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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:

---

Active Site Topology of Artificial Peroxidase-like Hemoproteins Based on Antibodies Constructed from a Specifically Designed Ortho-carboxy-substituted Tetraarylporphyrin

The topology of the binding site has been studied for two monoclonal antibodies 13G10 and 14H7, elicited against iron(III)‐α,α,α,β‐meso‐tetrakis(ortho‐carboxyphenyl)porphyrin {α,α,α,β‐Fe[(o‐COOHPh)4‐porphyrin]}, and which exhibit in the presence of this α,α,α,β‐Fe[(o‐COOHPh)4‐porphyrin] cofactor a peroxidase activity. A comparison of the dissociation constants of the complexes of 13G10 and 14H7 with various tetra‐aryl‐substituted porphyrin has shown that : (a) the central iron(III) atom of α,α,α,β‐Fe[(o‐COOHPh)4‐porphyrin] is not recognized by either of the two antibodies; and (b) the ortho‐carboxylate substituents of the meso‐phenyl rings of α,α,α,β‐Fe[(o‐COOHPh)4‐porphyrin] are essential for the recognition of the porphyrin by 13G10 and 14H7. Measurement of the dissociation constants for the complexes of 13G10 and 14H7 with the four atropoisomers of (o‐COOHPh)4‐porphyrinH2 as well as mono‐ and di‐ortho‐carboxyphenyl‐substituted porphyrins suggests that the three carboxylates in the α, α, β position are recognized by both 13G10 and 14H7 with the two in the α, β positions more strongly bound to the antibody protein. Accordingly, the topology of the active site of 13G10 and 14H7 has roughly two‐thirds of the α,α,α,β‐Fe[(o‐COOHPh)4‐porphyrin] cofactor inserted into the binding site of the antibodies, with one of the aryl ring remaining outside. Three of the carboxylates are bound to the protein but no amino acid residue acts as an axial ligand to the iron atom. Chemical modification of lysine, histidine, tryptophan and arginine residues has shown that only modification of arginine residues causes a decrease in both the binding of α,α,α,β‐Fe[(o‐COOHPh)4‐porphyrin] and the peroxidase activity of both antibodies. Consequently, at least one of the carboxylates of the hapten is bound to an arginine residue and no amino acids such as lysine, histidine or tryptophan participate in the catalysis of the heterolytic cleavage of the O‐O bond of H2O2. In addition, the amino acid sequence of both antibodies not only reveals the presence of arginine residues, which could be those involved in the binding of the carboxylates of the hapten, but also the presence of several amino acids in the complementary determining regions which could bind other carboxylates through a network of H bonds.

Metal:

Fe

Ligand type:

---

Host protein:

Antibody 13G10 / 14H7

Anchoring strategy:

Antibody

Optimization:

Chemical & genetic

Reaction:

Peroxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

---

A De Novo Designed Metalloenzyme for the Hydration of CO2

Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature’s approach to catalysis, a ZnII metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single‐stranded three‐helix bundle and binds ZnII with high affinity using His3O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400‐fold of the fastest carbonic anhydrase isoform, CAII, and 11‐fold of CAIII.

Metal:

Zn

Ligand type:

Amino acid

Host protein:

α3D peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

kcat/KM ≈ 3.8*104 M-1*s-1

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 Heme-[4Fe-4S] Metalloenzyme Catalyzes Sulfite Reduction like the Native Enzyme

Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement, but it is challenging to design artificial enzymes to catalyze these important reactions, owing to their structural and functional complexity. We report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved—through rational tuning of the secondary sphere interactions around the [4Fe-4S] and the substrate-binding sites—to be close to that of the native enzyme. By offering insight into the requirements for a demanding six-electron, seven-proton reaction that has so far eluded synthetic catalysts, this study provides strategies for designing highly functional multicofactor artificial enzymes.

Metal:

Fe

Host protein:

Cytochrome c peroxidase

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Reaction:

Sulfite reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

Designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase

Albumin-Conjugated Corrole Metal Complexes: Extremely Simple Yet Very Efficient Biomimetic Oxidation Systems

An extremely simple biomimetic oxidation system, consisting of mixing metal complexes of amphiphilic corroles with serum albumins, utilizes hydrogen peroxide for asymmetric sulfoxidation in up to 74% ee. The albumin-conjugated manganese corroles also display catalase-like activity, and mechanistic evidence points toward oxidant-coordinated manganese(III) as the prime reaction intermediate.

