10 publications

10 publications

An Enantioselective Artificial Metallo-Hydratase

Roelfes, G.

Chem. Sci., 2013, 10.1039/c3sc51449h

Direct addition of water to alkenes to generate important chiral alcohols as key motif in a variety of natural products still remains a challenge in organic chemistry. Here, we report the first enantioselective artificial metallo-hydratase, based on the transcription factor LmrR, which catalyses the conjugate addition of water to generate chiral β-hydroxy ketones with enantioselectivities up to 84% ee. A mutagenesis study revealed that an aspartic acid and a phenylalanine located in the active site play a key role in achieving efficient catalysis and high enantioselectivities.


Metal: Cu
Ligand type: Phenanthroline
Host protein: LmrR
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 30
ee: 84
PDB: 3F8B
Notes: ---

An Enantioselective Artificial Suzukiase Based on the Biotin–Streptavidin Technology

Ward, T.R.

Chem. Sci., 2015, 10.1039/c5sc03116h


Metal: Pd
Ligand type: Allyl; Phosphine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 88
ee: 80
PDB: ---
Notes: ---

Metal: Pd
Ligand type: Allyl; Carbene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 5
ee: ---
PDB: ---
Notes: ---

A Structural View of Synthetic Cofactor Integration into [FeFe]-Hydrogenases

Apfel, U.-P.; Happe, T.; Kurisu, G.

Chem. Sci., 2016, 10.1039/C5SC03397G


Metal: Fe
Ligand type: CN; CO; Dithiolate
Anchoring strategy: Dative
Optimization: Chemical
Reaction: H2 evolution
Max TON: ---
ee: ---
PDB: 4XDC
Notes: H2 evolution activity of the ArM: 2874 (mmol H2)*min-1*(mg protein)-1.

Design of an Enantioselective Artificial Metallo-Hydratase Enzyme Containing an Unnatural Metal-Binding Amino Acid

Maréchal, J.-D.; Roelfes, G.

Chem. Sci., 2017, 10.1039/C7SC03477F


Metal: Cu
Ligand type: Bipyridine
Host protein: LmrR
Anchoring strategy: ---
Optimization: Genetic
Reaction: Hydration
Max TON: 9
ee: 64
PDB: ---
Notes: ---

E. coli Surface Display of Streptavidin for Directed Evolution of an Allylic Deallylase

Ward, T.R.

Chem. Sci., 2018, 10.1039/c8sc00484f


Metal: Ru
Ligand type: Cp; Quinoline
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Reaction: Deallylation
Max TON: 148
ee: ---
PDB: 6FH8
Notes: ---

Enzyme Repurposing of a Hydrolase as an Emergent Peroxidase Upon Metal Binding

Fujieda, N.; Ward, T.R.

Chem. Sci., 2015, 10.1039/c5sc01065a


Metal: Cu
Ligand type: Amino acid
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 35
ee: ---
PDB: ---
Notes: ---

Human Carbonic Anhydrase II as Host Protein for the Creation of Artificial Metalloenzymes: The Asymmetric Transfer Hydrogenation of Imines

Ward, T.R.

Chem. Sci., 2013, 10.1039/c3sc51065d


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 47
ee: 70
PDB: ---
Notes: ---

Novel Artificial Metalloenzymes by In Vivo Incorporation of Metal-Binding Unnatural Amino Acids

Roelfes, G.

Chem. Sci., 2015, 10.1039/c4sc01525h


Metal: Cu
Ligand type: Bipyridine
Host protein: LmrR
Anchoring strategy: ---
Optimization: Genetic
Max TON: 10.4
ee: 83
PDB: 3F8B
Notes: ---

Ru–protein–Co Biohybrids Designed for Solar Hydrogen Production: Understanding Electron Transfer Pathways Related to Photocatalytic Function

Utschig, L.M.

Chem. Sci., 2016, 10.1039/c6sc03121h


Metal: Co
Ligand type: Oxime
Host protein: Ferredoxin (Fd)
Anchoring strategy: Dative
Optimization: Chemical
Reaction: H2 evolution
Max TON: 650
ee: ---
PDB: ---
Notes: Recalculated TON

Significant Improvement of Oxidase Activity Through the Genetic Incorporation of a Redox-Active Unnatural Amino Acid

Lu, Y.; Wang, J.

Chem. Sci., 2015, 10.1039/C5SC01126D


Metal: Cu
Ligand type: Amino acid
Host protein: Myoglobin (Mb)
Anchoring strategy: Dative
Optimization: Genetic
Reaction: O2 reduction
Max TON: >1100
ee: ---
PDB: ---
Notes: Reduction potential was lowered by incorporation of the unnatural amino acid 3-methoxy tyrosine.