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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.

An asymmetric catalyst

Asymmetric synthesis has hitherto succeeded only by using reagents or solvents having the asymmetric configuration.

Metal:

Pd

Ligand type:

Undefined

Host protein:

Silk fibroin fibre

Anchoring strategy:

Undefined

Optimization:

---

Reaction:

Hydrogenation

Max TON:

>22

ee:

---

PDB:

---

Notes:

---

Catalytic Properties and Specificity of the Extracellular Nuclease of Staphylococcus Aureus

Metal:

Sr

Ligand type:

Amino acid

Host protein:

Nuclease from S. aureus

Anchoring strategy:

Metal substitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

DNA cleavage

Metal Ion Dependent Binding of Sulphonamide to Carbonic Anhydrase

Metal:

Co

Ligand type:

Amino acid

Host protein:

Human carbonic anhydrase

Anchoring strategy:

Metal substitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

CO2 hydration

Metal:

Co

Ligand type:

Amino acid

Host protein:

Human carbonic anhydrase

Anchoring strategy:

Metal substitution

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

Ester cleavage

Rare Earth Metal Ions as Probes of Calcium Binding Sites in Proteins: Neodynium Acceleration of the Activation of Trypsinogen

Metal:

Nd

Ligand type:

Amino acid

Host protein:

Trypsin

Anchoring strategy:

Metal substitution

Optimization:

---

Max TON:

<1

ee:

---

PDB:

---

Notes:

---

Studies on the Oxidase Activity of Copper (II) Carboxypeptidase A

Metal:

Cu

Ligand type:

Amino acid

Host protein:

Carboxypeptidase A

Anchoring strategy:

Metal substitution

Optimization:

---

Reaction:

Oxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

Oxidation of vitamin C

Conversion of a Protein to a Homogeneous Asymmetric Hydrogenation Catalyst by Site-Specific Modification with a Diphosphinerhodium (I) Moiety

Metal:

Rh

Ligand type:

Phosphine

Host protein:

Avidin (Av)

Anchoring strategy:

Supramolecular

Optimization:

---

Reaction:

Hydrogenation

Max TON:

500

ee:

41

PDB:

---

Notes:

---

The Bovine Serum Albumin-2-Phenylpropane-1,2-diolatodioxoosmium(VI) Complex as an Enantioselective Catalyst for cis-Hydroxylation of Alkenes

Metal:

Os

Ligand type:

Undefined

Anchoring strategy:

Undefined

Optimization:

---

Reaction:

Dihydroxylation

Max TON:

40

ee:

68

PDB:

---

Notes:

---

Chemical Conversion of a DNA-Binding Protein into a Site-Specific Nuclease

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Oxidative cleavage

Max TON:

<1

ee:

---

PDB:

---

Notes:

Engineered sequence specificity

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:

---

Generation of a Hybrid Sequence-Specific Single Stranded Deoxyribonuclease

Metal:

Ca

Ligand type:

Undefined

Host protein:

Staphylococcal nuclease

Anchoring strategy:

---

Optimization:

---

Max TON:

<1

ee:

---

PDB:

---

Notes:

Engineered sequence specificity

Synthesis of a Sequence-Specific DNA-Cleaving Peptide

Metal:

Fe

Ligand type:

EDTA

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

DNA cleavage

Max TON:

<1

ee:

---

PDB:

---

Notes:

Engineered sequence specificity

Helichrome: Synthesis and Enzymatic Activity of a Designed Hemeprotein

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Artificial construct

Anchoring strategy:

Covalent

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

Only 60 amino acids

Sequence-Specific Peptide Cleavage Catalyzed by an Antibody

Metal:

Zn

Ligand type:

Tetramine

Host protein:

Antibody 28F11

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Max TON:

400

ee:

---

PDB:

---

Notes:

---

Autoxidation of Ascorbic Acid Catalyzed by a Semisynthetic Enzyme

Metal:

Cu

Ligand type:

Bipyridine

Host protein:

Papain (PAP)

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Oxidation

Max TON:

---

ee:

---

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

Peroxidase Activity of an Antibody-Heme Complex

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody7G12-A10-G1-A12

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

200-500

ee:

---

PDB:

---

Notes:

---

Towards Antibody-Mediated Metallo-Porphyrin Chemistry

Metal:

Mn

Ligand type:

Porphyrin

Host protein:

Antibody

Anchoring strategy:

Supramolecular

Optimization:

---

Max TON:

549

ee:

---

PDB:

---

Notes:

---

A Highly Specific Metal-Activated Catalytic Antibody

n/a

Metal:

Zn

Ligand type:

Undefined

Host protein:

IgG 84A3

Anchoring strategy:

Undefined

Optimization:

---

Max TON:

---

ee:

---

PDB:

---

Notes:

Substrate specificty

Semisynthesis of Bipyridyl-Alanine Cytochrome c Mutants: Novel Proteins with Enhanced Electron-Transfer Properties

Metal:

Fe; Ru

Ligand type:

Bipyridine; Porphyrin

Host protein:

Horse heart cytochrome c

Anchoring strategy:

Covalent

Optimization:

---

Reaction:

Electron transfer

Max TON:

---

ee:

---

PDB:

---

Notes:

No catalysis

Engineered Metal Regulation of Trypsin Specificity

Metal:

Zn

Ligand type:

Amino acid

Host protein:

Trypsin

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

Substrate specificty

Metal:

Ni

Ligand type:

Amino acid

Host protein:

Trypsin

Anchoring strategy:

Dative

Optimization:

Genetic

Max TON:

---

ee:

---

PDB:

---

Notes:

Substrate specificty

Thermostable Peroxidase-Activity with a Recombinant Antibody L-Chain-Porphyrin Fe(III) Complex

Metal:

Fe

Ligand type:

Porphyrin

Anchoring strategy:

Antibody

Optimization:

---

Reaction:

Peroxidation

Max TON:

---

ee:

---

PDB:

---

Notes:

---

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 Semisynthetic Metalloenzyme based on a Protein Cavity that Catalyzes the Enantioselective Hydrolysis of Ester and Amide Substrates

In an effort to prepare selective and efficient catalysts for ester and amide hydrolysis, we are designing systems that position a coordinated metal ion within a defined protein cavity. Here, the preparation of a protein-1,10-phenanthroline conjugate and the hydrolytic chemistry catalyzed by this construct are described. Iodoacetamido-1,10-phenanthroline was used to modify a unique cysteine residue in ALBP (adipocyte lipid binding protein) to produce the conjugate ALBP-Phen. The resulting material was characterized by electrospray mass spectrometry, UV/vis and fluorescence spectroscopy, gel filtration chromatography, and thiol titration. The stability of ALBP-Phen was evaluated by guanidine hydrochloride denaturation experiments, and the ability of the conjugate to bind Cu(II) was demonstrated by fluorescence spectroscopy. ALBP-Phen-Cu(II) catalyzes the enantioselective hydrolysis of several unactivated amino acid esters under mild conditions (pH 6.1, 25 °C) at rates 32−280-fold above the background rate in buffered aqueous solution. In 24 h incubations 0.70 to 7.6 turnovers were observed with enantiomeric excesses ranging from 31% ee to 86% ee. ALBP-Phen-Cu(II) also promotes the hydrolysis of an aryl amide substrate under more vigorous conditions (pH 6.1, 37 °C) at a rate 1.6 × 104-fold above the background rate. The kinetics of this amide hydrolysis reaction fit the Michaelis−Menten relationship characteristic of enzymatic processes. The rate enhancements for ester and amide hydrolysis reported here are 102−103 lower than those observed for free Cu(II) but comparable to those previously reported for Cu(II) complexes.

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

---

Max TON:

1 to 8

ee:

39 to 86

PDB:

---

Notes:

---

Peroxidation of Pyrogallol by Antibody−Metalloporphyrin Complexes

Metal:

Mn

Ligand type:

Porphyrin

Host protein:

Antibody 03-1

Anchoring strategy:

Antibody

Optimization:

---

Max TON:

200

ee:

---

PDB:

---

Notes:

---

Metal:

Fe

Ligand type:

Porphyrin

Host protein:

Antibody 03-1

Anchoring strategy:

Antibody

Optimization:

---

Max TON:

300

ee:

---

PDB:

---

Notes:

---

Pyridoxamine-Amino Acid Chimeras in Semisynthetic Aminotransferase Mimics

Metal:

Cu

Ligand type:

Undefined

Host protein:

RNase A

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Transamination

Max TON:

---

ee:

31

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:

---

Enantioselective Sulfoxidation Mediated by Vanadium-Incorporated Phytase: A Hydrolase Acting as a Peroxidase

Metal:

V

Ligand type:

Undefined

Host protein:

Phytase

Anchoring strategy:

Undefined

Optimization:

---

Reaction:

Sulfoxidation

Max TON:

~194

ee:

66

PDB:

---

Notes:

---

Metal:

V

Ligand type:

Oxide

Host protein:

Phytase

Anchoring strategy:

Undefined

Optimization:

---

Reaction:

Sulfoxidation

Max TON:

550

ee:

66

PDB:

---

Notes:

---

Hemoabzymes - Different Strategies for Obtaining Artificial Hemoproteins based on Antibodies

Review

Notes:

---

Antibody-Metalloporphyrin Catalytic Assembly Mimics Natural Oxidation Enzymes

Metal:

Ru

Ligand type:

Porphyrin

Host protein:

Antibody SN37.4

Anchoring strategy:

Supramolecular

Optimization:

Chemical

Reaction:

Sulfoxidation

Max TON:

750

ee:

43

PDB:

---

Notes:

---

Artificial Metalloenzymes based on Protein Cavities: Exploring the Effect of Altering the Metal Ligand Attachment Position by Site Directed Mutagenesis

Metal:

Cu

Ligand type:

Phenanthroline

Anchoring strategy:

Covalent

Optimization:

Genetic

Max TON:

1 to 4

ee:

61 to 94

PDB:

---

Notes:

Varied attachment position