Endseite: 93 - 99 Identifikator: -