25 publications

25 publications

A Chaperonin as Protein Nanoreactor for Atom-Transfer Radical Polymerization

Bruns, N.

Angew. Chem., Int. Ed., 2013, 10.1002/anie.201306798

The group II chaperonin thermosome (THS) from the archaea Thermoplasma acidophilum is reported as nanoreactor for atom‐transfer radical polymerization (ATRP). A copper catalyst was entrapped into the THS to confine the polymerization into this protein cage. THS possesses pores that are wide enough to release polymers into solution. The nanoreactor favorably influenced the polymerization of N‐isopropyl acrylamide and poly(ethylene glycol)methylether acrylate. Narrowly dispersed polymers with polydispersity indices (PDIs) down to 1.06 were obtained in the protein nanoreactor, while control reactions with a globular protein–catalyst conjugate only yielded polymers with PDIs above 1.84.


Metal: Cu
Host protein: Thermosome (THS)
Anchoring strategy: Covalent
Optimization: ---
Reaction: Polymerization
Max TON: ---
ee: ---
PDB: ---
Notes: Non-ROMP

A Clamp-Like Biohybrid Catalyst for DNA Oxidation

Nolte, R.J.M.

Nat. Chem., 2013, 10.1038/NCHEM.1752

In processive catalysis, a catalyst binds to a substrate and remains bound as it performs several consecutive reactions, as exemplified by DNA polymerases. Processivity is essential in nature and is often mediated by a clamp-like structure that physically tethers the catalyst to its (polymeric) template. In the case of the bacteriophage T4 replisome, a dedicated clamp protein acts as a processivity mediator by encircling DNA and subsequently recruiting its polymerase. Here we use this DNA-binding protein to construct a biohybrid catalyst. Conjugation of the clamp protein to a chemical catalyst with sequence-specific oxidation behaviour formed a catalytic clamp that can be loaded onto a DNA plasmid. The catalytic activity of the biohybrid catalyst was visualized using a procedure based on an atomic force microscopy method that detects and spatially locates oxidized sites in DNA. Varying the experimental conditions enabled switching between processive and distributive catalysis and influencing the sliding direction of this rotaxane-like catalyst.


Metal: Mn
Ligand type: Porphyrin
Host protein: gp45
Anchoring strategy: Covalent
Optimization: ---
Max TON: ---
ee: ---
PDB: 1CZD
Notes: ---

A Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin−Streptavidin Technology

Ward, T.R.

J. Am. Chem. Soc., 2013, 10.1021/ja309974s

Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.


Metal: Ir
Ligand type: Amino acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 14
ee: 11
PDB: ---
Notes: ---

Metal: Rh
Ligand type: Amino acid; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 100
ee: 79
PDB: ---
Notes: ---

A Hybrid Ring- Opening Metathesis Polymerization Catalyst Based on an Engineered Variant of the Beta-Barrel Protein FhuA

Okuda, J.; Schwaneberg, U.

Chem. - Eur. J., 2013, 10.1002/chem.201301515

A β‐barrel protein hybrid catalyst was prepared by covalently anchoring a Grubbs–Hoveyda type olefin metathesis catalyst at a single accessible cysteine amino acid in the barrel interior of a variant of β‐barrel transmembrane protein ferric hydroxamate uptake protein component A (FhuA). Activity of this hybrid catalyst type was demonstrated by ring‐opening metathesis polymerization of a 7‐oxanorbornene derivative in aqueous solution.


Metal: Ru
Ligand type: Carbene
Host protein: FhuA ΔCVFtev
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Olefin metathesis
Max TON: 955
ee: ---
PDB: ---
Notes: ROMP

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: ---

Aqueous Phase Transfer Hydrogenation of Aryl Ketones Catalysed by Achiral Ruthenium(II) and Rhodium(III) Complexes and their Papain Conjugates

Salmain, M.

Appl. Organomet. Chem., 2013, 10.1002/aoc.2929


Metal: Rh
Ligand type: Cp*; Poly-pyridine
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Hydrogenation
Max TON: 96
ee: 15
PDB: ---
Notes: ---

Artificial Metalloenzymes and Metallopeptide Catalysts for Organic Synthesis

Review

Lewis, J.C.

ACS Catal., 2013, 10.1021/cs400806a


Notes: ---

Biomacromolecules as Ligands for Artificial Metalloenzymes

Review

Ward, T.R.

Comprehensive Inorganic Chemistry II, 2013, 10.1016/B978-0-08-097774-4.00626-4


Notes: Book chapter

Building Reactive Copper Centers in Human Carbonic Anhydrase II

Emerson, J.P.

J. Biol. Inorg. Chem., 2013, 10.1007/s00775-013-1009-1


Metal: Cu
Ligand type: Amino acid
Anchoring strategy: Dative
Optimization: ---
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: 1RZC
Notes: Oxidation of 2-aminophenol with subsequent formation of 2-aminophenoxazinone. Reaction rate = 0.09 s-1

C(sp3)–H Bond Hydroxylation Catalyzed by Myoglobin Reconstituted with Manganese Porphycene

Hayashi, T

J. Am. Chem. Soc., 2013, 10.1021/ja409404k


Metal: Mn
Ligand type: Porphycene
Host protein: Myoglobin (Mb)
Anchoring strategy: Reconstitution
Optimization: ---
Reaction: Hydroxylation
Max TON: ---
ee: ---
PDB: 2WI8
Notes: ---

De Novo Design of Functional Proteins: Toward Artificial Hydrogenases

Review

Ghirlanda, G.

