A Highly Active Biohybrid Catalyst for Olefin Metathesis in Water: Impact of a Hydrophobic Cavity in a β-Barrel Protein
A series of Grubbs–Hoveyda type catalyst precursors for olefin metathesis containing a maleimide moiety in the backbone of the NHC ligand was covalently incorporated in the cavity of the β-barrel protein nitrobindin. By using two protein mutants with different cavity sizes and choosing the suitable spacer length, an artificial metalloenzyme for olefin metathesis reactions in water in the absence of any organic cosolvents was obtained. High efficiencies reaching TON > 9000 in the ROMP of a water-soluble 7-oxanorbornene derivative and TON > 100 in ring-closing metathesis (RCM) of 4,4-bis(hydroxymethyl)-1,6-heptadiene in water under relatively mild conditions (pH 6, T = 25–40 °C) were observed.
Optimization: ChemicalMax TON: 9900ee: ---PDB: ---Notes: ROMP (cis/trans: 48/52)
Efficient in Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme
Optimization: Chemical & geneticMax TON: >1980ee: ---PDB: ---Notes: ArM works in combination with the ene reductase (ER) of the Old Yellow Enzyme family fromThermus scotuductus (TsOYE).