3 publications

3 publications

An Artificial Enzyme Made by Covalent Grafting of an FeII Complex into β-Lactoglobulin: Molecular Chemistry, Oxidation Catalysis, and Reaction-Intermediate Monitoring in a Protein

Banse, F.; Mahy, J.-P.

Chem. - Eur. J. 2015, 21, 12188-12193, 10.1002/chem.201501755

An artificial metalloenzyme based on the covalent grafting of a nonheme FeII polyazadentate complex into bovine β‐lactoglobulin has been prepared and characterized by using various spectroscopic techniques. Attachment of the FeII catalyst to the protein scaffold is shown to occur specifically at Cys121. In addition, spectrophotometric titration with cyanide ions based on the spin‐state conversion of the initial high spin (S=2) FeII complex into a low spin (S=0) one allows qualitative and quantitative characterization of the metal center’s first coordination sphere. This biohybrid catalyst activates hydrogen peroxide to oxidize thioanisole into phenylmethylsulfoxide as the sole product with an enantiomeric excess of up to 20 %. Investigation of the reaction between the biohybrid system and H2O2 reveals the generation of a high spin (S=5/2) FeIII(η2‐O2) intermediate, which is proposed to be responsible for the catalytic sulfoxidation of the substrate.


Metal: Fe
Ligand type: Poly-pyridine
Host protein: ß-lactoglobulin
Anchoring strategy: Covalent
Optimization: ---
Reaction: Sulfoxidation
Max TON: 5.6
ee: 20
PDB: ---
Notes: ---

Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin for the Asymmetric Transfer Hydrogenation of an Aryl Ketone – Synthesis, Characterization and Catalytic Activity

Salmain, M.

Dalton Trans. 2014, 43, 5482-5489, 10.1039/c3dt53253d

Protein hybrids resulting from the supramolecular anchoring to bovine β-lactoglobulin of fatty acid-derived Rh(iii) diimine complexes catalysed the asymmetric transfer hydrogenation of trifluoroacetophenone with up to 32% ee.


Metal: Rh
Ligand type: Cp*; Poly-pyridine
Host protein: ß-lactoglobulin
Anchoring strategy: Supramolecular
Optimization: Chemical
Reaction: Hydrogenation
Max TON: 14
ee: 32
PDB: ---
Notes: ---

Enantioselective Transfer Hydrogenation of Ketone Catalysed by Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin

Salmain, M.

Chem. Commun. 2012, 48, 11984, 10.1039/c2cc36980j

Artificial metalloproteins resulting from the embedding of half-sandwich Ru(II)/Rh(III) fatty acid derivatives within β-lactoglobulin catalysed the asymmetric transfer hydrogenation of trifluoroacetophenone with modest to good conversions and fair ee's.


Metal: Rh
Ligand type: Cp*; Poly-pyridine
Host protein: ß-lactoglobulin
Anchoring strategy: Supramolecular
Optimization: Chemical
Reaction: Hydrogenation
Max TON: 34
ee: 26
PDB: ---
Notes: ---