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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 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.

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.

Metal:

Ru

Ligand type:

Carbene

Host protein:

Nitrobindin (Nb)

Anchoring strategy:

Covalent

Optimization:

Chemical

Reaction:

Olefin metathesis

Max TON:

9900

ee:

---

PDB:

---

Notes:

ROMP (cis/trans: 48/52)

Metal:

Ru

Ligand type:

Carbene

Host protein:

Nitrobindin (Nb)

Anchoring strategy:

Covalent

Optimization:

Chemical

Reaction:

Olefin metathesis

Max TON:

100

ee:

---

PDB:

---

Notes:

RCM

Albumin as a Promiscuous Biocatalyst in Organic Synthesis

Review
Albumin emerged as a biocatalyst in 1980 and the continuing interest in this protein is proved by numerous papers. The use of albumin was initially confined to the field of asymmetric oxidations and reductions, but more recently it has found a broader application to chemical reactions such as additions, condensations and eliminations. This review reports the main applications of albumin in organic synthesis that have appeared in the literature in the past decade.

Notes:

---

An Artificial Enzyme Made by Covalent Grafting of an FeII Complex into β-Lactoglobulin: Molecular Chemistry, Oxidation Catalysis, and Reaction-Intermediate Monitoring in a Protein

An artificial metalloenzyme based on the covalent grafting of a nonheme FeII polyazadentate complex into bovine β‐lactoglobulin has been prepared and characterized by using various spectroscopic techniques. Attachment of the FeII catalyst to the protein scaffold is shown to occur specifically at Cys121. In addition, spectrophotometric titration with cyanide ions based on the spin‐state conversion of the initial high spin (S=2) FeII complex into a low spin (S=0) one allows qualitative and quantitative characterization of the metal center’s first coordination sphere. This biohybrid catalyst activates hydrogen peroxide to oxidize thioanisole into phenylmethylsulfoxide as the sole product with an enantiomeric excess of up to 20 %. Investigation of the reaction between the biohybrid system and H2O2 reveals the generation of a high spin (S=5/2) FeIII(η2‐O2) intermediate, which is proposed to be responsible for the catalytic sulfoxidation of the substrate.

Metal:

Fe

Ligand type:

Poly-pyridine

Host protein:

ß-lactoglobulin

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Sulfoxidation

Max TON:

5.6

ee:

20

PDB:

---

Notes:

---

An Enantioselective Artificial Suzukiase Based on the Biotin–Streptavidin Technology

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:

---

Aqueous Light Driven Hydrogen Production by a Ru–Ferredoxin–Co Biohybrid

Metal:

Co

Ligand type:

Oxime

Host protein:

Ferredoxin (Fd)

Anchoring strategy:

Dative

Optimization:

---

Reaction:

H2 evolution

Max TON:

210

ee:

---

PDB:

---

Notes:

Recalculated TON

Artificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle Structure

Review

Notes:

---

Artificial Hydrogenase: Biomimetic Approaches Controlling Active Molecular Catalysts

Review

Notes:

---

Artificial Hydrogenases: Biohybrid and Supramolecular Systems for Catalytic Hydrogen Production or Uptake

Review

Notes:

---

Artificial Metalloenzymes Derived from Three-Helix Bundles

Review

Notes:

---

Artificial Metalloenzymes for Asymmetric Catalysis by Creation of Novel Active Sites in Protein and DNA Scaffolds

Review

Notes:

---

Artificial Metalloenzymes for the Diastereoselective Reduction of NAD+ to NAD2H

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Artificial Metalloenzymes in Asymmetric Catalysis: Key Developments and Future Directions

Review

Notes:

---

Carbonic Anhydrase II as Host Protein for the Creation of a Biocompatible Artificial Metathesase

Metal:

Ru

Ligand type:

Carbene

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Reaction:

Olefin metathesis

Max TON:

28

ee:

---

PDB:

---

Notes:

Ring closing metathesis. 28 turnovers obtained under physiological conditions within 4 hours.

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

De Novo Protein Design as a Methodology for Synthetic Bioinorganic Chemistry

Review

Notes:

---

Directed Evolution of Artificial Metalloenzymes

Review

Notes:

---

Direct Hydrogenation of Carbon Dioxide by an Artificial Reductase Obtained by Substituting Rhodium for Zinc in the Carbonic Anhydrase Catalytic Center. A Mechanistic Study

Metal:

Rh

Ligand type:

Amino acid

Anchoring strategy:

Metal substitution

Optimization:

---

Reaction:

Hydrogenation

Max TON:

---

ee:

---

PDB:

---

Notes:

Computational study of the reaction mechanism of the formation of HCOOH from CO2

Engineering a Dirhodium Artificial Metalloenzyme for Selective Olefin Cyclopropanation

Metal:

Rh

Ligand type:

Poly-carboxylic acid

Anchoring strategy:

Covalent

Optimization:

Chemical & genetic

Reaction:

Cyclopropanation

Max TON:

74

ee:

92

PDB:

---

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:

---

From Enzyme Maturation to Synthetic Chemistry: The Case of Hydrogenases

Review

Notes:

---

From "Hemoabzymes" to "Hemozymes": Towards new Biocatalysts for Selective Oxidations

Review

Notes:

---

Generation of New Artificial Metalloproteins by Cofactor Modification of Native Hemoproteins

Review

Notes:

---

Hybrid [FeFe]-Hydrogenases with Modified Active Sites Show Remarkable Residual Enzymatic Activity

Metal:

Fe

Ligand type:

CN; CO; Dithiolate

Anchoring strategy:

Dative

Optimization:

Chemical

Max TON:

---

ee:

---

PDB:

---

Notes:

H2 evolution: TOF = 450 s-1. H2 oxidation: TOF = 150 s-1.

Hybrid Ruthenium ROMP Catalysts Based on an Engineered Variant of β-Barrel Protein FhuA ΔCVFtev: Effect of Spacer Length

Metal:

Ru

Ligand type:

Carbene

Host protein:

FhuA ΔCVFtev

Anchoring strategy:

Covalent

Optimization:

Chemical

Reaction:

Olefin metathesis

Max TON:

555

ee:

---

PDB:

---

Notes:

ROMP; cis/trans = 58/42

Improving the Catalytic Performance of an Artificial Metalloenzyme by Computational Design

Metal:

Ir

Ligand type:

Cp*; Pyridine sulfonamide

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

100

ee:

96

PDB:

---

Notes:

---

Latest Developments in Metalloenzyme Design and Repurposing

Review

Notes:

---

Lipase Active Site Covalent Anchoring of Rh(NHC) Catalysts: Towards Chemoselective Artificial Metalloenzymes

Metal:

Rh

Ligand type:

Carbene

Host protein:

Cutinase

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Hydrogenation

Max TON:

20

ee:

rac.

PDB:

1CEX

Notes:

---

Metal:

Rh

Ligand type:

Carbene

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Hydrogenation

Max TON:

20

ee:

rac.

PDB:

1CEX

Notes:

---

Metal-Binding Promiscuity in Artificial Metalloenzyme Design

Review

Notes:

---

Metallopeptide Catalysts and Artificial Metalloenzymes Containing Unnatural Amino Acids

Review

Notes:

---