Bio-inspired Catalysts [electronic resource] /edited by Thomas R. Ward.
by Ward, Thomas R [editor.]; SpringerLink (Online service).
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Item type | Current location | Call number | Status | Date due | Barcode |
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MAIN LIBRARY | QD410-412.5 (Browse shelf) | Available |
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QA75.5-76.95 Advances in Neural Networks - ISNN 2008 | Uranium, Mining and Hydrogeology | QD410-412.5 Metal Catalysts in Olefin Polymerization | QD410-412.5 Bio-inspired Catalysts | TK5105.5-5105.9 Distributed Computing | TK5105.5-5105.9 Software Technologies for Embedded and Ubiquitous Systems | Q334-342 Logics in Artificial Intelligence |
DNA in Metal Catalysis -- Artificial Metalloproteins Exploiting Vacant Space: Preparation, Structures, and Functions -- Manganese-Substituted ?-Carbonic Anhydrase as an Enantioselective Peroxidase -- Directed Evolution of Stereoselective Hybrid Catalysts -- Artificial Metalloenzymes for Enantioselective Catalysis Based on the Biotin–Avidin Technology.
With the aim of complementing well-established catalytic strategies for enantioselective catalysis, the field of artificial metalloenzymes has attracted increasing interest in the past decade. Artificial metalloenzymes result from the incorporation of a catalytically active organometallic moiety within a macromolecular host. Localization of the competent metal is ensured either by covalent, dative or supramolecular anchoring in either DNA or a protein scaffold. The properties of the resulting hybrid catalysts combine attractive features of both homogeneous and enzymatic catalysis. In particular, the optimization of such systems can be achieved both by chemical and genetic means. The book, consisting of five chapters written by leading experts, critically summarizes the state of the art in enantioselective epoxidation, sulfoxidation, fluorination, hydrogenation, allylic alkylation, Diels-Alder cycloadditions as well as Michael additions catalyzed by artificial metalloenzymes. This timely review unambiguously demonstrates the compatibility and complementarity of organometallic and enzymatic catalysis.
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