Metal:

Mn

Ligand type:

Corrole

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Sulfoxidation

Max TON:

8

ee:

74

PDB:

---

Notes:

---

Metal:

Mn

Ligand type:

Corrole

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Sulfoxidation

Max TON:

42

ee:

52

PDB:

---

Notes:

---

An Artificial Heme Enzyme for Cyclopropanation Reactions

Metal:

Fe

Ligand type:

Protoporphyrin IX

Host protein:

LmrR

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Cyclopropanation

Max TON:

449

ee:

51

PDB:

6FUU

Notes:

---

An Artificial Metalloenzyme for Carbene Transfer Based on a Biotinylated Dirhodium Anchored Within Streptavidin

Metal:

Rh

Ligand type:

Carboxylate

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Cyclopropanation

Max TON:

~60

ee:

---

PDB:

---

Notes:

Cyclopropanation reaction was also performed in the E. coli periplasm.

Metal:

Rh

Ligand type:

Carboxylate

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

C-H insertion

Max TON:

~60

ee:

---

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 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:

---

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:

---

A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Oxidation

Max TON:

~1650

ee:

---

PDB:

5OJ9

Notes:

Oxidation of amplex red

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 Copper Enzymes for Asymmetric Diels–AlderReactions

Metal:

Cu

Anchoring strategy:

Covalent

Optimization:

Chemical & genetic

Max TON:

9.6

ee:

25

PDB:

1IKT

Notes:

---

Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials

Metal:

Fe

Ligand type:

Amino acid; Porphyrin

Anchoring strategy:

Covalent

Optimization:

Chemical & genetic

Reaction:

Oxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

Immobilization of the ArM on gold surfaces via a lipoic acid anchor.

Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase

Metal:

Co

Ligand type:

Oxime

Host protein:

Heme oxygenase (HO)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

H2 evolution

Max TON:

15.3

ee:

---

PDB:

---

Notes:

---

Artificial Metalloenzymes as Catalysts for Oxidative Lignin Degradation

Metal:

Fe

Anchoring strategy:

Cystein-maleimide

Optimization:

Chemical & genetic

Reaction:

Lignin oxidation

Max TON:

20

ee:

---

PDB:

---

Notes:

Reaction performed with a lignin model compound and hydrogen peroxide as oxidizing agent

Artificial Metalloenzymes Based on Biotin-Avidin Technology for the Enantioselective Reduction of Ketones by Transfer Hydrogenation

Metal:

Ru

Ligand type:

Amino-sulfonamide; P-cymene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

92

ee:

94

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; Benzene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

30

ee:

63

PDB:

---

Notes:

---

Artificial Metalloenzymes for Asymmetric Allylic Alkylation on the Basis of the Biotin–Avidin Technology

Metal:

Pd

Ligand type:

Phosphine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Allylic alkylation

Max TON:

10

ee:

93

PDB:

---

Notes:

---

Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin-Avidin

Metal:

Rh

Ligand type:

Phosphine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Hydrogenation

Max TON:

---

ee:

96

PDB:

---

Notes:

---

Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium-Diphosphine Complexes

Metal:

Rh

Ligand type:

Phosphine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Hydrogenation

Max TON:

---

ee:

94

PDB:

---

Notes:

---

Artificial Metalloenzymes Through Cysteine-Selective Conjugation of Phosphines to Photoactive Yellow Protein

Metal:

Pd

Ligand type:

Allyl; Phosphine

Anchoring strategy:

Covalent

Optimization:

Chemical & genetic

Reaction:

Allylic amination

Max TON:

45

ee:

---

PDB:

2PHY

Notes:

---

Artificial Metalloproteins Containing Co4O4 Cubane Active Sites

Metal:

Co

Ligand type:

OAc; Pyridine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

6AUC

Notes:

Co-complex in Sav WT

Metal:

Co

Ligand type:

OAc; Pyridine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

6AUC

Notes:

Co-complex in Sav S112Y

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:

---

Asymmetric δ-Lactam Synthesis with a Monomeric Streptavidin Artificial Metalloenzyme

Metal:

Rh

Ligand type:

Cp*; OAc

Host protein:

Streptavidin (monmeric)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Lactam synthesis

Max TON:

33

ee:

97

PDB:

---

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)

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

Burkavidin: A Novel Secreted Biotin-Binding Protein from the Human Pathogen Burkholderia Pseudomallei

Metal:

Rh

Ligand type:

Diphenylphosphine

Host protein:

Burkavidin

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Hydrogenation

Max TON:

~110

ee:

65

PDB:

---

Notes:

---