Cover
Title Page
Copyright
Preface
Chapter 1: Preparation of Artificial Metalloenzymes
1. 1.1 Introduction
2. 1.2 ArM Formation via Metal Binding
3. 1.3 ArM Formation via Supramolecular Interactions
4. 1.4 ArM Formation via Covalent Linkage
5. 1.5 Conclusion
6. Acknowledgments
7. References
Chapter 2: Preparation of MetalloDNAzymes
1. 2.1 Introduction
2. 2.2 In Vitro Selection of MetalloDNAzymes in the Presence of Metal Ions
3. 2.3 From In Vitro Selection to Design of MetalloDNAzymes in the Presence of Metallocofactors
4. 2.4 Design and Preparation of DNA-Based Hybrid Catalysts
5. 2.5 Summary and Future Directions
6. Acknowledgments
7. References
Chapter 3: Experimental Characterization Techniques of Hybrid Catalysts
1. 3.1 Introduction
2. 3.2 Characterization of Modified Naturally Occurring Metalloproteins
3. 3.3 Characterization of New Metalloenzymes Created from Metal-Free Proteins
4. 3.4 Characterization of DNAzymes
5. 3.5 Conclusions
6. Acknowledgments
7. References
Chapter 4: Computational Studies of Artificial Metalloenzymes
1. 4.1 Introduction
2. 4.2 From Computational Transition Metal Catalysis to Artificial Metalloenzymes Design
3. 4.3 The Toolbox of the Artificial Enzyme Modeler
4. 4.4 Application of Computational Methods to the Optimization and Design of Artificial Metalloenzymes
5. 4.5 Outlook
6. 4.6 Conclusion
7. Acknowledgments
8. References
Chapter 5: Directed Evolution of Artificial Metalloenzymes
1. 5.1 Evolution Enables Chemical Innovation
2. 5.2 Directed Evolution Applied to Natural Metalloenzymes
3. 5.3 Directed Evolution of Hemoproteins for Abiological Catalysis
4. 5.4 Metalloenzymes with Artificial Cofactors or Metal-Binding Sites
5. 5.5 Conclusion
6. Acknowledgments
7. References
Chapter 6: Artificial Metalloenzymes for Hydrogenation and Transfer Hydrogenation Reactions
1. 6.1 Impact of Metallohydrogenases in the Field of Artificial Metalloenzymes
2. 6.2 Biotinylated Metal Complexes in Avidin and Streptavidin
3. 6.3 Artificial Enzymes with Covalent Metalloprotein Constitution
4. 6.4 Chemocatalysts Embedded in Protein Motifs
5. 6.5 Conclusions
6. References
Chapter 7: Hybrid Catalysts for Oxidation Reactions
1. 7.1 Metal Switch
2. 7.2 Structural Modulation of Natural Enzymes
3. 7.3 Cofactor Replacement: Reconstitution Strategy
4. 7.4 Rational Design of Enzymes
5. 7.5 De Novo Synthetic Active Site
6. 7.6 De Novo Protein Scaffold
7. 7.7 Concluding Remarks
8. References
Chapter 8: Hybrid Catalysts as Lewis Acid
1. 8.1 Introduction
2. 8.2 C−C Bond-Forming Reactions
3. 8.3 C−X Bond-Forming Reactions
4. 8.4 Hydrolytic Reactions
5. 8.5 Conclusions and Outlook
6. References
Chapter 9: Hybrid Catalysts for C−H Activation and Other X−H Insertion Reactions
1. 9.1 General Introduction
2. 9.2 Artificial Metalloenzymes for C−H Insertion
3. 9.3 Repurposing Hemoproteins for C−H Insertion Reactions
4. 9.4 Conclusion
5. References
Chapter 10: Hybrid Catalysts for Other C−C and C−X Bond Formation Reactions
1. 10.1 Introduction
2. 10.2 Allylic Substitution
3. 10.3 Palladium-Catalyzed Cross-Coupling Reactions
4. 10.4 Hydroformylation
5. 10.5 Phenylacetylene Polymerization
6. 10.6 Olefin Metathesis
7. 10.7 Summary and Future Trends
8. Acknowledgments
9. References
Chapter 11: Metal–Enzyme Hybrid Catalysts in Cascade and Multicomponent Processes
1. 11.1 Introduction
