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Host protein

6-Phospho-gluconolactonase (6-PGLac) A2A adenosine receptor Adipocyte lipid binding protein (ALBP) Antibody Antibody 03-1 Antibody 12E11G Antibody 13G10 Antibody 13G10 / 14H7 Antibody 14H7 Antibody 1G8 Antibody 28F11 Antibody 38C2 Antibody 3A3 Antibody 7A3 Antibody7G12-A10-G1-A12 Antibody L-chain from Mab13-1 hybridoma cells Antibody SN37.4 Apo-[Fe]-hydrogenase from M. jannaschii Apo-ferritin Apo-HydA1 ([FeFe]-hydrogenase) from C. reinhardtii Apo-HydA enzymes from C. reinhardtii, M. elsdenii, C. pasteurianum Artificial construct Avidin (Av) Azurin Binding domain of Rabenosyn (Rab4) Bovine carbonic anhydrase (CA) Bovine carbonic anhydrase II (CA) Bovine serum albumin (BSA) Bovine β-lactoglobulin (βLG) Bromelain Burkavidin C45 (c-type cytochrome maquette) Carbonic anhydrase (CA) Carboxypeptidase A Catabolite activator protein (CAP) CeuE C-terminal domain of calmodulin Cutinase Cytochrome b562 Cytochrome BM3h Cytochrome c Cytochrome c552 Cytochrome cb562 Cytochrome c peroxidase Cytochrome P450 (CYP119) Domain of Hin recombinase Due Ferro 1 E. coli catabolite gene activator protein (CAP) [FeFe]-hydrogenase from C. pasteurianum (CpI) Ferredoxin (Fd) Ferritin FhuA FhuA ΔCVFtev Flavodoxin (Fld) Glyoxalase II (Human) (gp27-gp5)3 gp45 [(gp5βf)3]2 Heme oxygenase (HO) Hemoglobin Horse heart cytochrome c Horseradish peroxidase (HRP) Human carbonic anhydrase Human carbonic anhydrase II (hCAII) Human retinoid-X-receptor (hRXRa) Human serum albumin (HSA) HydA1 ([FeFe]-hydrogenase) from C. reinhardtii IgG 84A3 Laccase Lipase B from C. antarctica (CALB) Lipase from G. thermocatenulatus (GTL) LmrR Lysozyme Lysozyme (crystal) Mimochrome Fe(III)-S6G(D)-MC6 (De novo designed peptide) Mouse adenosine deaminase Myoglobin (Mb) Neocarzinostatin (variant 3.24) NikA Nitrobindin (Nb) Nitrobindin variant NB4 Nuclease from S. aureus Papain (PAP) Photoactive Yellow Protein (PYP) Photosystem I (PSI) Phytase Prolyl oligopeptidase (POP) Prolyl oligopeptidase (POP) from P. furiosus Rabbit serum albumin (RSA) Ribonuclease S RNase A Rubredoxin (Rd) Silk fibroin fibre Small heat shock protein from M. jannaschii ß-lactoglobulin Staphylococcal nuclease Steroid Carrier Protein 2L (SCP 2L) Sterol Carrier Protein (SCP) Streptavidin (monmeric) Streptavidin (Sav) Thermolysin Thermosome (THS) tHisF TM1459 cupin TRI peptide Trypsin Tryptophan gene repressor (trp) Xylanase A (XynA) Zn8:AB54 Zn8:AB54 (mutant C96T) α3D peptide α-chymotrypsin β-lactamase β-lactoglobulin (βLG)

