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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 clearMyoglobin (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:

---

Addressable DNA–Myoglobin Photocatalysis

A hybrid myoglobin, containing a single‐stranded DNA anchor and a redox‐active ruthenium moiety tethered to the heme center can be used as a photocatalyst. The catalyst can be selectively immobilized on a surface‐bound complementary DNA molecule and thus readily recycled from complex reaction mixtures. This principle may be applied to a range of heme‐dependent enzymes allowing the generation of novel light‐triggered photocatalysts. Photoactivatable myoglobin containing a DNA oligonucleotide as a structural anchor was designed by using the reconstitution of artificial heme moieties containing Ru3+ ions. This semisynthetic DNA–enzyme conjugate was successfully used for the oxidation of peroxidase substrates by using visible light instead of H2O2 for the activation. The DNA anchor was utilized for the immobilization of the enzyme on the surface of magnetic microbeads. Enzyme activity measurements not only indicated undisturbed biofunctionality of the tethered DNA but also enabled magnetic separation‐based enrichment and recycling of the photoactivatable biocatalyst.

Metal:

Ru

Ligand type:

Bipyridine

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

---

Reaction:

Photooxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

Horse heart myoglobin

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 Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme

Terminal oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, most biomimetic catalysts have much lower activity than native oxidases. Herein we report a designed oxidase in myoglobin with an O2 reduction rate (52 s–1) comparable to that of a native cytochrome (cyt) cbb3 oxidase (50 s–1) under identical conditions. We achieved this goal by engineering more favorable electrostatic interactions between a functional oxidase model designed in sperm whale myoglobin and its native redox partner, cyt b5, resulting in a 400-fold electron transfer (ET) rate enhancement. Achieving high activity equivalent to that of native enzymes in a designed metalloenzyme offers deeper insight into the roles of tunable processes such as ET in oxidase activity and enzymatic function and may extend into applications such as more efficient oxygen reduction reaction catalysts for biofuel cells.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

O2 reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

O2 reduction rates of 52 s-1 were achieved in combination with the native redox partner cyt b5.

A 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

A Site-Selective Dual Anchoring Strategy for Artificial Metalloprotein Design

Introducing nonnative metal ions or metal-containing prosthetic groups into a protein can dramatically expand the repertoire of its functionalities and thus its range of applications. Particularly challenging is the control of substrate-binding and thus reaction selectivity such as enantioselectivity. To meet this challenge, both non-covalent and single-point attachments of metal complexes have been demonstrated previously. Since the protein template did not evolve to bind artificial metal complexes tightly in a single conformation, efforts to restrict conformational freedom by modifying the metal complexes and/or the protein are required to achieve high enantioselectivity using the above two strategies. Here we report a novel site-selective dual anchoring (two-point covalent attachment) strategy to introduce an achiral manganese salen complex (Mn(salen)), into apo sperm whale myoglobin (Mb) with bioconjugation yield close to 100%. The enantioselective excess increases from 0.3% for non-covalent, to 12.3% for single point, and to 51.3% for dual anchoring attachments. The dual anchoring method has the advantage of restricting the conformational freedom of the metal complex in the protein and can be generally applied to protein incorporation of other metal complexes with minimal structural modification to either the metal complex or the protein.

Metal:

Mn

Ligand type:

Salen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Covalent

Optimization:

Genetic

Reaction:

Sulfoxidation

Max TON:

3.9

ee:

51

PDB:

1MBO

Notes:

Sperm whale myoglobin

Bimetallic Copper-Heme-Protein-DNA Hybrid Catalyst for Diels Alder Reaction

Metal:

Cu

Ligand type:

Bipyridine

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

7.1

ee:

18

PDB:

---

Notes:

Horse heart myoglobin

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 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

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

Cobaloxime-Based Artificial Hydrogenase

Metal:

Co

Ligand type:

Oxime

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

H2 evolution

Max TON:

5

ee:

---

PDB:

---

Notes:

Sperm whale myoglobin

Coordinated Design of Cofactor and Active Site Structures in Development of New Protein Catalysts

Metal:

Mn

Ligand type:

Salophen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

1V9Q

Notes:

---

Metal:

Cr

Ligand type:

Salophen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

1V9Q

Notes:

---

Metal:

Mn

Ligand type:

Salen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Metal:

Cr

Ligand type:

Salen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

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:

---

C(sp3)–H Bond Hydroxylation Catalyzed by Myoglobin Reconstituted with Manganese Porphycene

Metal:

Mn

Ligand type:

Porphycene

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

---

Reaction:

Hydroxylation

Max TON:

---

ee:

---

PDB:

2WI8

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

Hybridization of Modified-Heme Reconstitution and Distal Histidine Mutation to Functionalize Sperm Whale Myoglobin

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Genetic

Max TON:

---

ee:

---

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:

---

Introducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase Activity

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

320

ee:

---

PDB:

3MN0

Notes:

Sperm whale myoglobin

Manganese(V) Porphycene Complex Responsible for Inert C–H Bond Hydroxylation in a Myoglobin Matrix

Metal:

Mn

Ligand type:

Amino acid; Porphycene

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

---

Reaction:

Hydroxylation

Max TON:

13

ee:

---

PDB:

5YL3

Notes:

---

Meso-Unsubstituted Iron Corrole in Hemoproteins: Remarkable Differences in Effects on Peroxidase Activities between Myoglobin and Horseradish Peroxidase

Metal:

Fe

Ligand type:

Corrole

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Metal:

Fe

Ligand type:

Corrole

Anchoring strategy:

Reconstitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Noncovalent Modulation of pH-Dependent Reactivity of a Mn–Salen Cofactor in Myoglobin with Hydrogen Peroxide

Metal:

Mn

Ligand type:

Salen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Covalent

Optimization:

Chemical & genetic

Reaction:

Sulfoxidation

Max TON:

4.1

ee:

50

PDB:

---

Notes:

Sperm whale myoglobin

Peroxidase Activity of Myoglobin is Enhanced by Chemical Mutation of Heme-Propionates

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Precise Design of Artificial Cofactors for Enhancing Peroxidase Activity of Myoglobin: Myoglobin Mutant H64D Reconstituted with a “Single-Winged Cofactor” is Equivalent to Native Horseradish Peroxidase in Oxidation Activity

Metal:

Fe

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Preparation of Artificial Metalloenzymes by Insertion of Chromium(III) Schiff Base Complexes into apo-Myoglobin Mutants

Metal:

Cr

Ligand type:

Salophen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Reconstitution

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Protein Scaffold of a Designed Metalloenzyme Enhances the Chemoselectivity in Sulfoxidation of Thioanisole

Metal:

Mn

Ligand type:

Salen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Sulfoxidation

Max TON:

5.2

ee:

60

PDB:

---

Notes:

Sperm whale myoglobin

Protein Secondary-Shell Interactions Enhance the Photoinduced Hydrogen Production of Cobalt Protoporphyrin IX

Metal:

Co

Ligand type:

Porphyrin

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Metal substitution

Optimization:

Genetic

Reaction:

H2 evolution

Max TON:

518

ee:

---

PDB:

---

Notes:

---

Rational Design of a Structural and Functional Nitric Oxide Reductase

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

NO reduction

Max TON:

~5

ee:

---

PDB:

3K9Z

Notes:

Design of a catalytically active non-haem iron-binding site (FeB) in sperm whale myoglobin.

Roles of Glutamates and Metal Ions in a Rationally Designed Nitric Oxide Reductase Based on Myoglobin

Metal:

Fe

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

NO reduction

Max TON:

---

ee:

---

PDB:

3M39

Notes:

X-ray structure of mutant I107E.

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

NO reduction

Max TON:

---

ee:

---

PDB:

3M39

Notes:

X-ray structure of mutant I107E.

Significant Improvement of Oxidase Activity Through the Genetic Incorporation of a Redox-Active Unnatural Amino Acid

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

O2 reduction

Max TON:

>1100

ee:

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PDB:

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Notes:

Reduction potential was lowered by incorporation of the unnatural amino acid 3-methoxy tyrosine.