2. 11.2 Metal-Based Catalyst Hybrids with Enzymes for Cascade and Multicomponent Processes
3. 11.3 Design Strategy for Metal–Enzyme Hybrid Catalysts in Multicomponent Cascade Reactions
4. 11.4 Reaction Mechanisms of Metal–Enzyme Hybrid Catalysts in Multicomponent Cascade Reactions
5. 11.5 Conclusion and Future Perspectives
6. Acknowledgments
7. References
Chapter 12: Metalloenzyme-Inspired Systems for Alternative Energy Harvest
1. 12.1 Introduction: Artificial Photosynthesis
2. 12.2 Hydrogen Evolution
3. 12.3 Hybrid Systems for Overall Water Splitting
4. 12.4 Bioinspired Systems for O₂ Reduction
5. 12.5 Conclusions and Outlook
6. Acknowledgments
7. References
Chapter 13: Synthesis and Application of Hybrid Catalysts with Metalloenzyme-Like Properties
1. 13.1 Introduction
2. 13.2 Synthesis of Pd Nanobiohybrids (Pd(0)NPs-Enzyme Hybrids)
3. 13.3 Synthesis of Au Nanobiohybrids
4. 13.4 Synthesis of Ag Nanobiohybrids
5. 13.5 Synthesis of Cu Nanobiohybrids
6. 13.6 Synthesis of Pt Nanobiohybrids
7. 13.7 Chemical Applications of Nanobiohybrids
8. 13.8 Conclusions
9. Acknowledgments
10. References
Index
End User License Agreement

List of Illustrations

Chapter 1: Preparation of Artificial Metalloenzymes
1. Figure 1.1 Approaches to generate ArMs via metal binding.
2. Figure 1.2 Overlay of His/His/His metal binding site in hCAII structures containing Zn(II) (gray), Co(II) (red), Cu(II) (yellow), Ni(II) (blue), and Mn(II) (green) bearing H₂O/O₂ (Zn, Cu, and Co) and sulfate (Ni and Mn) ligands.
3. Figure 1.3 (a) Apo-recombinant horse liver ferritin with highlighted subunit in red. (b) Ferritin threefold axis binding site occupied with Pd(II) (top, blue spheres) and Rh(I) (bottom, purple spheres). (c) Ferritin accumulation binding site with Pd(II) (top, blue spheres) and Rh(I) (bottom, purple spheres).
4. Figure 1.4 Locations of metal binding sites introduced into scaffold proteins. (a) tHisF scaffold with mutation sites in red. (b) Rab4 Zn-directed homodimer crystal structure with Zn(II) represented with gray spheres. (c) NMR structure of 3His-G4DFsc bound to two Zn(II) ions (gray spheres). (d) Crystal structure of Zn₈:^A104/G57AB34 with structural Zn(II) sites on the vertical axis and catalytic Zn(II) sites on the horizontal axis.
5. Figure 1.5 Structures of unnatural amino acids incorporated into protein scaffolds to create ArMs or improve ArM activity.
6. Figure 1.6 ArM formation via cofactor binding and cofactor anchoring.
7. Figure 1.7 Representative structures of cofactors used for ArM formation via cofactor binding.
8. Figure 1.8 Structures of cofactors used for ArM formation via cofactor anchoring.
9. Figure 1.9 Structures of cofactors used for ArM formation via cofactor anchoring. Anchoring groups are highlighted in grey.
10. Figure 1.10 General scheme for ArM formation via covalent linkage.
11. Figure 1.11 Representative covalent ArM cofactors.
Chapter 2: Preparation of MetalloDNAzymes
1. Figure 2.1 DNAzymes in (a) ssDNA and (b) G-quadruplex and (c) B-DNA scaffolds (also called double-stranded DNA (dsDNA)).
2. Figure 2.2 General DNAzyme structure in which structural features such as the thermostable tetraloop is indicated in green, Watson–Crick base-pairing binding arms are in black, and the random region is highlighted in red and bases are indicated by N.