Corresponding author

Akabori, S. Alberto, R. Albrecht, M. Anderson, J. L. R. Apfel, U.-P. Arnold, F. H. Artero, V. Bäckvall, J. E. Baker, D. Ball, Z. T. Banse, F. Berggren, G. Bian, H.-D. Birnbaum, E. R. Borovik, A. S. Bren, K. L. Bruns, N. Brustad, E. M. Cardona, F. Case, M. A. Cavazza, C. Chan, A. S. C. Coleman, J. E. Craik, C. S. Creus, M. Cuatrecasas, P. Darnall, D. W. DeGrado, W. F. Dervan, P. B. de Vries, J. Diéguez, M. Distefano, M. D. Don Tilley, T. Duhme-Klair, A. K. Ebright, R. H. Emerson, J. P. Eppinger, J. Fasan, R. Filice, M. Fontecave, M. Fontecilla-Camps, J. C. Fruk, L. Fujieda, N. Fussenegger, M. Gademann, K. Gaggero, N. Germanas, J. P. Ghattas, W. Ghirlanda, G. Golinelli-Pimpaneau, B. Goti, A. Gras, E. Gray, H. B. Green, A. P. Gross, Z. Gunasekeram, A. Happe, T. Harada, A. Hartwig, J. F. Hasegawa, J.-Y. Hayashi, T Hemschemeier, A. Herrick, R. S. Hilvert, D. Hirota, S. Huang, F.-P. Hureau, C. Hu, X. Hyster, T. K. Imanaka, T. Imperiali, B. Itoh, S. Janda, K. D. Jarvis, A. G. Jaussi, R. Jeschek, M. Kaiser, E. T. Kamer, P. C. J. Kazlauskas, R. J. Keinan, E. Khare, S. D. Kim, H. S. Kitagawa, S. Klein Gebbink, R. J. M. Kokubo, T. Korendovych, I. V. Kuhlman, B. Kurisu, G. Laan, W. Lee, S.-Y. Lehnert, N. Leow, T. C. Lerner, R. A. Lewis, J. C. Liang, H. Lindblad, P. Lin, Y.-W. Liu, J. Lombardi, A. Lubitz, W. Lu, Y. Maglio, O. Mahy, J.-P. Mangiatordi, G. F. Marchetti, M. Maréchal, J.-D. Marino, T. Marshall, N. M. Matile, S. Matsuo, T. McNaughton, B. R. Ménage, S. Messori, L. Mulfort, K. L. Nastri, F. Nicholas, K. M. Niemeyer, C. M. Nolte, R. J. M. Novič, M. Okamoto, Y. Okano, M. Okuda, J. Onoda, A. Oohora, K. Palomo, J. M. Pàmies, O. Panke, S. Pan, Y. Paradisi, F. Pecoraro, V. L. Pordea, A. Reetz, M. T. Reijerse, E. Renaud, J.-L. Ricoux, R. Rimoldi, I. Roelfes, G. Rovis, T. Sakurai, S. Salmain, M. Sasaki, T. Sauer, D. F. Schultz, P. G. Schwaneberg, U. Seelig, B. Shafaat, H. S. Shahgaldian, P. Sheldon, R. A. Shima, S. Sigman, D. S. Song, W. J. Soumillion, P. Strater, N. Sugiura, Y. Szostak, J. W. Tezcan, F. A. Thorimbert, S. Tiede, D. M. Tiller, J. C. Turner, N. J. Ueno, T. Utschig, L. M. van Koten, G. Wang, J. Ward, T. R. Watanabe, Y. Whitesides, G. M. Wilson, K. S. Woolfson, D. N. Yilmaz, F. Zhang, J.-L.

