Kamer, P.C.J.; Laan, W.

ChemCatChem 2013, 5, 1184-1191, 10.1002/cctc.201200671

The development of artificial copper enzymes from sterol carrier protein type 2 like domain (SCP‐2L) for the use in asymmetric catalysis was explored. For this purpose, proteins were modified with various nitrogen donor ligands. Maleimide‐containing ligands were found most suitable for selective cysteine bio‐conjugation. Fluorescence spectroscopy was used to confirm copper binding to an introduced phenanthroline ligand, which was introduced in two unique cysteine containing SCP‐2L mutants. Copper adducts of several modified SCP‐2L templates were applied in asymmetric Diels–Alder reactions. A clear influence of both the protein environment and the introduced ligand was found in the asymmetric Diels–Alder reaction between azachalcone and cyclopentadiene. A promising enantioselectivity of 25 % ee was obtained by using SCP‐2L V83C modified with phenanthroline–maleimide ligand. Good endo selectivity was observed for SCP‐2L modified with the dipicolylamine‐based nitrogen donor ligand. These artificial metalloenzymes provide a suitable starting point for the implementation of various available techniques to optimise the performance of this system.

Kamer, P.C.J.; Laan, W.

Chem. - Eur. J. 2011, 17, 4680-4698, 10.1002/chem.201003646

Many bioinspired transition‐metal catalysts have been developed over the recent years. In this review the progress in the design and application of ligand systems based on peptides and DNA and the development of artificial metalloenzymes are reviewed with a particular emphasis on the combination of phosphane ligands with powerful molecular recognition and shape selectivity of biomolecules. The various approaches for the assembly of these catalytic systems will be highlighted, and the possibilities that the use of the building blocks of Nature provide for catalyst optimisation strategies are discussed.

Kamer, P.C.J.; Laan, W.

Dalton Trans. 2010, 39, 8477, 10.1039/c0dt00239a

The preparation of hybrid transition metalloproteins by thiol-selective incorporation of organometallic rhodium- and ruthenium complexes is described. Phosphine ligands and two rhodium-diphosphine complexes bearing a carboxylic acid group were coupled to the cysteine of PYP R52G, yielding a metalloenzyme active in the rhodium catalyzed hydrogenation of dimethyl itaconate. The successful coupling was shown by 31P NMR spectroscopy and ESI mass spectroscopy. In addition wild-type PYP (PYP WT), PYP R52G and ALBP were successfully modified with a (η6-arene) ruthenium(II) phenanthroline complex via a maleimide linker.