Bio-inspired catalysts by Ewold W Dijk, Ben L. Feringa, Gerard Roelfes (auth.), Thomas

By Ewold W Dijk, Ben L. Feringa, Gerard Roelfes (auth.), Thomas R. Ward (eds.)

In order to satisfy the ever-increasing calls for for enantiopure compounds, heteroge- ous, homogeneous and enzymatic catalysis advanced independently some time past. even supposing all 3 techniques have yielded industrially attainable approaches, the latter are the main commonly used and will be considered as complementary in lots of respects. regardless of the development in structural, computational and mechanistic reviews, even though, thus far there's no common recipe for the optimization of catalytic techniques. therefore, a trial-and-error method continues to be major in catalyst discovery and optimization. With the purpose of complementing the well-established fields of homogeneous and enzymatic catalysis, organocatalysis and synthetic metalloenzymes have loved a up to date revival. man made metalloenzymes, that are the focal point of this publication, end result from comb- ing an lively yet unselective organometallic moiety with a macromolecular host. Kaiser and Whitesides prompt the opportunity of growing man made metallo- zymes as in the past because the overdue Nineteen Seventies. in spite of the fact that, there has been a common trust that proteins and organometallic catalysts have been incompatible with one another. This significantly hampered examine during this zone on the interface among homogeneous and enzymatic catalysis. because 2000, even if, there was a growing to be curiosity within the box of synthetic metalloenzymes for enantioselective catalysis. the present cutting-edge and the opportunity of destiny improvement are p- sented in 5 well-balanced chapters. G. Roelfes, B. Feringa et al. summarize study hoping on DNA as a macromolecular host for enantioselective catalysis.

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11c). The system in the protein cage architecture can provide a new concept for hydrogen production [64]. Engelkamp et al. have reported the incorporation of horseradish peroxidase in the interior cage of CCMV by using its disassembly/assembly property to elucidate a single molecule study of enzyme behaviors (Fig. 11d). They showed that CCMV permits easy access of substrates and products through the pores of CCMV and that this permeability can be controlled by pH [58]. These results show that protein nanocages are very useful templates for the entrapment of functional materials and provide chemical reaction space.

2 Catalytic Promiscuity: Enantioselective Hydrolysis of Esters hCAII also shows a catalytically promiscuous activity – hydrolysis of activated esters such as P-nitrophenyl acetate (PNPA). The hydrolysis shows low enantioselectivity toward some esters, but high enantioselectivity (E > 100) toward N-acetyl Fig. 1 Structure of the active site of human carbonic anhydrase isozyme II (hCAII) as revealed by X-ray crystallography [30]. Three histidine residues (His119, His94, His96) bind the zinc ion (green ball).

Indeed, the transmission electron microscopic images of RGD-4C Fr containing a magnetite nanoparticle of Fe3O4 show that electron-dense particles corresponding to Fe3O4 were observed on the surface of the C32 melanoma cells (Fig. 11a). These results show how nanoscale protein containers serve to accommodate a variety of functional metal complexes and metal clusters. 3 S. Abe et al. Application to Catalysts Protein nanocages can be used as a catalytic reaction space of metal particles [54, 64]. For example, Ueno et al.

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