Journal

3 Biotech Acc. Chem. Res. ACS Catal. ACS Cent. Sci. ACS Sustainable Chem. Eng. Adv. Synth. Catal. Angew. Chem., Int. Ed. Appl. Biochem. Biotechnol. Appl. Organomet. Chem. Artificial Metalloenzymes and MetalloDNAzymes in Catalysis: From Design to Applications Beilstein J. Org. Chem. Biochemistry Biochim. Biophys. Acta, Bioenerg. Biochimie Bioconjug. Chem. Bioorg. Med. Chem. Bioorg. Med. Chem. Lett. Bioorganometallic Chemistry: Applications in Drug Discovery, Biocatalysis, and Imaging Biopolymers Biotechnol. Adv. Biotechnol. Bioeng. Can. J. Chem. Catal. Lett. Catal. Sci. Technol. Cat. Sci. Technol. ChemBioChem ChemCatChem Chem. Commun. Chem. Rev. Chem. Sci. Chem. Soc. Rev. Chem. - Eur. J. Chem. - Asian J. Chem. Lett. ChemistryOpen ChemPlusChem Chimia Commun. Chem. Comprehensive Inorganic Chemistry II Comprehensive Supramolecular Chemistry II C. R. Chim. Coordination Chemistry in Protein Cages: Principles, Design, and Applications Coord. Chem. Rev. Croat. Chem. Acta Curr. Opin. Biotechnol. Curr. Opin. Chem. Biol. Curr. Opin. Struct. Biol. Dalton Trans. Effects of Nanoconfinement on Catalysis Energy Environ. Sci. Eur. J. Biochem. Eur. J. Inorg. Chem. FEBS Lett. Helv. Chim. Acta Inorg. Chim. Acta Inorg. Chem. Int. J. Mol. Sci. Isr. J. Chem. J. Biol. Chem. J. Biol. Inorg. Chem. J. Immunol. Methods J. Inorg. Biochem. J. Mol. Catal. A: Chem. J. Mol. Catal. B: Enzym. J. Organomet. Chem. J. Phys. Chem. Lett. J. Porphyr. Phthalocyanines J. Protein Chem. J. Am. Chem. Soc. J. Chem. Soc. J. Chem. Soc., Chem. Commun. Methods Enzymol. Mol. Divers. Molecular Encapsulation: Organic Reactions in Constrained Systems Nature Nat. Catal. Nat. Chem. Biol. Nat. Chem. Nat. Commun. Nat. Protoc. Nat. Rev. Chem. New J. Chem. Org. Biomol. Chem. Plos ONE Proc. Natl. Acad. Sci. U. S. A. Process Biochem. Prog. Inorg. Chem. Prot. Eng. Protein Engineering Handbook Protein Expression Purif. Pure Appl. Chem. RSC Adv. Science Small Synlett Tetrahedron Tetrahedron: Asymmetry Tetrahedron Lett. Chem. Rec. Top. Catal. Top. Organomet. Chem. Trends Biotechnol.

A Chaperonin as Protein Nanoreactor for Atom-Transfer Radical Polymerization

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 Cofactor Approach to Copper-Dependent Catalytic Antibodies

A strategy for the preparation of semisynthetic copper(II)-based catalytic metalloproteins is described in which a metal-binding bis-imidazole cofactor is incorporated into the combining site of the aldolase antibody 38C2. Antibody 38C2 features a large hydrophobic-combining site pocket with a highly nucleophilic lysine residue, LysH93, that can be covalently modified. A comparison of several lactone and anhydride reagents shows that the latter are the most effective and general derivatizing agents for the 38C2 Lys residue. A bis-imidazole anhydride (5) was efficiently prepared from N-methyl imidazole. The 38C2–5-Cu conjugate was prepared by either (i) initial derivatization of 38C2 with 5 followed by metallation with CuCl2, or (ii) precoordination of 5 with CuCl2 followed by conjugation with 38C2. The resulting 38C2–5-Cu conjugate was an active catalyst for the hydrolysis of the coordinating picolinate ester 11, following Michaelis–Menten kinetics [kcat(11) = 2.3 min−1 and Km(11) 2.2 mM] with a rate enhancement [kcat(11)kuncat(11)] of 2.1 × 105. Comparison of the second-order rate constants of the modified 38C2 and the Cu(II)-bis-imidazolyl complex k(6-CuCl2) gives a rate enhancement of 3.5 × 104 in favor of the antibody complex with an effective molarity of 76.7 M, revealing a significant catalytic benefit to the binding of the bis-imidazolyl ligand into 38C2.

Metal:

Cu

Ligand type:

Bisimidazol

Host protein:

Antibody 38C2

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers

Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O2 to H2O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

1056

ee:

---

PDB:

4FWX

Notes:

Sperm whale myoglobin

A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme

Terminal oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, most biomimetic catalysts have much lower activity than native oxidases. Herein we report a designed oxidase in myoglobin with an O2 reduction rate (52 s–1) comparable to that of a native cytochrome (cyt) cbb3 oxidase (50 s–1) under identical conditions. We achieved this goal by engineering more favorable electrostatic interactions between a functional oxidase model designed in sperm whale myoglobin and its native redox partner, cyt b5, resulting in a 400-fold electron transfer (ET) rate enhancement. Achieving high activity equivalent to that of native enzymes in a designed metalloenzyme offers deeper insight into the roles of tunable processes such as ET in oxidase activity and enzymatic function and may extend into applications such as more efficient oxygen reduction reaction catalysts for biofuel cells.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

O2 reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

O2 reduction rates of 52 s-1 were achieved in combination with the native redox partner cyt b5.