3. Figure 2.3 Isolation techniques for in vitro selection using (a) column-based and (b) gel-based separation methods.
4. Figure 2.4 PCR 1 (a) and 2 (b) amplification to regenerate the original DNAzyme sequence and (c) separation of the dsDNA generated by PCR to recover the active ssDNA pool. The squiggly line denotes a non-amplifiable spacer, and rA denotes the ribonucleotide cleavage site.
5. Figure 2.5 Truncation (a) and cis-to-trans transformation (b) of NaA43. The truncated sequence is highlighted in red, while the tetraloop removed to allow for multi-turnover reactivity is indicated in blue. The enzyme and substrate sequences generated from this transformation are shown in green and black, respectively.
6. Figure 2.6 Protected nucleoside bases used for targeted postsynthetic modification.
Chapter 3: Experimental Characterization Techniques of Hybrid Catalysts
1. Figure 3.1 Replacement of native metal by a suitable transition metal to afford a new artificial metalloenzyme.
2. Figure 3.2 (a) Preparation of Cr-2-apo-Mb. (b) Deconvoluted ESI-TOF mass spectra of Cr-2-apo-Mb with two equivalents of hemin in ammonium acetate.
3. Figure 3.3 Preparation of Mn(salen)-(L72C/Y03C) and UV–Vis spectra of apo-Mb (L72C/Y103C) (red dashed line)and Mn(salen)-(L72C/Y03C) (blue solid line).
4. Figure 3.4 (a) Preparation of a size-selective Pd catalyst for the hydrogenation of olefins. (b) TEM image of Pd–apoferritin particles stained with uranyl acetate.
5. Figure 3.5 Os(VI)-1-BSA complex, dimeric complex 2, and 2-phenylpropane-1,2-diolatodioxoethylenediamine osmium(VIII) complex 3.
6. Figure 3.6 Raman spectra of (a) Cu^II-BpyAla (75 μM), (b) LmrR_M89BpyAla_Cu^II (60 μM of Cu^II), (c) LmrR_M89BpyAla in 20 mM MOPS buffer, 150 mM NaCl at pH 7 λ_exc 355 nm.
7. Figure 3.7 Formation of an artificial metalloenzyme via covalent interaction.
8. Figure 3.8 Schematic representation of the hybrid catalyst where the Cu^II complex is located at the interface of a protein scaffold. Bipyridine and phenanthroline ligands used for the anchorage.
9. Figure 3.9 (A) Preparation of the hybrid catalyst. (B) Fluorescence emission spectra of: (a) SCP-2LV83C (▪), (b) SCP-2LV83C–N3 (•), (c) CP-2LV83C–N3 + copper(II) nitrate (1 equiv.) and SCP-2LV83C–N3 (♦), (d) +Cu(NO₃)₂, 1 equiv. (▴), and (e) +Cu(NO₃)₂, 1 equiv. + 100 equiv. EDTA (□).
10. Figure 3.10 Preparation of an artificial metalloenzyme for hydrogenation and ESI spectra of the hybrid after purification.
11. Figure 3.11 Preparation of an artificial metalloenzyme for olefin metathesis and ESI-MS spectra of the hybrid.
12. Figure 3.12 (a) Biotinylated half-sandwich complex incorporated into streptavidin (Sav) mutants. (b) X-ray crystal structure of [η-(benzene)RuCl(Biot-p-L)]⊂S112KSav.
13. Figure 3.13 Evolution of CD spectra of βLG upon addition of increasing amounts of 3-Rh.
14. Figure 3.14 Parts of the metal-conjugated affinity labels (m-ALs) consisting of the metal complex, reactive element, and recognition group.
15. Figure 3.15 (a) Au-tagged CAL-B by HAADF-STEM. The larger and brighter set of particles corresponds to Au-tagged CAL-B and the smaller set to the Pd nanoparticles. (b) HAADF-STEM of the hybrid catalyst without Au nanoparticles.
16. Figure 3.16 Raman spectra of (a) Cu(II)-dmbpy, (b) Cu(II)-dpq, and (c) Cu(II)-dppz in the presence (blue line) and in the absence (black line) of st-DNA at λ_exc 355 nm.
