An original concept called “Artificial metalloenzymes” has recently emerged at the border between organometallic and enzymatic catalysis, in which biomacromolecules (proteins, DNA) act as hosts to metallic species (ions, coordination or organometallic complexes) affording new hybrid catalysts with unprecedented reactivities. At the laboratory, several half-sandwich complexes of Ru(II) et de Rh(III) including various diimine ligands and a specific chemical function allowing their covalent anchoring to cysteine 25 of papain chosen as protein host. Modified papain acquires Diels-Alderase, formate dehydrogenase or transfer hydrogenase activities according to the metallic cofactor introduced within the protein scaffold.
- B. Talbi, P. Haquette, A. Martel, F. de Montigny, C. Fosse, S. Cordier, T. Roisnel, G. Jaouen, and M. Salmain. (2010) (η6-arene) ruthenium(II) complexes and metallo-papain hybrid as Lewis acid catalysts of Diels-Alder reaction in water, Dalton Trans. 39, 5605-5607.
- P. Haquette, B. Talbi, L. Barilleau, N. Madern, C. Fosse, and M. Salmain. (2011) Chemically engineered papain as artificial formate dehydrogenase for NAD(P)H regeneration, Org. Biomol. Chem. 9, 5720 - 5727.
- A. Chevalley, and M. Salmain. (2012) Enantioselective transfer hydrogenation of ketone catalysed by artificial metalloenzymes derived from bovine b-lactoglobulin, Chem. Commun. 48, 11984-11986.