An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein

Guided by nature: A designed binding site comprising the His/His/Asp motif for CuII complexation has been constructed in a robust protein by site‐specific mutagenesis (see picture). The artificial metalloenzyme catalyzes an enantioselective Diels–Alder reaction.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

tHisF

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

6.7

ee:

46

PDB:

---

Notes:

---

An Enantioselective Artificial Metallo-Hydratase

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:

---

Artificial Copper Enzymes for Asymmetric Diels–AlderReactions

Metal:

Cu

Anchoring strategy:

Covalent

Optimization:

Chemical & genetic

Max TON:

9.6

ee:

25

PDB:

1IKT

Notes:

---

Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo- b-lactamase into a Catechol Oxidase

Metal:

Cu

Ligand type:

Amino acid

Host protein:

β-lactamase

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Catechol oxidation

Max TON:

---

ee:

---

PDB:

2FU7

Notes:

---

Artificial Diels–Alderase based on the Transmembrane Protein FhuA

Metal:

Cu

Ligand type:

Terpyridine

Host protein:

FhuA

Anchoring strategy:

Cystein-maleimide

Optimization:

Chemical

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Artificial Metalloenzymes based on Protein Cavities: Exploring the Effect of Altering the Metal Ligand Attachment Position by Site Directed Mutagenesis

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

1 to 4

ee:

61 to 94

PDB:

---

Notes:

Varied attachment position

Artificial Metalloenzymes with the Neocarzinostatin Scaffold: Toward a Biocatalyst for the Diels–Alder Reaction

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

33

ee:

---

PDB:

---

Notes:

Up to endo/exo ratio 62:38

A Semisynthetic Metalloenzyme based on a Protein Cavity that Catalyzes the Enantioselective Hydrolysis of Ester and Amide Substrates

In an effort to prepare selective and efficient catalysts for ester and amide hydrolysis, we are designing systems that position a coordinated metal ion within a defined protein cavity. Here, the preparation of a protein-1,10-phenanthroline conjugate and the hydrolytic chemistry catalyzed by this construct are described. Iodoacetamido-1,10-phenanthroline was used to modify a unique cysteine residue in ALBP (adipocyte lipid binding protein) to produce the conjugate ALBP-Phen. The resulting material was characterized by electrospray mass spectrometry, UV/vis and fluorescence spectroscopy, gel filtration chromatography, and thiol titration. The stability of ALBP-Phen was evaluated by guanidine hydrochloride denaturation experiments, and the ability of the conjugate to bind Cu(II) was demonstrated by fluorescence spectroscopy. ALBP-Phen-Cu(II) catalyzes the enantioselective hydrolysis of several unactivated amino acid esters under mild conditions (pH 6.1, 25 °C) at rates 32−280-fold above the background rate in buffered aqueous solution. In 24 h incubations 0.70 to 7.6 turnovers were observed with enantiomeric excesses ranging from 31% ee to 86% ee. ALBP-Phen-Cu(II) also promotes the hydrolysis of an aryl amide substrate under more vigorous conditions (pH 6.1, 37 °C) at a rate 1.6 × 104-fold above the background rate. The kinetics of this amide hydrolysis reaction fit the Michaelis−Menten relationship characteristic of enzymatic processes. The rate enhancements for ester and amide hydrolysis reported here are 102−103 lower than those observed for free Cu(II) but comparable to those previously reported for Cu(II) complexes.

