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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.

8-Amino-5,6,7,8-tetrahydroquinoline in Iridium(III) Biotinylated Cp* Complex as Artificial Imine Reductase

Diamine ligands I–IV coordinated to an iridium metal complex with the biotin moiety anchored to the Cp* ring were investigated. This strategy, in contrast to the traditional biotin–streptavidin technology that uses a biotinylated ligand in the artificial imine reductase, is practical for envisaging how the enantiodiscrimination by different Streptavidin (Sav) mutants could influence the chiral environment of the metal cofactor. Only in the case of (R)-CAMPY IV did the chirality at the metal centre and the second coordination sphere environment, which was dictated by the host protein, operate in a synergistic way, producing better enantioselectivity at a S112M Sav catalyst/catalyst ratio of 1.0 : 2.5. Under these optimized conditions, the artificial imine reductase afforded a good enantiomeric excess (83%) in the asymmetric transfer hydrogenation of 6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline.

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

32

ee:

83

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

99

ee:

13

PDB:

---

Notes:

---

Abiological Catalysis by Artificial Haem Proteins Containing Noble Metals in Place of Iron

Enzymes that contain metal ions—that is, metalloenzymes—possess the reactivity of a transition metal centre and the potential of molecular evolution to modulate the reactivity and substrate-selectivity of the system1. By exploiting substrate promiscuity and protein engineering, the scope of reactions catalysed by native metalloenzymes has been expanded recently to include abiological transformations2,3. However, this strategy is limited by the inherent reactivity of metal centres in native metalloenzymes. To overcome this limitation, artificial metalloproteins have been created by incorporating complete, noble-metal complexes within proteins lacking native metal sites1,4,5. The interactions of the substrate with the protein in these systems are, however, distinct from those with the native protein because the metal complex occupies the substrate binding site. At the intersection of these approaches lies a third strategy, in which the native metal of a metalloenzyme is replaced with an abiological metal with reactivity different from that of the metal in a native protein6,7,8. This strategy could create artificial enzymes for abiological catalysis within the natural substrate binding site of an enzyme that can be subjected to directed evolution. Here we report the formal replacement of iron in Fe-porphyrin IX (Fe-PIX) proteins with abiological, noble metals to create enzymes that catalyse reactions not catalysed by native Fe-enzymes or other metalloenzymes9,10. In particular, we prepared modified myoglobins containing an Ir(Me) site that catalyse the functionalization of C–H bonds to form C–C bonds by carbene insertion and add carbenes to both β-substituted vinylarenes and unactivated aliphatic α-olefins. We conducted directed evolution of the Ir(Me)-myoglobin and generated mutants that form either enantiomer of the products of C–H insertion and catalyse the enantio- and diastereoselective cyclopropanation of unactivated olefins. The presented method of preparing artificial haem proteins containing abiological metal porphyrins sets the stage for the generation of artificial enzymes from innumerable combinations of PIX-protein scaffolds and unnatural metal cofactors to catalyse a wide range of abiological transformations.

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

7260

ee:

68

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

92

ee:

84

PDB:

---

Notes:

---

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

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:

---

An Artificial Imine Reductase Based on the Ribonuclease S Scaffold

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Ribonuclease S

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

4

ee:

18

PDB:

---

Notes:

---

An Artificial Metalloenzyme with the Kinetics of Native Enzymes

Natural enzymes contain highly evolved active sites that lead to fast rates and high selectivities. Although artificial metalloenzymes have been developed that catalyze abiological transformations with high stereoselectivity, the activities of these artificial enzymes are much lower than those of natural enzymes. Here, we report a reconstituted artificial metalloenzyme containing an iridium porphyrin that exhibits kinetic parameters similar to those of natural enzymes. In particular, variants of the P450 enzyme CYP119 containing iridium in place of iron catalyze insertions of carbenes into C–H bonds with up to 98% enantiomeric excess, 35,000 turnovers, and 2550 hours−1 turnover frequency. This activity leads to intramolecular carbene insertions into unactivated C–H bonds and intermolecular carbene insertions into C–H bonds. These results lift the restrictions on merging chemical catalysis and biocatalysis to create highly active, productive, and selective metalloenzymes for abiological reactions.

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Cytochrome P450 (CYP119)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

582

ee:

98

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Cytochrome P450 (CYP119)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

35129

ee:

91

PDB:

---

Notes:

---

An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades

Metal:

Ir

Ligand type:

Cp*; Phenanthroline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

>999

ee:

>99

PDB:

---

Notes:

---

Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology

Metal:

Ru

Ligand type:

Amino-sulfonamide; Benzene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Alcohol oxidation

Max TON:

200

ee:

---

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; Benzene

Host protein:

Avidin (Av)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Alcohol oxidation

Max TON:

230

ee:

---

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Bipyridine; C6Me6

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Alcohol oxidation

Max TON:

173

ee:

---

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Alcohol oxidation

Max TON:

7.5

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Alcohol oxidation

Max TON:

30

ee:

---

PDB:

---

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 Transfer Hydrogenases Based on the Biotin-(Strept)avidin Technology: Fine Tuning the Selectivity by Saturation Mutagenesis of the Host Protein

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

96

ee:

80

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

73

ee:

60

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; Benzene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

95

ee:

70

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; P-cymene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

79

ee:

97

PDB:

---

Notes:

---

Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4000

ee:

96

PDB:

3PK2

Notes:

---

Metal:

Rh

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

94

ee:

52

PDB:

3PK2

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; P-cymene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

97

ee:

22

PDB:

3PK2

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; Benzene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

76

ee:

12

PDB:

3PK2

Notes:

---

Beyond Iron: Iridium-Containing P450 Enzymes for Selective Cyclopropanations of Structurally Diverse Alkenes

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Cytochrome P450 (CYP119)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

Cyclopropanation

Max TON:

10181

ee:

98

PDB:

---

Notes:

Selectivity for cis product (cis/trans = 90:1)

Catalytic Water Oxidation by Iridium-Modified Carbonic Anhydrase

Metal:

Ir

Ligand type:

Amino acid

Anchoring strategy:

Metal substitution

Optimization:

Chemical

Reaction:

Water oxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

Sodium periodate as sacrificial oxidant. TOF at pH 7 and 30°C is 39.8 min-1.

