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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.

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:

---

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 Clamp-Like Biohybrid Catalyst for DNA Oxidation

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

Metal:

Mn

Ligand type:

Porphyrin

Host protein:

gp45

Anchoring strategy:

Covalent

Optimization:

---

Max TON:

---

ee:

---

PDB:

1CZD

Notes:

---

A 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

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 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:

---

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

Antibody-Metalloporphyrin Catalytic Assembly Mimics Natural Oxidation Enzymes

Metal:

Ru

Ligand type:

Porphyrin

Host protein:

Antibody SN37.4

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Sulfoxidation

Max TON:

750

ee:

43

PDB:

---

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 Peroxidase-Like Hemoproteins Based on Antibodies Constructed from a Specifically Designed Ortho-Carboxy Substituted Tetraarylporphyrin Hapten and Exhibiting a High Affinity for Iron-Porphyrins

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 13G10

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

kcat/KM = 105 M-1 * s-1

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)

Capture and Characterization of a Reactive Haem– Carbenoid Complex in an Artificial Metalloenzyme

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

---

Optimization:

Genetic

Reaction:

Cyclopropanation

Max TON:

1000

ee:

99

PDB:

6F17

Notes:

Structure of the Mb*(NMH) haem-iron complex

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

---

Optimization:

Genetic

Reaction:

Cyclopropanation

Max TON:

1000

ee:

99

PDB:

6F17

Notes:

Structure of the Mb*(NMH) haem-iron–carbenoid complex

Capture and Characterization of a Reactive Haem– Carbenoid Complex in an Artificial Metalloenzyme

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

---

Optimization:

Genetic

Reaction:

Cyclopropanation

Max TON:

1000

ee:

99

PDB:

6F17

Notes:

Structure of the Mb*(NMH) haem-iron complex

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

---

Optimization:

Genetic

Reaction:

Cyclopropanation

Max TON:

1000

ee:

99

PDB:

6F17

Notes:

Structure of the Mb*(NMH) haem-iron–carbenoid complex

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

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:

---

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:

---

Construction and In Vivo Assembly of a Catalytically Proficient and Hyperthermostable De Novo Enzyme

Metal:

Fe

Ligand type:

Porphyrin

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Oxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

Oxidation of 2,2′-azino-bis(3-ethylbenzothiazo-line-6-sulfonic acid (ABTS)

Coordination Chemistry of Iron(III)-Porphyrin-Antibody Complexes Influence on the Peroxidase Activity of the Axial Coordination of an Imidazole on the Iron Atom

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 13G10

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

kcat/KM = 15200 M-1 * s-1

Coordination Chemistry Studies and Peroxidase Activity of a New Artificial Metalloenzyme Built by the “Trojan Horse” Strategy

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 7A3

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

k1 = 574 M-1 * min-1

Crystal Structure of Two Anti-Porphyrin Antibodies with Peroxidase Activity

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 13G10

Anchoring strategy:

Antibody

Optimization:

Chemical & genetic

Reaction:

Peroxidation

Max TON:

---

ee:

---

PDB:

4AMK

Notes:

---

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 14H7

Anchoring strategy:

Antibody

Optimization:

Chemical & genetic

Reaction:

Peroxidation

Max TON:

---

ee:

---

PDB:

4AMK

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

Enzyme stabilization via computationally guided protein stapling

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Cyclopropanation

Max TON:

4740

ee:

99.2

PDB:

---

Notes:

Stapling of protein via thioether bond formation between the noncanonical amino acid O-2-bromoethyl tyrosine and cysteine

Flavohemoglobin: A Semisynthetic Hydroxylase Acting in the Absence of Reductase

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Hemoglobin

Anchoring strategy:

---

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Helichrome: Synthesis and Enzymatic Activity of a Designed Hemeprotein

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Artificial construct

Anchoring strategy:

Covalent

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

Only 60 amino acids

Hemoabzymes: Towards New Biocatalysts for Selective Oxidations

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 3A3

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

kcat/KM = 33000 M-1 * s-1

Hemozymes Peroxidase Activity Of Artificial Hemoproteins Constructed From the Streptomyces Lividans Xylanase A and Iron(III)-Carboxy-Substituted Porphyrins

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Xylanase A (XynA)

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

kcat/KM = 1083 M-1 * s-1

Incorporation of Manganese Complexes into Xylanase: New Artificial Metalloenzymes for Enantioselective Epoxidation

Metal:

Mn

Ligand type:

Porphyrin

Host protein:

Xylanase A (XynA)

Anchoring strategy:

Supramolecular

Optimization:

---

Reaction:

Epoxidation

Max TON:

21

ee:

80

PDB:

---

Notes:

---

Intramolecular C(sp3)-H Amination of Arylsulfonyl Azides with Engineered and Artificial Myoglobin-Based Catalysts

Metal:

Mn

Ligand type:

Amino acid; Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Metal substitution

Optimization:

Chemical & genetic

Reaction:

C-H activation

Max TON:

142

ee:

---

PDB:

---

Notes:

---

Neocarzinostatin-Based Hybrid Biocatalysts for Oxidation Reactions

Metal:

Fe

Ligand type:

Porphyrin

Anchoring strategy:

Supramolecular

Optimization:

---

Reaction:

Sulfoxidation

Max TON:

6

ee:

13

PDB:

---

Notes:

---

New Activities of a Catalytic Antibody with a Peroxidase Activity: Formation of Fe(II)–RNO Complexes and Stereoselective Oxidation of Sulfides

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 3A3

Anchoring strategy:

Supramolecular

Optimization:

---

Reaction:

Sulfoxidation

Max TON:

82

ee:

45

PDB:

---

Notes:

---