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Issue 5, 2014
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Supramolecular catalysis. Part 2: artificial enzyme mimics

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Abstract

The design of artificial catalysts able to compete with the catalytic proficiency of enzymes is an intense subject of research. Non-covalent interactions are thought to be involved in several properties of enzymatic catalysis, notably (i) the confinement of the substrates and the active site within a catalytic pocket, (ii) the creation of a hydrophobic pocket in water, (iii) self-replication properties and (iv) allosteric properties. The origins of the enhanced rates and high catalytic selectivities associated with these properties are still a matter of debate. Stabilisation of the transition state and favourable conformations of the active site and the product(s) are probably part of the answer. We present here artificial catalysts and biomacromolecule hybrid catalysts which constitute good models towards the development of truly competitive artificial enzymes.

Graphical abstract: Supramolecular catalysis. Part 2: artificial enzyme mimics

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Publication details

The article was received on 31 Jan 2013 and first published on 23 Dec 2013


Article type: Review Article
DOI: 10.1039/C3CS60037H
Chem. Soc. Rev., 2014,43, 1734-1787

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    Supramolecular catalysis. Part 2: artificial enzyme mimics

    M. Raynal, P. Ballester, A. Vidal-Ferran and P. W. N. M. van Leeuwen, Chem. Soc. Rev., 2014, 43, 1734
    DOI: 10.1039/C3CS60037H

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