17. Figure 3.17 (a) Ligand and Pt-modified st-DNA. (b) CD spectra of st-DNA (red line) and st-DNA modified via covalent anchoring (blue line).
Chapter 4: Computational Studies of Artificial Metalloenzymes
1. Figure 4.1 Main features of a transition metal catalyst (a) and an artificial metalloenzyme (b).
2. Figure 4.2 First (inside) and second (outside) coordination spheres around an iridium-containing organometallic cofactor. The example illustrates an artificial transfer hydrogenase based on the biotin–streptavidin technology designed by Ward's group.
3. Figure 4.3 The multidimensional chemogenetic space.
4. Figure 4.4 The three main families of molecular modeling methods applied in the field of artificial metalloenzymes.
5. Figure 4.5 Main steps in the integrative procedure employed to analyze the changes in the first coordination sphere of the Corynebacterium diphtheriae heme oxygenase when the heme prosthetic group is substituted by a Fe(Schiff base) salophen [66].
6. Figure 4.6 The enantioselectivity of an O₂-dependent hydroxylation at a mononuclear nonheme iron center was switched from S in the native enzyme (left) to R in the ArM by changing the orientation of the substrate ligand at the metal center through protein redesign.
7. Figure 4.7 Schematic representation of the Rosetta design protocols. They start with a minimal model of the transition state active center and its surroundings, called “theozyme” (above, right). The theozyme is then accommodated in a suitable protein scaffold (center) by an inverse rotamer lookup (inside-out strategy) or the RosettaMatch algorithm (outside–in strategy). The next step takes the previously obtained results and refines them to minimize the steric clashes and optimize the catalytic geometry (left).
8. Figure 4.8 General view of the lowest-energy docking solution for 2-azachalcone bound to the artificial metalloenzyme formed by associating neocarzinostatin (NCS-3.24) with a copper–phenanthroline–testosterone complex.
9. Figure 4.9 Schematic representation of the approach employed for the identification of the catalytic mechanism inside a proteic scaffold of an artificial transferhydrogenase.
Chapter 5: Directed Evolution of Artificial Metalloenzymes
1. Figure 5.1 Overview of directed evolution.
2. Figure 5.2 Directed evolution takes a protein along its fitness landscape, where fitness is a metric defined by the experimenter. Sequence diversification samples the nearby sequences, and screening identifies fitness improvements. Two possible evolutionary trajectories from a single starting point illustrate that there may exist multiple local maxima or solutions to any given optimization, and the results may depend on the path taken. Sequence space is of very high dimensionality; a simplified fitness landscape is presented here.
3. Figure 5.3 Directed evolution of a carbonic anhydrase stable to CO₂ capture process conditions. (a) Carbonic anhydrase catalyzes the reversible hydration of CO₂ to bicarbonate and a proton. The enzyme utilizes a catalytic zinc atom, displayed as a sphere. Only a single subunit of the tetrameric protein is shown (PDB 2A5V). (b) Evolution of an ultrastable carbonic anhydrase. Half-lives of the variants at the indicated temperature (black) were determined by measuring CO₂ absorption in a reactor. The fold improvement over the previous round is shown above each bar.
4. Figure 5.4 Engineering a cytochrome P450 for regioselective oxidation of permethylated monosaccharides. (a) Model reaction for P450-catalyzed demethylation. (b) Evolutionary trajectory of a regioselective catalyst.
5. Figure 5.5 Regiodivergent hydroxylation of testosterone by engineered P450_BM3 variants.
6. Figure 5.6 Developing a biocatalytic route to antidepressant levomilnacipran. (a) P450_BM3 variants catalyze the cyclopropanation of acrylamide 5.7 with ethyl diazoacetate to form levomilnacipran core 5.8. (b) Evolution of a P450_BM3 variant for improved enantioselectivity for the cyclopropanation of 5.7.
7. Figure 5.7 Regiodivergent C−H amination catalyzed by engineered cytochrome P450_BM3 variants.
8. Figure 5.8 Evolution of a highly selective aziridination catalyst derived from P450_BM3.
9. Figure 5.9 Evolution of a protein catalyst for formal asymmetric allylic amination. (a) Accessing chiral allylic amines via a sulfimidation/sigmatropic rearrangement sequence. DTT, dithiothreitol. (b) A substrate walk approach to evolve P450_BM3-based catalysts for nitrene transfer to an allyl sulfide. TON, turnover number.