Chemoselective, Enzymatic C−H Bond Amination Catalyzed by a Cytochrome P450 Containing an Ir(Me)-PIX Cofactor

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Cytochrome P450 (CYP119)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

294

ee:

26

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Methyl; Porphyrin

Host protein:

Cytochrome P450 (CYP119)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

192

ee:

95

PDB:

---

Notes:

---

Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

970

ee:

13

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

158

ee:

82

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Carbene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Olefin metathesis

Max TON:

105

ee:

---

PDB:

---

Notes:

RCM, biotinylated Hoveyda-Grubbs second generation catalyst

Metal:

---

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Anion-π catalysis

Max TON:

6

ee:

41

PDB:

---

Notes:

No metal

Computational Insights on an Artificial Imine Reductase Based on the Biotin-Streptavidin Technology

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

---

ee:

96

PDB:

3PK2

Notes:

Prediction of the enantioselectivity by computational methods.

Cross-Regulation of an Artificial Metalloenzyme

Metal:

Ir

Ligand type:

Cp*; Phenanthroline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

96

ee:

---

PDB:

---

Notes:

Cross-regulated reduction of the antibiotic enrofloxacin by an ArM.

Directed Evolution of an Artificial Imine Reductase

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

380

ee:

95

PDB:

6ESS

Notes:

Salsolidine formation; Sav mutant S112A-N118P-K121A-S122M: (R)-selective

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

220

ee:

85

PDB:

6ESS

Notes:

Salsolidine formation; Sav mutant S112R-N118P-K121A-S122M-L124Y: (S)-selective

Efficient in Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

>1980

ee:

---

PDB:

---

Notes:

ArM works in combination with the ene reductase (ER) of the Old Yellow Enzyme family fromThermus scotuductus (TsOYE).

Evaluation of Chemical Diversity of Biotinylated Chiral 1,3-Diamines as a Catalytic Moiety in Artificial Imine Reductase

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

>99

ee:

83

PDB:

3PK2

Notes:

---

Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

188

ee:

43

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino carboxylic acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4

ee:

21

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Pyrazine amide

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

26

ee:

16

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

12

ee:

13

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Oxazoline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

102

ee:

14

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

94

ee:

67

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino amide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

10

ee:

7

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino carboxylic acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

8

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Pyrazine amide

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4

ee:

6

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Oxazoline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

8

ee:

0

PDB:

---

Notes:

---

Ferritin Encapsulation of Artificial Metalloenzymes: Engineering a Tertiary Coordination Sphere for an Artificial Transfer Hydrogenase

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

3874

ee:

75

PDB:

---

Notes:

---

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

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli’s Periplasm

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

1000

ee:

76

PDB:

6GMI

Notes:

---

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

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

---

ee:

60

PDB:

---

Notes:

---

High-Level Secretion of Recombinant Full-Length Streptavidin in Pichia Pastoris and its Application to Enantioselective Catalysis

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

152

ee:

61

PDB:

---

Notes:

Sav expression in E. coli

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

158

ee:

64

PDB:

---

Notes:

Sav expression in P. pastoris

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

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

47

ee:

70

PDB:

---

Notes:

---

Immobilization of an Artificial Imine Reductase Within Silica Nanoparticles Improves its Performance

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

4554

ee:

89

PDB:

---

Notes:

Reaction in nanoparticles

Immobilization of Two Organometallic Complexes into a Single Cage to Construct Protein-Based Microcompartment

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Apo-ferritin

Anchoring strategy:

Dative

Optimization:

Chemical

Reaction:

Hydrogenation

Max TON:

~2

ee:

15

PDB:

5E2D

Notes:

Tandem reaction (Hydrogenation and Suzuki-Miyaura coupling) to form biphenylethanol from 4-iodoacetophenone and phenylboronic acid. TON and ee are given for the tandem reaction product.

Metal:

Pd

Ligand type:

Allyl; Amino acid

Host protein:

Apo-ferritin

Anchoring strategy:

Dative

Optimization:

Chemical

Max TON:

~1

ee:

15

PDB:

5E2D

Notes:

Tandem reaction (Hydrogenation and Suzuki-Miyaura coupling) to form biphenylethanol from 4-iodoacetophenone and phenylboronic acid.

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:

---

Library Design and Screening Protocol for Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

183

ee:

71

PDB:

---

Notes:

Purified streptavidin (mutant K121A)

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

42

ee:

59

PDB:

---

Notes:

Cell free extract (mutant Sav K121A) treated with diamide

Metal:

Ru

Ligand type:

N-heterocyclic carbene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

66

ee:

---

PDB:

---

Notes:

Purified streptavidin (mutant K121A)

Metal:

Ru

Ligand type:

N-heterocyclic carbene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

18

ee:

---

PDB:

---

Notes:

Cell free extract (mutant Sav K121A immobilised on iminobiotin-sepharose beads)