79 publications

79 publications

8-Amino-5,6,7,8-tetrahydroquinoline in Iridium(III) Biotinylated Cp* Complex as Artificial Imine Reductase

Rimoldi, I.

New J. Chem., 2018, 10.1039/C8NJ04558E

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: ---

Abiological Catalysis by Artificial Haem Proteins Containing Noble Metals in Place of Iron

Hartwig, J. F.

Nature, 2016, 10.1038/nature17968

Enzymes that contain metal ions—that is, metalloenzymes—possess the reactivity of a transition metal centre and the potential of molecular evolution to modulate the reactivity and substrate-selectivity of the system1. By exploiting substrate promiscuity and protein engineering, the scope of reactions catalysed by native metalloenzymes has been expanded recently to include abiological transformations2,3. However, this strategy is limited by the inherent reactivity of metal centres in native metalloenzymes. To overcome this limitation, artificial metalloproteins have been created by incorporating complete, noble-metal complexes within proteins lacking native metal sites1,4,5. The interactions of the substrate with the protein in these systems are, however, distinct from those with the native protein because the metal complex occupies the substrate binding site. At the intersection of these approaches lies a third strategy, in which the native metal of a metalloenzyme is replaced with an abiological metal with reactivity different from that of the metal in a native protein6,7,8. This strategy could create artificial enzymes for abiological catalysis within the natural substrate binding site of an enzyme that can be subjected to directed evolution. Here we report the formal replacement of iron in Fe-porphyrin IX (Fe-PIX) proteins with abiological, noble metals to create enzymes that catalyse reactions not catalysed by native Fe-enzymes or other metalloenzymes9,10. In particular, we prepared modified myoglobins containing an Ir(Me) site that catalyse the functionalization of C–H bonds to form C–C bonds by carbene insertion and add carbenes to both β-substituted vinylarenes and unactivated aliphatic α-olefins. We conducted directed evolution of the Ir(Me)-myoglobin and generated mutants that form either enantiomer of the products of C–H insertion and catalyse the enantio- and diastereoselective cyclopropanation of unactivated olefins. The presented method of preparing artificial haem proteins containing abiological metal porphyrins sets the stage for the generation of artificial enzymes from innumerable combinations of PIX-protein scaffolds and unnatural metal cofactors to catalyse a wide range of abiological transformations.


Metal: Ir
Ligand type: Methyl; Porphyrin
Host protein: Myoglobin (Mb)
Anchoring strategy: Metal substitution
Optimization: Chemical & genetic
Reaction: C-H activation
Max TON: 7260
ee: 68
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Methyl; Porphyrin
Host protein: Myoglobin (Mb)
Anchoring strategy: Metal substitution
Optimization: Chemical & genetic
Reaction: C-H activation
Max TON: 92
ee: 84
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: ---

A De Novo Designed Metalloenzyme for the Hydration of CO2

Pecoraro, V. L.

Angew. Chem., Int. Ed., 2014, 10.1002/anie.201404925

Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature’s approach to catalysis, a ZnII metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single‐stranded three‐helix bundle and binds ZnII with high affinity using His3O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400‐fold of the fastest carbonic anhydrase isoform, CAII, and 11‐fold of CAIII.


Metal: Zn
Ligand type: Amino acid
Host protein: α3D peptide
Anchoring strategy: Dative
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: ---
Notes: kcat/KM ≈ 3.8*104 M-1*s-1

A Designed Functional Metalloenzyme that Reduces O2 to H2O with Over One Thousand Turnovers

Lu, Y.

Angew. Chem., Int. Ed., 2012, 10.1002/anie.201201981

Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O2 to H2O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity.


Metal: Cu
Ligand type: Amino acid
Host protein: Myoglobin (Mb)
Anchoring strategy: Dative
Optimization: Chemical & genetic
Max TON: 1056
ee: ---
PDB: 4FWX
Notes: Sperm whale myoglobin

A Designed Heme-[4Fe-4S] Metalloenzyme Catalyzes Sulfite Reduction like the Native Enzyme

Lu, Y.

Science, 2018, 10.1126/science.aat8474

Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement, but it is challenging to design artificial enzymes to catalyze these important reactions, owing to their structural and functional complexity. We report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved—through rational tuning of the secondary sphere interactions around the [4Fe-4S] and the substrate-binding sites—to be close to that of the native enzyme. By offering insight into the requirements for a demanding six-electron, seven-proton reaction that has so far eluded synthetic catalysts, this study provides strategies for designing highly functional multicofactor artificial enzymes.


Metal: Fe
Host protein: Cytochrome c peroxidase
Anchoring strategy: Dative
Optimization: Chemical & genetic
Reaction: Sulfite reduction
Max TON: ---
ee: ---
PDB: ---
Notes: Designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase

Albumin-Conjugated Corrole Metal Complexes: Extremely Simple Yet Very Efficient Biomimetic Oxidation Systems

Gross, Z.