10. Figure 5.10 Rma cyt c-catalyzed carbon–silicon bond formation via carbene insertion into Si−H bond. (a) Directed evolution of Rma cyt c for carbon–silicon bond formation. Amino acid residues M100, V75, and M103 shown in the “active site” structure of wild-type Rma cyt c (PDB: 3CP5) were subjected to sequential site-saturation mutagenesis. (b) Chemoselectivity for carbene Si−H insertion over N−H insertion increased markedly during directed evolution of Rma cyt c. EDA, ethyl diazoacetate; TTN, total turnover number; WT, wild-type.
11. Figure 5.11 Heme cofactor in sperm whale myoglobin is solvent-exposed (PDB: 1A6K). Mutation of amino acid residues F43, H64, and V68, which are close to the heme cofactor, affects diastereo- and enantioselectivity of a nonnatural cyclopropanation reaction.
12. Figure 5.12 Carbene transfer catalyzed by metal-substituted myoglobin variants. (a) Representative C−H insertion reaction. (b) Evolutionary trajectory resulting in variants with divergent enantioselectivity for product 5.14.
13. Figure 5.13 Artificial Zn-binding protein of Tezcan and coworker [51]. (a) Ester hydrolysis catalyzed by protein variants. (b) Tetrameric complex that served as parent for directed evolution (PDB 4U9D). (c) Substrates described in this study. (d) Progression of evolution for ampicillin-hydrolase activity.
14. Figure 5.14 Enantioselective hydrogenation with Rh–streptavidin metalloenzymes. (a) Biotin linker for attachment of organometallic catalysts. (b) Schematic of catalyst design. (c) Hydrogenation of alkenes reported by Reetz et al.. (d) Directed evolution to improve enantioselectivity.
15. Figure 5.15 Reduction of ketones to alcohols with Ru–streptavidin metalloenzymes. (a) Reactions tested by Ward and coworkers. (b) Enantiodivergent catalysts obtained through directed evolution.
16. Figure 5.16 Suzuki cross-coupling catalyzed by a Pd–streptavidin metalloenzyme. (a) Reaction tested by Ward and coworkers. (b) Optimization of enantioselectivity.
17. Figure 5.17 Alkene metathesis catalyst derived from streptavidin. (a) Model of complex 5.27 in streptavidin.
18. Figure 5.18 A platform for Rh–protein conjugates based on proline peptidase. (a) Strategy for formation of artificial metalloenzyme. (b) Carbene transfer catalyzed by enzyme variants. (c) Optimization of activity and enantioselectivity.
Chapter 6: Artificial Metalloenzymes for Hydrogenation and Transfer Hydrogenation Reactions
1. Figure 6.1 Key features that launched hydrogenation as protagonist application in the development of artificial metalloenzymes: (a) the catalyst-promoted formation of chiral products from non-chiral olefins, ketones, and imines, (b) the combination of proteins with biologically non-occurring metals, and (c) the pioneer work from 1978 by Whitesides on the conversion of a protein to a homogeneous asymmetric hydrogenation catalyst.
2. Figure 6.2 A rhodium–biotin catalyst promotes enantioselectivity in the hydrogenation of 1 in the presence of the protein avidin as observed in the enantiomeric excess (ee) measured by polarimetry.
3. Figure 6.3 Avidin as protein host not only promotes the catalytic enantioselectivity but can also stir the configuration of the product, showing metal-protein cooperativity in the asymmetric hydrogenation of itaconic acid.
4. Figure 6.4 Series of biotinylated diphosphine ligands in the study of the hydrogenation of 1 with Rh(biotin)–avidin and –streptavidin hybrids.
5. Figure 6.5 Competitive hydrogenation of 1 and 5 by different combinations of Sav mutants and Rh–biotin complexes.
6. Figure 6.6 Introduction of chiral amino acid spacers in biotin–Sav artificial metalloenzymes.
7. Figure 6.7 Multivariable optimization of artificial transfer hydrogenases (ATHases).
8. Figure 6.8 Transfer hydrogenation of imine 10 to form salsolidine 11 (a) and the general proposed mechanism for the transfer hydrogenation of ketones and imines (b).
