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Development of late transition metalloenzymes for highly efficient catalytic processes.

Objective

Waste-free chemical processes are a must for a sustainable society. In nature, enzymes enable the atom economic synthesis of numerous natural products. Unfortunately, nature does not provide enzymes for the synthesis of the many pharmaceuticals, agrochemi cals and fine-chemicals that are needed. To solve this problem, our interdisciplinary scientific team wants to establish a paradigm shift in catalysis research by developing "artificial enzymes" containing transition metals that nature has not acquired for the production of important products.We propose a demanding new interdisciplinary approach for a 'de novo' design of metalloenzymes. Molecular recognition properties of proteins will be exploited by incorporation of metals such as rhodium, nickel and pall adium via amino acids containing phosphino ligands. Two types of artificial enzymes are targeted, namely those with mononuclear transition metals and those with transition metal nanoclusters that are stabilised by phosphine modified peptides, enabling effi cient cascade reactions. The design process is to be aided by molecular modeling and by structure determination using NMR and X-ray crystallography.By ligating small phosphino functionalised oligopeptides with proteins, we will create a new class of highly selective catalysts for reactions that nature can not perform, such as CO insertion, alkene insertion and (asymmetric) C-C coupling reactions. The catalytic performance and stability of these artizymes will be optimised by adjusting the amino acid sequenc e and the ligand structure. The protein part will induce the proper substrate orientation to the metal centre. Encapsulating substrates by these "synthetic proteins" will ultimately enable clean conversion of unfunctionalised molecules by C-H activation.Th ese catalysts will exhibit substrate specificity, i.e. they will be able to pick out a single substrate, even when it is present at low concentrations in complex mixtures.

Call for proposal

FP6-2003-NEST-B-3
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Funding Scheme

STREP - Specific Targeted Research Project

Coordinator

THE UNIVERSITY COURT OF THE UNIVERSITY OF ST. ANDREWS
Address
College Gate, North Street
St Andrews
United Kingdom

Participants (6)

CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE
France
Address
Rue Michel-ange, 3
Paris
JUSTUS-LIEBIG-UNIVERSITAT GIESSEN
Germany
Address
Ludwigstrasse 23
Giessen
UNIVERSIDADE DE SANTIAGO DE COMPOSTELA
Spain
Address
Pazo De San Xerome - Plaza Do Obradoiro, S/n
Santiago De Compostela
UNIVERSITEIT LEIDEN
Netherlands
Address
Rapenburg 70
Leiden
UNIVERSITEIT VAN AMSTERDAM
Netherlands
Address
Spui 21
Amsterdam
VERENIGING VOOR CHRISTELIJK HOGER ONDERWIJS, WETENSCHAPPELIJK ONDERZOEK EN PATIENTENZORG
Netherlands
Address
De Boelelaan 1105
Amsterdam