J. Am. Chem. Soc., 2005, 10.1021/ja045372c

An extremely simple biomimetic oxidation system, consisting of mixing metal complexes of amphiphilic corroles with serum albumins, utilizes hydrogen peroxide for asymmetric sulfoxidation in up to 74% ee. The albumin-conjugated manganese corroles also display catalase-like activity, and mechanistic evidence points toward oxidant-coordinated manganese(III) as the prime reaction intermediate.


Metal: Mn
Ligand type: Corrole
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Sulfoxidation
Max TON: 8
ee: 74
PDB: ---
Notes: ---

Metal: Mn
Ligand type: Corrole
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Sulfoxidation
Max TON: 42
ee: 52
PDB: ---
Notes: ---

An Artificial Heme Enzyme for Cyclopropanation Reactions

Roelfes, G.

Angew. Chem., Int. Ed., 2018, 10.1002/anie.201802946


Metal: Fe
Ligand type: Protoporphyrin IX
Host protein: LmrR
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Cyclopropanation
Max TON: 449
ee: 51
PDB: 6FUU
Notes: ---

An Artificial Metalloenzyme for Carbene Transfer Based on a Biotinylated Dirhodium Anchored Within Streptavidin

Ward, T. R.

Cat. Sci. Technol., 2018, 10.1039/C8CY00646F


Metal: Rh
Ligand type: Carboxylate
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Cyclopropanation
Max TON: ~60
ee: ---
PDB: ---
Notes: Cyclopropanation reaction was also performed in the E. coli periplasm.

Metal: Rh
Ligand type: Carboxylate
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: C-H insertion
Max TON: ~60
ee: ---
PDB: ---
Notes: ---

An Artificial Metalloenzyme with the Kinetics of Native Enzymes

Hartwig, J. F.

Science, 2016, 10.1126/science.aah4427

Natural enzymes contain highly evolved active sites that lead to fast rates and high selectivities. Although artificial metalloenzymes have been developed that catalyze abiological transformations with high stereoselectivity, the activities of these artificial enzymes are much lower than those of natural enzymes. Here, we report a reconstituted artificial metalloenzyme containing an iridium porphyrin that exhibits kinetic parameters similar to those of natural enzymes. In particular, variants of the P450 enzyme CYP119 containing iridium in place of iron catalyze insertions of carbenes into C–H bonds with up to 98% enantiomeric excess, 35,000 turnovers, and 2550 hours−1 turnover frequency. This activity leads to intramolecular carbene insertions into unactivated C–H bonds and intermolecular carbene insertions into C–H bonds. These results lift the restrictions on merging chemical catalysis and biocatalysis to create highly active, productive, and selective metalloenzymes for abiological reactions.


Metal: Ir
Ligand type: Methyl; Porphyrin
Host protein: Cytochrome P450 (CYP119)
Anchoring strategy: Metal substitution
Optimization: Chemical & genetic
Reaction: C-H activation
Max TON: 582
ee: 98
PDB: ---
Notes: ---

Metal: Ir
Ligand type: Methyl; Porphyrin
Host protein: Cytochrome P450 (CYP119)
Anchoring strategy: Metal substitution
Optimization: Chemical & genetic
Reaction: C-H activation
Max TON: 35129
ee: 91
PDB: ---
Notes: ---

An Enantioselective Artificial Suzukiase Based on the Biotin–Streptavidin Technology

Ward, T. R.

Chem. Sci., 2015, 10.1039/c5sc03116h


Metal: Pd
Ligand type: Allyl; Phosphine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 88
ee: 80
PDB: ---
Notes: ---

Metal: Pd
Ligand type: Allyl; Carbene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 5
ee: ---
PDB: ---
Notes: ---

An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades

Ward, T. R.

J. Am. Chem. Soc., 2016, 10.1021/jacs.6b02470


Metal: Ir
Ligand type: Cp*; Phenanthroline
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: >999
ee: >99
PDB: ---
Notes: ---

A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold

Green, A. P.; Hilvert, D.

J. Am. Chem. Soc., 2018, 10.1021/jacs.7b12621


Metal: Fe
Host protein: Myoglobin (Mb)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Oxidation
Max TON: ~1650
ee: ---
PDB: 5OJ9
Notes: Oxidation of amplex red

Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology

Ward, T. R.

J. Organomet. Chem., 2005, 10.1016/j.jorganchem.2005.02.001


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: ---

Artificial Copper Enzymes for Asymmetric Diels–AlderReactions

Kamer, P. C. J.; Laan, W.

ChemCatChem, 2012, 10.1002/cctc.201200671


Metal: Cu
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Max TON: 9.6
ee: 25
PDB: 1IKT
Notes: ---

Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials

Lombardi, A.; Nastri, F.

Int. J. Mol. Sci., 2018, 10.3390/ijms19102896


Metal: Fe
Ligand type: Amino acid; Porphyrin
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: ---
Notes: Immobilization of the ArM on gold surfaces via a lipoic acid anchor.

Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase

Artero, V.

ChemPlusChem, 2016, 10.1002/cplu.201600218


Metal: Co
Ligand type: Oxime
Host protein: Heme oxygenase (HO)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: H2 evolution
Max TON: 15.3
ee: ---
PDB: ---
Notes: ---

Artificial Metalloenzymes as Catalysts for Oxidative Lignin Degradation

Jarvis, A. G.

ACS Sustainable Chem. Eng., 2018, 10.1021/acssuschemeng.8b03568


Metal: Fe
Anchoring strategy: Cystein-maleimide
Optimization: Chemical & genetic
Reaction: Lignin oxidation
Max TON: 20
ee: ---
PDB: ---
Notes: Reaction performed with a lignin model compound and hydrogen peroxide as oxidizing agent

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

Ward, T. R.

Proc. Natl. Acad. Sci. U. S. A., 2005, 10.1073/pnas.0409684102


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: ---

Artificial Metalloenzymes for Asymmetric Allylic Alkylation on the Basis of the Biotin–Avidin Technology

Ward, T. R.

Angew. Chem., Int. Ed., 2008, 10.1002/anie.200703159


Metal: Pd
Ligand type: Phosphine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Allylic alkylation
Max TON: 10
ee: 93
PDB: ---
Notes: ---

Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin-Avidin

Ward, T. R.

J. Am. Chem. Soc., 2003, 10.1021/ja035545i


Metal: Rh
Ligand type: Phosphine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Hydrogenation
Max TON: ---
ee: 96
PDB: ---
Notes: ---

Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium-Diphosphine Complexes

Ward, T. R.

J. Am. Chem. Soc., 2004, 10.1021/ja0476718


Metal: Rh
Ligand type: Phosphine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Hydrogenation
Max TON: ---
ee: 94
PDB: ---
Notes: ---

Artificial Metalloenzymes Through Cysteine-Selective Conjugation of Phosphines to Photoactive Yellow Protein

Kamer, P. C. J.

ChemBioChem, 2010, 10.1002/cbic.201000159


Metal: Pd
Ligand type: Allyl; Phosphine
Anchoring strategy: Covalent
Optimization: Chemical & genetic
Reaction: Allylic amination
Max TON: 45
ee: ---
PDB: 2PHY
Notes: ---

Artificial Metalloproteins Containing Co4O4 Cubane Active Sites

Borovik, A. S.; Don Tilley, T.

J. Am. Chem. Soc., 2018, 10.1021/jacs.7b13052


Metal: Co
Ligand type: OAc; Pyridine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: 6AUC
Notes: Co-complex in Sav WT

Metal: Co
Ligand type: OAc; Pyridine
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: 6AUE
Notes: Co-complex in Sav S112Y

Artificial Transfer Hydrogenases Based on the Biotin-(Strept)avidin Technology: Fine Tuning the Selectivity by Saturation Mutagenesis of the Host Protein

Ward, T. R.

J. Am. Chem. Soc., 2006, 10.1021/ja061580o


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

Ward, T. R.

Angew. Chem., Int. Ed., 2011, 10.1002/anie.201007820


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

McNaughton, B. R.; Rovis, T.

J. Am. Chem. Soc., 2019, 10.1021/jacs.9b01596


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: ---

Beyond Iron: Iridium-Containing P450 Enzymes for Selective Cyclopropanations of Structurally Diverse Alkenes

Hartwig, J. F.

ACS Cent. Sci., 2017, 10.1021/acscentsci.6b00391


Metal: Ir
Ligand type: Methyl; Porphyrin
Host protein: Cytochrome P450 (CYP119)
Anchoring strategy: Metal substitution
Optimization: Chemical & genetic
Reaction: Cyclopropanation
Max TON: 10181
ee: 98
PDB: ---
Notes: Selectivity for cis product (cis/trans = 90:1)

Biosynthesis of a Site-Specific DNA Cleaving Protein

Schultz, P. G.

J. Am. Chem. Soc., 2008, 10.1021/ja804653f


Metal: Cu
Ligand type: Bipyridine
Anchoring strategy: ---
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: ---
Notes: Catabolite activator protein from E. coli

Metal: Fe
Ligand type: Bipyridine
Anchoring strategy: ---
Optimization: Chemical & genetic
Max TON: ---
ee: ---
PDB: ---
Notes: Catabolite activator protein from E. coli

Burkavidin: A Novel Secreted Biotin-Binding Protein from the Human Pathogen Burkholderia Pseudomallei

Creus, M.

Protein Expression Purif., 2011, 10.1016/j.pep.2011.01.003


Metal: Rh
Ligand type: Diphenylphosphine
Host protein: Burkavidin
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Reaction: Hydrogenation
Max TON: ~110
ee: 65
PDB: ---
Notes: ---