9. Figure 6.9 Anchoring of Rh catalysts in Sav via dual anchoring of biotinylated η⁵-Cp ligands. By using coordinating His residues in different positions of Sav “pseudo-mirror image” catalysts are produced.
10. Figure 6.10 Multienzymatic cascade reactions for the transfer hydrogenation of imine 12 toward amine 13 by accumulation of the (R)-product using formic acid/formate (a) or glucose (b) as hydride source.
11. Figure 6.11 Reetz (a) and de Vries (b) approaches for the covalent hybridization of papain with rhodium catalysts for hydrogenation.
12. Figure 6.12 Transfer hydrogenation of NAD⁺ and acetophenones by Ru and Rh artificial enzymes of papain reported by Salmain.
13. Figure 6.13 Dual (supramolecular covalent) hybridization of papain with Ru and Rh complexes for the enantioselective transfer hydrogenation of acetophenones.
14. Figure 6.14 Approach for covalent modification of PYP by Kamer.
15. Figure 6.15 (a) General reaction of the covalent, active site-directed hybridization of lipases with organometallic phosphonate inhibitors. (b) Artificial hydrogenation metalloenzymes developed by Klein Gebbink.
16. Figure 6.16 Iridium catalysts for the hydrogenation of cyclic imine 10 anchored to HCA II by Zn coordination of tethered diamine ligands.
17. Figure 6.17 Palladium nanoclusters embedded in apoferritin afford a metalloenzyme, which hydrogenates olefins with a TOF that decreases with the size of the substrate.
18. Figure 6.18 The aliphatic affinity of β-lactoglobulin allows the embedding of hydrogenation catalysts of Ru and Rh centers bearing linear hydrocarbon chains.
Chapter 7: Hybrid Catalysts for Oxidation Reactions
1. Figure 7.1 Crystal structure of the active site of manganese-substituted carbonic anhydrase II (PDB code: 1RZD).
2. Figure 7.2 (a) Structure of the substrate pocket of the F87W/Y96F/V247L mutant of P450_cam (PDB code: 1J51). Heme is depicted in cyan. The nine residues with bulky substitutions to produce an engineered P450 capable of oxidizing ethane are depicted in green. Protein cavities are depicted in blue. (b) Proposed catalytic reaction mechanism of P450_BM3 in complex with fluoroalkyl fatty acids for propane oxidation (DOI: 10.1002/anie.201007975).
3. Figure 7.3 Chart of heme-type cofactors presented in this chapter.
4. Figure 7.4 Rational design of nitric oxide reductase. Crystal structure of the engineered heme pocket of myoglobin (PDB code: 3K9Z). Heme is depicted in cyan. Fe(II)-coordinating residues are depicted in green.
5. Figure 7.5 Chart of salen-type ligands presented in this chapter.
6. Figure 7.6 (a) Crystal structure of Mb-Ala71Gly in complex with Cr-salophen (PDB code: 1J3F). Metal complex is depicted in cyan. Residues involved in the proposed binding site for thioanisole are depicted in green. (b) Calculated active site structure of Mn-3,3′-Me₂-Mb-His64Asp/Ala71Gly superimposed on Mn-3,3′-Pr₂-Mb-His64Asp/Ala71Gly (DOI: 10.1021/ja045995q).
7. Figure 7.7 (a) Representation of V-Sav where the inorganic part is depicted in cyan and residues constituting the first coordination sphere in orange. Residues constituting the substrate-binding site are depicted in green. (b) N-naphthyl-S-(3-aminophenyl)-thioglycolamide docked in Fe-L1-NikA (DOI: 10.1002/anie.201209021).
8. Figure 7.8 Crystal structures of Fe-L-NikA at different aromatic hydroxylation stages. PDB codes: 3MVW (Fe-L-NikA), 3MVX (Fe-L-NikA in the reduced state), 3MVY (diatomic oxo-intermediate), and 3MWO (doubly hydroxylated Fe-L-NikA). Fe-L-NikA crystals of the different intermediates are shown in each frame. L is depicted in cyan and iron as an orange sphere. Residues constituting the second coordination sphere are depicted in green.
