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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 clearProc. 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 Cofactor Approach to Copper-Dependent Catalytic Antibodies

A strategy for the preparation of semisynthetic copper(II)-based catalytic metalloproteins is described in which a metal-binding bis-imidazole cofactor is incorporated into the combining site of the aldolase antibody 38C2. Antibody 38C2 features a large hydrophobic-combining site pocket with a highly nucleophilic lysine residue, LysH93, that can be covalently modified. A comparison of several lactone and anhydride reagents shows that the latter are the most effective and general derivatizing agents for the 38C2 Lys residue. A bis-imidazole anhydride (5) was efficiently prepared from N-methyl imidazole. The 38C2–5-Cu conjugate was prepared by either (i) initial derivatization of 38C2 with 5 followed by metallation with CuCl2, or (ii) precoordination of 5 with CuCl2 followed by conjugation with 38C2. The resulting 38C2–5-Cu conjugate was an active catalyst for the hydrolysis of the coordinating picolinate ester 11, following Michaelis–Menten kinetics [kcat(11) = 2.3 min−1 and Km(11) 2.2 mM] with a rate enhancement [kcat(11)kuncat(11)] of 2.1 × 105. Comparison of the second-order rate constants of the modified 38C2 and the Cu(II)-bis-imidazolyl complex k(6-CuCl2) gives a rate enhancement of 3.5 × 104 in favor of the antibody complex with an effective molarity of 76.7 M, revealing a significant catalytic benefit to the binding of the bis-imidazolyl ligand into 38C2.

Metal:

Cu

Ligand type:

Bisimidazol

Host protein:

Antibody 38C2

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

---

Artificial Metalloenzymes Based on Biotin-Avidin Technology for the Enantioselective Reduction of Ketones by Transfer Hydrogenation

Metal:

Ru

Ligand type:

Amino-sulfonamide; P-cymene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

92

ee:

94

PDB:

---

Notes:

---

Metal:

Ru

Ligand type:

Amino-sulfonamide; Benzene

Host protein:

Streptavidin (Sav)

Anchoring strategy:

Supramolecular

Optimization:

Chemical & genetic

Max TON:

30

ee:

63

PDB:

---

Notes:

---

Conversion of a Helix-Turn-Helix Motif Sequence-Specific DNA Binding Protein into a Site-Specific DNA Cleavage Agent

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Oxidative cleavage

Max TON:

<1

ee:

---

PDB:

---

Notes:

Engineered sequence specificity

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

Designing a Functional Type 2 Copper Center that has Nitrite Reductase Activity Within α-Helical Coiled Coils

Metal:

Cu

Ligand type:

Amino acid

Host protein:

TRI peptide

Anchoring strategy:

Dative

Optimization:

Chemical & genetic

Max TON:

>5

ee:

---

PDB:

---

Notes:

Nitrite reduction

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

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

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.