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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.

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

An Artificial Metalloenzyme for Olefin Metathesis

A Grubbs–Hoveyda type olefin metathesis catalyst, equipped with an electrophilic bromoacetamide group, was used to modify a cysteine-containing variant of a small heat shock protein from Methanocaldococcus jannaschii. The resulting artificial metalloenzyme was found to be active under acidic conditions in a benchmark ring closing metathesis reaction.

Metal:

Ru

Ligand type:

Carbene

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Olefin metathesis

Max TON:

25

ee:

---

PDB:

---

Notes:

RCM

Artificial Metalloenzymes Based on the Biotin-Avidin Technology: Enantioselective Catalysis and Beyond

Review

Notes:

---

Artificial Metalloenzymes for Olefin Metathesis Based on the Biotin-(Strept)Avidin Technology

Metal:

Ru

Ligand type:

Carbene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Olefin metathesis

Max TON:

14

ee:

---

PDB:

---

Notes:

RCM

Metal:

Ru

Ligand type:

Carbene

Host protein:

Avidin (Av)

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Olefin metathesis

Max TON:

19

ee:

---

PDB:

---

Notes:

RCM

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:

---

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

Bioinspired Catalyst Design and Artificial Metalloenzymes

Review

Notes:

---

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:

---

Chemically Engineered Papain as Artificial Formate Dehydrogenase for NAD(P)H Regeneration

Metal:

Rh

Ligand type:

Cp*; Poly-pyridine

Host protein:

Papain (PAP)

Anchoring strategy:

Covalent

Optimization:

Chemical

Reaction:

Hydrogenation

Max TON:

---

ee:

---

PDB:

---

Notes:

TOF = 52.1 h-1 for NAD+

Covalent Anchoring of a Racemization Catalyst to CALB-Beads: Towards Dual Immobilization of DKR Catalysts

Metal:

Ru

Anchoring strategy:

Covalent

Optimization:

Chemical

Reaction:

Acylation

Max TON:

---

ee:

>99%

PDB:

---

Notes:

Lipase CALB is immobilized on a solid support (Novozym®435). Dynamic kinetic resolution (DKR) of 1-phenylethanol to the acylated product.

Covalent Versus Non-covalent (Biocatalytic) Approaches for Enantioselective Sulfoxidation Catalyzed by Corrole Metal Complexes

Metal:

Mn

Ligand type:

Corrole

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Reaction:

Sulfoxidation

Max TON:

45

ee:

70

PDB:

---

Notes:

---

Definite Coordination Arrangement of Organometallic Palladium Complexes Accumulated on the Designed Interior Surface of Apo-Ferritin

Metal:

Pd

Ligand type:

Allyl

Host protein:

Ferritin

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Suzuki coupling

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Design of a Switchable Eliminase

Metal:

Ca

Ligand type:

Amino acid

Anchoring strategy:

Dative

Optimization:

Genetic

Reaction:

Kemp elimination

Max TON:

>40

ee:

---

PDB:

2KZ2

Notes:

Ca acts as allosteric regulator, catalytically active site contains no metal

Dual Modification of a Triple-Stranded β-Helix Nanotube with Ru and Re Metal Complexes to Promote Photocatalytic Reduction of CO2

Metal:

Re

Ligand type:

Bipyridine; CO

Host protein:

[(gp5βf)3]2

Anchoring strategy:

Cystein-maleimide

Optimization:

---

Reaction:

CO2 reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Bipyridine

Host protein:

[(gp5βf)3]2

Anchoring strategy:

Lysine-succinimide

Optimization:

Genetic

Reaction:

CO2 reduction

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Hydrolytic Catalysis and Structural Stabilization in a Designed Metalloprotein

Metal:

Hg; Zn

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

>10

ee:

---

PDB:

3PBJ

Notes:

Zn ion for catalytic activity, Hg ion for structural stability of the ArM. PDB ID 3PBJ = Structure of an analogue.

Metal:

Hg; Zn

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

---

ee:

---

PDB:

3PBJ

Notes:

Zn ion for catalytic activity, Hg ion for structural stability of the ArM, kcat/KM ≈ 1.8*105 M-1*s-1. PDB ID 3PBJ = Structure of an analogue.

Merging the Best of Two Worlds: Artificial Metalloenzymes for Enantioselective Catalysis

Review

Notes:

---

Nature-Driven Photochemistry for Catalytic Solar Hydrogen Production: A Photosystem I-Transition Metal Catalyst Hybrid

Metal:

Co

Ligand type:

Oxime; Pyridine

Host protein:

Photosystem I (PSI)

Anchoring strategy:

Undefined

Optimization:

---

Reaction:

H2 evolution

Max TON:

2080

ee:

---

PDB:

---

Notes:

Recalculated TON

OsO4·Streptavidin: A Tunable Hybrid Catalyst for the Enantioselective cis-Dihydroxylation of Olefins

Metal:

Os

Ligand type:

Undefined

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Dihydroxylation

Max TON:

16

ee:

97

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:

---

The Important Role of Covalent Anchor Positions in Tuning Catalytic Properties of a Rationally Designed MnSalen-Containing Metalloenzyme

Metal:

Mn

Ligand type:

Salen

Host protein:

Myoglobin (Mb)

Anchoring strategy:

Covalent

Optimization:

Genetic

Reaction:

Sulfoxidation

Max TON:

---

ee:

83

PDB:

---

Notes:

Reaction rate: 2.3 min-1