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

Csendes, Zita; Varga, Gabor; Schmehl, Hajnal; Timar, Zita; Carlson, Stefan LU ; Canton, Sophie LU ; Bajnoczi, Eva G.; Sebok, Daniel; Dekany, Imre and Elek, Gabor, et al. (2014) In Journal of Molecular Catalysis A: Chemical 395. p.93-99
Abstract
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... (More)
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. (Less)
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published
subject
keywords
Biomimetic catalysis, Silica immobilised Ni(II)-complexes, XAS, Catalytic activities
in
Journal of Molecular Catalysis A: Chemical
volume
395
pages
93 - 99
publisher
Elsevier
external identifiers
  • wos:000347498500012
  • scopus:84906538887
ISSN
1381-1169
DOI
10.1016/j.molcata.2014.07.033
language
English
LU publication?
yes
id
bef240e1-a92f-481a-9564-39326af8f923 (old id 5070111)
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2015-02-25 16:21:50
date last changed
2017-01-01 06:32:52
@article{bef240e1-a92f-481a-9564-39326af8f923,
  abstract     = {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.},
  author       = {Csendes, Zita and Varga, Gabor and Schmehl, Hajnal and Timar, Zita and Carlson, Stefan and Canton, Sophie and Bajnoczi, Eva G. and Sebok, Daniel and Dekany, Imre and Elek, Gabor and Sipos, Pal and Palinko, Istvan},
  issn         = {1381-1169},
  keyword      = {Biomimetic catalysis,Silica immobilised Ni(II)-complexes,XAS,Catalytic activities},
  language     = {eng},
  pages        = {93--99},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Catalysis A: Chemical},
  title        = {Superoxide dismutase inspired immobilised Ni(II)-protected amino acid catalysts Synthesis, characterisation, and catalytic activity},
  url          = {http://dx.doi.org/10.1016/j.molcata.2014.07.033},
  volume       = {395},
  year         = {2014},
}