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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:

---

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:

---

A Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin−Streptavidin Technology

Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

14

ee:

11

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

100

ee:

79

PDB:

---

Notes:

---

A Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin−Streptavidin Technology

Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

14

ee:

11

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

100

ee:

79

PDB:

---

Notes:

---

An Artificial Imine Reductase Based on the Ribonuclease S Scaffold

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Ribonuclease S

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

4

ee:

18

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:

---

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:

---

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:

---

Aqueous Phase Transfer Hydrogenation of Aryl Ketones Catalysed by Achiral Ruthenium(II) and Rhodium(III) Complexes and their Papain Conjugates

Metal:

Rh

Ligand type:

Cp*; Poly-pyridine

Host protein:

Papain (PAP)

Anchoring strategy:

Covalent

Optimization:

Chemical

Reaction:

Hydrogenation

Max TON:

96

ee:

15

PDB:

---

Notes:

---

A Rhodium Complex-Linked β-Barrel Protein as a Hybrid Biocatalyst for Phenylacetylene Polymerization

Our group recently prepared a hybrid catalyst containing a rhodium complex, Rh(Cp)(cod), with a maleimide moiety at the peripheral position of the Cp ligand. This compound was then inserted into a β-barrel protein scaffold of a mutant of aponitrobindin (Q96C) via a covalent linkage. The hybrid protein is found to act as a polymerization catalyst and preferentially yields trans-poly(phenylacetylene) (PPA), although the rhodium complex without the protein scaffold normally produces cis PPA.

Metal:

Rh

Ligand type:

COD; Cp*

Host protein:

Nitrobindin (Nb)

Anchoring strategy:

Cystein-maleimide

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin for the Asymmetric Transfer Hydrogenation of an Aryl Ketone – Synthesis, Characterization and Catalytic Activity

Metal:

Rh

Ligand type:

Cp*; Poly-pyridine

Host protein:

ß-lactoglobulin

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Hydrogenation

Max TON:

14

ee:

32

PDB:

---

Notes:

---

Artificial Metalloenzymes for the Diastereoselective Reduction of NAD+ to NAD2H

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

---

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 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:

---

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:

---

Biotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C–H Activation

Metal:

Rh

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

C-H activation

Max TON:

95

ee:

82

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+

Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

970

ee:

13

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

158

ee:

82

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Carbene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Olefin metathesis

Max TON:

105

ee:

---

PDB:

---

Notes:

RCM, biotinylated Hoveyda-Grubbs second generation catalyst

Metal:

---

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Anion-π catalysis

Max TON:

6

ee:

41

PDB:

---

Notes:

No metal

Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

970

ee:

13

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

158

ee:

82

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Carbene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Olefin metathesis

Max TON:

105

ee:

---

PDB:

---

Notes:

RCM, biotinylated Hoveyda-Grubbs second generation catalyst

Metal:

---

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Reaction:

Anion-π catalysis

Max TON:

6

ee:

41

PDB:

---

Notes:

No metal

Computational Insights on an Artificial Imine Reductase Based on the Biotin-Streptavidin Technology

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Genetic

Max TON:

---

ee:

96

PDB:

3PK2

Notes:

Prediction of the enantioselectivity by computational methods.

Cross-Regulation of an Artificial Metalloenzyme

Metal:

Ir

Ligand type:

Cp*; Phenanthroline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

96

ee:

---

PDB:

---

Notes:

Cross-regulated reduction of the antibiotic enrofloxacin by an ArM.

Directed Evolution of an Artificial Imine Reductase

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

380

ee:

95

PDB:

6ESS

Notes:

Salsolidine formation; Sav mutant S112A-N118P-K121A-S122M: (R)-selective

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

220

ee:

85

PDB:

6ESS

Notes:

Salsolidine formation; Sav mutant S112R-N118P-K121A-S122M-L124Y: (S)-selective

Directed Evolution of an Artificial Imine Reductase

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

380

ee:

95

PDB:

6ESS

Notes:

Salsolidine formation; Sav mutant S112A-N118P-K121A-S122M: (R)-selective

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

220

ee:

85

PDB:

6ESS

Notes:

Salsolidine formation; Sav mutant S112R-N118P-K121A-S122M-L124Y: (S)-selective

Efficient in Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

>1980

ee:

---

PDB:

---

Notes:

ArM works in combination with the ene reductase (ER) of the Old Yellow Enzyme family fromThermus scotuductus (TsOYE).

Enantioselective Transfer Hydrogenation of Ketone Catalysed by Artificial Metalloenzymes Derived from Bovine β-Lactoglobulin

Metal:

Rh

Ligand type:

Cp*; Poly-pyridine

Host protein:

ß-lactoglobulin

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Hydrogenation

Max TON:

34

ee:

26

PDB:

---

Notes:

---

Evaluation of Chemical Diversity of Biotinylated Chiral 1,3-Diamines as a Catalytic Moiety in Artificial Imine Reductase

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

>99

ee:

83

PDB:

3PK2

Notes:

---

Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

188

ee:

43

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino carboxylic acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4

ee:

21

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Pyrazine amide

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

26

ee:

16

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

12

ee:

13

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Oxazoline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

102

ee:

14

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

94

ee:

67

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino amide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

10

ee:

7

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino carboxylic acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

8

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Pyrazine amide

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4

ee:

6

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Oxazoline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

8

ee:

0

PDB:

---

Notes:

---

Expanding the Chemical Diversity in Artificial Imine Reductases Based on the Biotin–Streptavidin Technology

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

188

ee:

43

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino carboxylic acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4

ee:

21

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Pyrazine amide

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

26

ee:

16

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

0

ee:

---

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

12

ee:

13

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Cp*; Oxazoline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

102

ee:

14

PDB:

---

Notes:

---

Metal:

Ir

Ligand type:

Amino acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

94

ee:

67

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino amide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

10

ee:

7

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino carboxylic acid; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

8

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Diamine

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Pyrazine amide

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Bipyridine; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

4

ee:

6

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Amino-sulfonamide; Cp*

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

6

ee:

1

PDB:

---

Notes:

---

Metal:

Rh

Ligand type:

Cp*; Oxazoline

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

8

ee:

0

PDB:

---

Notes:

---