A Protein-Rhodium Complex as an Efficient Catalyst for Two-Phase Olefin Hydroformylation
Tetrahedron Lett. 2000, 41, 3717-3720, 10.1016/S0040-4039(00)00473-1
A highly efficient and chemoselective biphasic hydroformylation of olefins was accomplished using water soluble complexes formed by the interaction between Rh(CO)2(acac) and human serum albumin (HSA), a readily available water soluble protein. A new type of shape-selectivity was observed in the hydroformylation of sterically hindered olefins.
Host protein: Human serum albumin (HSA)Anchoring strategy: UndefinedOptimization: ---Max TON: ~600ee: ---PDB: ---Notes: ---
Enzyme Activity by Design: An Artificial Rhodium Hydroformylase for Linear Aldehydes
Angew. Chem. Int. Ed. 2017, 129, 13784-13788, 10.1002/ange.201705753
Ligand type: Acac; DiphenylphosphineHost protein: Steroid Carrier Protein 2L (SCP-2L)Anchoring strategy: Cystein-maleimideOptimization: Chemical & geneticMax TON: 409ee: ---PDB: ---Notes: Selectivity for the linear product over the branched product
Regioselective Hydroformylation of Styrene Using Rhodium-Substituted Carbonic Anhydrase
ChemCatChem 2010, 2, 953-957, 10.1002/cctc.201000159
CA confidential: Replacing the active‐site zinc in carbonic anhydrase (CA) by rhodium forms a new enzymatic catalyst for cofactor‐free hydroformylation of styrene with syn gas. Unlike free rhodium, this rhodium–protein hybrid, [Rh]–CA, is regioselective (8.4:1) for linear over branched aldehyde product, which is a 40‐fold change in regioselectivity compared to free rhodium.
Host protein: Human carbonic anhydrase II (hCAII)Anchoring strategy: Metal substitutionOptimization: GeneticMax TON: 298ee: ---PDB: 4CACNotes: PDB ID 4CAC = Structure of Zn containing hCAII