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

---

Max TON:

1 to 8

ee:

39 to 86

PDB:

---

Notes:

---

Autoxidation of Ascorbic Acid Catalyzed by a Semisynthetic Enzyme

Metal:

Cu

Ligand type:

Bipyridine

Host protein:

Papain (PAP)

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Oxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Bimetallic Copper-Heme-Protein-DNA Hybrid Catalyst for Diels Alder Reaction

Metal:

Cu

Ligand type:

Bipyridine

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

7.1

ee:

18

PDB:

---

Notes:

Horse heart myoglobin

Biosynthesis of a Site-Specific DNA Cleaving Protein

Metal:

Cu

Ligand type:

Bipyridine

Anchoring strategy:

---

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

Catabolite activator protein from E. coli

Metal:

Fe

Ligand type:

Bipyridine

Anchoring strategy:

---

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

Catabolite activator protein from E. coli

Building Reactive Copper Centers in Human Carbonic Anhydrase II

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

Carbene in Cupredoxin Protein Scaffolds: Replacement of a Histidine Ligand in the Active Site Substantially Alters Copper Redox Properties

Metal:

Cu

Host protein:

Azurin

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Reaction:

Electron transfer

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Catalytic Reduction of NO to N2O by a Designed Heme Copper Center in Myoglobin: Implications for the Role of Metal Ions

Metal:

Cu

Ligand type:

Amino acid; Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

2400

ee:

---

PDB:

---

Notes:

Sperm whale myoglobin

Chemical Conversion of a DNA-Binding Protein into a Site-Specific Nuclease

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Oxidative cleavage

Max TON:

<1

ee:

---

PDB:

---

Notes:

Engineered sequence specificity

Construction of a Hybrid Biocatalyst Containing a Covalently-Linked Terpyridine Metal Complex within a Cavity of Aponitrobindin

Metal:

Cu

Ligand type:

Terpyridine

Host protein:

Nitrobindin (Nb)

Anchoring strategy:

Cystein-maleimide

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Construction of Robust Bio-Nanotubes using the Controlled Self-Assembly of Component Proteins of Bacteriophage T4

Metal:

Cu

Ligand type:

Flavin

Host protein:

[(gp5βf)3]2

Anchoring strategy:

Lysine-succinimide

Optimization:

---

Reaction:

Cycloaddition

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Conversion of a Helix-Turn-Helix Motif Sequence-Specific DNA Binding Protein into a Site-Specific DNA Cleavage Agent

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Oxidative cleavage

Max TON:

<1

ee:

---

PDB:

---

Notes:

Engineered sequence specificity

Copper–Phthalocyanine Conjugates of Serum Albumins as Enantioselective Catalysts in Diels–Alder Reactions

Metal:

Cu

Ligand type:

Phthalocyanine

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Max TON:

45.5

ee:

98

PDB:

---

Notes:

---

Defining the Role of Tyrosine and Rational Tuning of Oxidase Activity by Genetic Incorporation of Unnatural Tyrosine Analogs

Metal:

Cu

Ligand type:

Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

1200

ee:

---

PDB:

4FWX

Notes:

Sperm whale myoglobin

Designing a Functional Type 2 Copper Center that has Nitrite Reductase Activity Within α-Helical Coiled Coils

Metal:

Cu

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

>5

ee:

---

PDB:

---

Notes:

Nitrite reduction

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

Metal:

Cu

Ligand type:

Bipyridine

Host protein:

LmrR

Anchoring strategy:

---

Optimization:

Genetic

Reaction:

Hydration

Max TON:

9

ee:

64

PDB:

---

Notes:

---

Enantioselective Artificial Metalloenzymes by Creation of a Novel Active Site at the Protein Dimer Interface

Metal:

Cu

Ligand type:

Bipyridine; Phenanthroline

Host protein:

LmrR

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

32.7

ee:

97

PDB:

3F8B

Notes:

---

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

Metal:

Cu

Ligand type:

Amino acid

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

35

ee:

---

PDB:

---

Notes:

---

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

Metal:

Cu

Ligand type:

Bipyridine

Host protein:

LmrR

Anchoring strategy:

---

Optimization:

Genetic

Max TON:

10.4

ee:

83

PDB:

3F8B

Notes:

---

Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins

Metal:

Cu

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Oxidation

Max TON:

---

ee:

---

PDB:

6ANX

Notes:

---