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- W1522380248 abstract "Abstract Metalloenzymes are natural catalysts that carry out various types of reactions including hydrolytic, redox, and others, with impressive turnovers and exquisite selectivity. To achieve this goal, they gather a metal active site and a well‐defined supramolecular environment generated by the protein folding that allows specific spatial preorganization of the substrate and thus high reaction kinetics and selectivities. Traditional chemical models of metalloenzymes (classical coordination complexes), despite being a source of valuable data, miss this fundamental supramolecular aspect. Over the last 30 years, chemists have thus developed several supramolecular strategies to refine them, through the use of molecular receptors or mesoporous matrices to mimic the binding pocket of the enzyme. This field is still in its infancy, but several behaviors observed in natural systems were evidenced by these synthetic supramolecular systems. Each results from supramolecular strategies based on the control of metal site nuclearity, metal/substrate interaction, and the interlocking of host–guest and metal properties. These various approaches constitute tools for the development of new generations of biomimetic coordination systems." @default.
- W1522380248 created "2016-06-24" @default.
- W1522380248 creator A5030326797 @default.
- W1522380248 creator A5067876079 @default.
- W1522380248 date "2012-01-27" @default.
- W1522380248 modified "2023-10-13" @default.
- W1522380248 title "Supramolecular Bioinorganic Chemistry" @default.
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