Biopolymers, 2013, 10.1002/bip.22420


Notes: ---

Designing Enzyme-Like Catalysts: A Rhodium(II) Metallopeptide Case Study

Review

Ball, Z.T.

Acc. Chem. Res., 2013, 10.1021/ar300261h


Notes: ---

Designing Functional Metalloproteins: From Structural to Catalytic Metal Sites

Review

Pecoraro, V.L.

Coord. Chem. Rev., 2013, 10.1016/j.ccr.2013.02.007


Notes: ---

Fluorescence-Based Assay for the Optimization of the Activity of Artificial Transfer Hydrogenase within a Biocompatible Compartment

Ward, T.R.

ChemCatChem, 2013, 10.1002/cctc.201200834


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Genetic Optimization of the Catalytic Efficiency of Artificial Imine Reductases Based on Biotin−Streptavidin Technology

Ward, T.R.

ACS Catal., 2013, 10.1021/cs400428r


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: ---
ee: 60
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: ---

Influence of Active Site Location on Catalytic Activity in De Novo-Designed Zinc Metalloenzymes

Pecoraro, V.L.

J. Am. Chem. Soc., 2013, 10.1021/ja401537t


Metal: Hg; Zn
Ligand type: Amino acid
Host protein: TRI peptide
Anchoring strategy: Dative
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: 3PBJ
Notes: Influence of position of Zn and Hg ion on catalytic activity of the ArM tested. PDB ID 3PBJ = Structure of an analogue.

Metal-Catalyzed Organic Transformations Inside a Protein Scaffold Using Artificial Metalloenzymes

Review

Ward, T.R.

Coordination Chemistry in Protein Cages: Principles, Design, and Applications, 2013, 10.1002/9781118571811.ch8


Notes: Book chapter

Metal-Conjugated Affinity Labels: A New Concept to Create Enantioselective Artificial Metalloenzymes

Eppinger, J.

ChemistryOpen, 2013, 10.1002/open.201200044


Metal: Rh
Ligand type: Cp*; Phosphine
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Hydrogenation
Max TON: 89
ee: 64
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Benzene; Phosphine
Host protein: Bromelain
Anchoring strategy: Covalent
Optimization: Chemical
Reaction: Hydrogenation
Max TON: 44
ee: 20
PDB: ---
Notes: ---

Metal Incorporated Horseradish Peroxidase (HRP) Catalyzed Oxidation of Resveratrol: Selective Dimerization or Decomposition

Pan, Y.

RSC Adv., 2013, 10.1039/c3ra43784a


Metal: Ca; Co; Mn; Ni; Zn
Ligand type: Undefined
Anchoring strategy: Undefined
Optimization: Chemical
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: ---
Notes: Oxidation of resveratrol. Dimerisation product obtained.

Metalloprotein Design

Review

Marshall, N.M.

Comprehensive Inorganic Chemistry II, 2013, 10.1016/B978-0-08-097774-4.00325-9


Notes: Book chapter

Protein Delivery of a Ni Catalyst to Photosystem I for Light-Driven Hydrogen Production

Tiede, D.M.; Utschig, L.M.

J. Am. Chem. Soc., 2013, 10.1021/ja405277g


Metal: Ni
Ligand type: Phosphine
Host protein: Flavodoxin (Fld)
Anchoring strategy: Supramolecular
Optimization: ---
Reaction: H2 evolution
Max TON: 94
ee: ---
PDB: ---
Notes: Recalculated TON

Metal: Ni
Ligand type: Phosphine
Host protein: Photosystem I (PSI)
Anchoring strategy: Undefined
Optimization: ---
Reaction: H2 evolution
Max TON: 1870
ee: ---
PDB: ---
Notes: Recalculated TON

Spontaneous Activation of [FeFe]-Hydrogenases by an Inorganic [2Fe] Active Site Mimic

Happe, T.

Nat. Chem. Biol., 2013, 10.1038/Nchembio.1311


Metal: Fe
Ligand type: CN; CO; Dithiolate
Anchoring strategy: Dative
Optimization: Chemical
Reaction: H2 evolution
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Structural Basis for Enantioselectivity in the Transfer Hydrogenation of a Ketone Catalyzed by an Artificial Metalloenzyme

Fontecilla-Camps, J.C.

Eur. J. Inorg. Chem., 2013, 10.1002/ejic.201300592


Metal: Rh
Ligand type: 2,2'-Dipyridylamine; Cp*
Anchoring strategy: Supramolecular
Optimization: ---
Max TON: ---
ee: 26
PDB: 4KII
Notes: ---

Synthetic Cascades are Enabled by Combining Biocatalysts with Artificial Metalloenzymes

Turner, N.J.; Ward, T.R.

Nat. Chem., 2013, 10.1038/NCHEM.1498


Metal: Ir
Ligand type: Amino-sulfonamide; Cp*
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 100
ee: > 99
PDB: ---
Notes: Cascade