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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.

Achiral Cyclopentadienone Iron Tricarbonyl Complexes Embedded in Streptavidin: An Access to Artificial Iron Hydrogenases and Application in Asymmetric Hydrogenation

We report on the synthesis of biotinylated (cyclopentadienone)iron tricarbonyl complexes, the in situ generation of the corresponding streptavidin conjugates and their application in asymmetric hydrogenation of imines and ketones.

Metal:

Fe

Ligand type:

CO; Cyclopentadienone

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Hydrogenation

Max TON:

20

ee:

34

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 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

A Hydrogenase Model System Based on the Sequence of Cytochrome c: Photochemical Hydrogen Evolution in Aqueous Media

The diiron carbonyl cluster is held by a native CXXC motif, which includes Cys14 and Cys17, in the cytochrome c sequence. It is found that the diiron carbonyl complex works well as a catalyst for H2 evolution. It has a TON of ∼80 over 2 h at pH 4.7 in the presence of a Ru-photosensitizer and ascorbate as a sacrificial reagent in aqueous media.

Metal:

Fe

Ligand type:

Carbonyl

Host protein:

Cytochrome c

Anchoring strategy:

Dative

Optimization:

---

Reaction:

H2 evolution

Max TON:

82

ee:

---

PDB:

---

Notes:

Horse heart cytochrome C

Alteration of the Oxygen-Dependent Reactivity of De Novo Due Ferri Proteins

De novo proteins provide a unique opportunity to investigate the structure–function relationships of metalloproteins in a minimal, well-defined and controlled scaffold. Here, we describe the rational programming of function in a de novo designed di-iron carboxylate protein from the Due Ferri family. Originally created to catalyse the O2-dependent, two-electron oxidation of hydroquinones, the protein was reprogrammed to catalyse the selective N-hydroxylation of arylamines by remodelling the substrate access cavity and introducing a critical third His ligand to the metal-binding cavity. Additional second- and third-shell modifications were required to stabilize the His ligand in the core of the protein. These structural changes resulted in at least a 106-fold increase in the relative rate between the arylamine N-hydroxylation and hydroquinone oxidation reactions. This result highlights the potential for using de novo proteins as scaffolds for future investigations of the geometric and electronic factors that influence the catalytic tuning of di-iron active sites.

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

N-Hydroxylation

Max TON:

---

ee:

---

PDB:

2LFD

Notes:

---

A Metal Ion Regulated Artificial Metalloenzyme

Regulation of enzyme activity is essential in living cells. The rapidly increasing number of designer enzymes with new-to-nature activities makes it necessary to develop novel strategies for controlling their catalytic activity. Here we present the development of a metal ion regulated artificial metalloenzyme created by combining two anchoring strategies, covalent and supramolecular, for introducing a regulatory and a catalytic site, respectively. This artificial metalloenzyme is activated in the presence of Fe2+ ions, but only marginally in the presence of Zn2+.

Metal:

Fe

Ligand type:

Bypyridine

Host protein:

LmrR

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

14

ee:

75

PDB:

---

Notes:

---

Metal:

Zn

Ligand type:

Bypyridine

Host protein:

LmrR

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

6

ee:

80

PDB:

---

Notes:

---

An Artificial Di-Iron Oxo-Orotein with Phenol Oxidase Activity

Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol-binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Sufficient stability was, however, obtained by optimizing the sequence of a loop distant from the active site.

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Alcohol oxidation

Max TON:

>50

ee:

---

PDB:

2KIK

Notes:

kcat/KM ≈ 1380 M-1*min-1

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Amine oxidation

Max TON:

---

ee:

---

PDB:

2KIK

Notes:

kcat/KM ≈ 83 M-1*min-1

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 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 Oxygenase Built from Scratch: Substrate Binding Site Identified Using a Docking Approach

The substrate for an artificial iron monooxygenase was selected by using docking calculations. The high catalytic efficiency of the reported enzyme for sulfide oxidation was directly correlated to the predicted substrate binding mode in the protein cavity, thus illustrating the synergetic effect of the substrate binding site, protein scaffold, and catalytic site.

Metal:

Fe

Ligand type:

BPMCN; BPMEN

Host protein:

NikA

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Sulfoxidation

Max TON:

199

ee:

≤5

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

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 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 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

A Structural View of Synthetic Cofactor Integration into [FeFe]-Hydrogenases

Metal:

Fe

Ligand type:

CN; CO; Dithiolate

Anchoring strategy:

Dative

Optimization:

Chemical

Reaction:

H2 evolution

Max TON:

---

ee:

---

PDB:

4XDC

Notes:

H2 evolution activity of the ArM: 2874 (mmol H2)*min-1*(mg protein)-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

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

Catalysis Without a Headache: Modification of Ibuprofen for the Design of Artificial Metalloenzyme for Sulfide Oxidation

Metal:

Fe

Ligand type:

BPHMEN

Anchoring strategy:

Supramolecular

Optimization:

---

Reaction:

Sulfoxidation

Max TON:

1367

ee:

---

PDB:

---

Notes:

---

Catalytic Cyclopropanation by Myoglobin Reconstituted with Iron Porphycene: Acceleration of Catalysis due to Rapid Formation of the Carbene Species

Metal:

Fe

Ligand type:

Amino acid; Porphycene

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

---

Reaction:

Cyclopropanation

Max TON:

---

ee:

---

PDB:

---

Notes:

Cyclopropanation of styrene with ethyl diazoacetate: kcat/KM = 1.3 mM-1 * s-1, trans/cis = 99:1

Chalcogenide Substitution in the [2Fe] Cluster of [FeFe]-Hydrogenases Conserves High Enzymatic Activity

Metal:

Fe

Ligand type:

CN; CO; Diselenolate

Anchoring strategy:

Dative

Optimization:

Chemical

Reaction:

H2 evolution

Max TON:

---

ee:

---

PDB:

5OEF

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

Cross-Linked Artificial Enzyme Crystals as Heterogeneous Catalysts for Oxidation Reactions

Metal:

Fe

Ligand type:

---

Host protein:

NikA

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Max TON:

28000

ee:

---

PDB:

5ON0

Notes:

Cross-Linked Enzyme Crystals (CLEC) as catalysts.

Metal:

Fe

Ligand type:

---

Host protein:

NikA

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Max TON:

5900

ee:

---

PDB:

5ON0

Notes:

Cross-Linked Enzyme Crystals (CLEC) as catalysts.

Crystal Structure and Peroxidase Activity of Myoglobin Reconstituted with Iron Porphycene

Metal:

Fe

Ligand type:

Porphycene

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

1MBI

Notes:

---

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:

---

De Novo Design of Catalytic Proteins

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Due Ferro 1

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Alcohol oxidation

Max TON:

>100

ee:

---

PDB:

---

Notes:

kcat/KM ≈ 1540 M-1*min-1

Design of Metal Cofactors Activated by a Protein–Protein Electron Transfer System

Metal:

Fe

Ligand type:

Salophen

Host protein:

Heme oxygenase (HO)

Anchoring strategy:

Reconstitution

Optimization:

Chemical

Reaction:

O2 reduction

Max TON:

---

ee:

---

PDB:

1WZD

Notes:

---

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:

---