Bio-inspired manipulation of catalytic sites via immobilization of metal ion complexes in zeolites
By careful selection of the appropriate preparation parameters we show how it is possible to immobilize transition metal ion complexes within the supercages of zeolite Y to create molecular species, which mimic the active sites of enzymes and their catalytic function. In particular, we demonstrate the use of 3,3-bis(1-methylimidazol-2-yl)propionate (MIm2Pr) combined with Cu2+ to imitate enzyme actives sites based on the 2-His-1-carboxylate facial triad motif and the use of histidine moieties (His) to replicate the active site of galactose oxidase. Characterization of these active site mimics using a variety of advanced spectroscopic techniques, has also been performed in order to understand why they possess this improved catalytic activity.
A. M. Beale J. G. Mesu K. Kervinen T. Visser F. Soulimani P. C. A. Bruijnincx R. J. M. Klein Gebbink G. van Koten B. M. Weckhuysen
Inorganic Chemistry and Catalysis, Department of Chemistry, Utrecht University,Sorbonnelaan 16, 3584 Organic Chemistry and Catalysis, Department of Chemistry, Utrecht University, Padualaan 8,3584 CA Ut
国际会议
北京
英文
2007-08-12（万方平台首次上网日期，不代表论文的发表时间）