398 publications

398 publications

An asymmetric catalyst

Akabori, S.; Sakurai, S.

Nature, 1956, 10.1038/178323b0

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

Cuatrecasas, P.

J. Biol. Chem., 1967, PMID 4290246


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

Coleman, J. E.

Nature, 1967, 10.1038/214193a0


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

Birnbaum, E. R.; Darnall, D. W.

J. Biol. Chem., 1970, PMID 5484822


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

Kaiser, E. T.

J. Chem. Soc., Chem. Commun., 1976, 10.1039/C39760000830


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

Whitesides, G. M.

J. Am. Chem. Soc., 1978, 10.1021/ja00469a064


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

Kokubo, T.; Okano, M.

J. Chem. Soc., Chem. Commun., 1983, 10.1039/C39830000769


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

Sigman, D. S.

Science, 1987, 10.1126/science.2820056


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

Kaiser, E. T.

J. Am. Chem. Soc., 1987, 10.1021/ja00236a062


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

Schultz, P. G.

Science, 1987, 10.1126/science.3685986


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

Dervan, P. B.

Science, 1987, 10.1126/science.3120311


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

Kaiser, E. T.; Sasaki, T.

J. Am. Chem. Soc., 1989, 10.1021/ja00183a065


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

Lerner, R. A.

Science, 1989, 10.1126/science.2922606


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

Kaiser, E. T.

Biopolymers, 1990, 10.1002/bip.360290107


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

Ebright, R. H.; Gunasekeram, A.

Proc. Natl. Acad. Sci. U. S. A., 1990, 10.1073/pnas.87.8.2882


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

Schultz, P. G.

J. Am. Chem. Soc., 1990, 10.1021/ja00181a065


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

Keinan, E.

Pure Appl. Chem., 1990, 10.1351/pac199062102013


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

Janda, K. D.; Lerner, R. A.

J. Am. Chem. Soc., 1993, 10.1021/ja00064a068

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

Gray, H. B.; Imperiali, B.

J. Am. Chem. Soc., 1993, 10.1021/ja00071a068


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

Craik, C. S.

Biochemistry, 1995, 10.1021/bi00007a010


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

Imanaka, T.

FEBS Lett., 1995, 10.1016/0014-5793(95)01224-3


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

Mahy, J.-P.

FEBS Lett., 1996, 10.1016/0014-5793(96)01006-X


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

Distefano, M. D.

J. Am. Chem. Soc., 1997, 10.1021/JA970820K

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

Harada, A.

Inorg. Chem., 1997, 10.1021/ic9610849


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

Imperiali, B.

Prot. Eng., 1997, 10.1093/protein/10.6.691


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

Mahy, J.-P.

Eur. J. Biochem., 1998, 10.1046/j.1432-1327.1998.2570121.x

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

Sheldon, R. A.

Chem. Commun., 1998, 10.1039/a804702b


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

Mahy, J.-P.

Appl. Biochem. Biotechnol., 1998, 10.1007/Bf02787712


Notes: ---

Antibody-Metalloporphyrin Catalytic Assembly Mimics Natural Oxidation Enzymes

Keinan, E.

J. Am. Chem. Soc., 1999, 10.1021/ja990314q


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

Distefano, M. D.

Bioorg. Med. Chem. Lett., 1999, 10.1016/S0960-894X(98)00684-2


Metal: Cu
Ligand type: Phenanthroline
Anchoring strategy: Covalent
Optimization: Genetic
Max TON: 1 to 4
ee: 61 to 94
PDB: ---
Notes: Varied attachment position