9. Figure 7.9 (a) Representation of Kaiser's helichrome in solution. (b) An example of mimochrome: crystal structure of mimochrome IV in complex with Co in a bis-His axial coordination (PDB code: 1PYZ). Coordinating histidines are depicted in orange. Porphyrin IX is depicted in cyan. (c-I) Dimer subunit of bacterioferritin (PDB code: 1BRF). (c-II) Heme facing helices of BFR are used as a scaffold to design MP3. Residues 14–28 and 44–58 were connected by a loop (in red). The heme group and metal ions are represented with space filling (DOI: 10.1002/chem.201201404).
Chapter 8: Hybrid Catalysts as Lewis Acid
1. Scheme 8.1 Cu(II)-catalyzed Diels–Alder reaction of aza-chalcone and cyclopentadiene.
2. Scheme 8.2 (a) Schematic representation of the DNA-based catalysis of Diels–Alder reaction using the supramolecular assembly of a copper complex of first-generation ligands. (b) Second-generation ligands.
3. Scheme 8.3 Schematic representation of the DNA-based asymmetric Diels–Alder reaction using α,β-unsaturated 2-acyl imidazoles as substrate
4. Scheme 8.4 Diels–Alder reaction catalyzed by DNA G-quadruplex/terpyridine-Cu(II) hybrid catalysts.
5. Scheme 8.5 Schematic representation of the DNA-based copper-catalyzed asymmetric Diels–Alder reaction using a modular approach of catalyst assembly.
6. Scheme 8.6 Schematic representation of DNA-based catalysts assembled using cisplatin to bind the catalytically active copper (II) complex to DNA applied in the asymmetric Friedel–Crafts alkylation and Diels–Alder cycloaddition reaction.
7. Scheme 8.7 (a) Schematic representation of the monomer/dimer equilibrium of bPP. (b) Asymmetric Diels–Alder reactions catalyzed by bPP^x–Cu^II complex in water.
8. Figure 8.1 Schematic representation of an artificial metalloenzyme and anchoring strategies with the metal-binding moieties of artificial metalloenzymes known to act as Lewis acid catalysts in Diels–Alder reaction and their best results of catalysis of the model reaction of cyclopentadiene with 2-aza-chalcone.
9. Scheme 8.8 Schematic representation of the asymmetric Diels–Alder reaction catalyzed by Ru-phenanthroline complex linked to papain.
10. Scheme 8.9 Schematic representation of the asymmetric DNA-based copper-catalyzed Michael reaction of α,β-unsaturated 2-acyl imidazoles and dimethyl malonate, nitromethane, or cyanoacetates as nucleophiles.
11. Scheme 8.10 Schematic representation of the asymmetric Michael addition reaction catalyzed by bPP-based artificial metalloenzyme containing 3-pyridylalanine (bPP^x).
12. Scheme 8.11 The asymmetric l- and d-DNA-based copper-catalyzed Friedel–Crafts and Michael reaction.
13. Scheme 8.12 Schematic representation of the asymmetric Friedel–Crafts reaction catalyzed by LmrR-based artificial metalloenzymes with (A) schematic representation of artificial enzyme containing unnatural amino acid Bpy and (B) schematic representation of artificial metalloenzyme containing Cu(II) phenanthroline ligand.
14. Scheme 8.13 One-pot process involving laccase-mediated allylic oxidation and DNA-based copper-catalyzed oxa-Michael addition reaction.
15. Scheme 8.14 Schematic representation of the water addition reaction catalyzed by LmrR-M89C_Phen_Cu hybrid catalyst.
16. Scheme 8.15 The asymmetric DNA-based copper-catalyzed fluorination of β-ketoesters.
17. Scheme 8.16 The asymmetric DNA-based hydrolytic kinetic resolution of 2-pyridyloxiranes.
18. Scheme 8.17 Hydrolysis reactions catalyzed by protein-phenanthroline_ALBP conjugate.
19. Scheme 8.18 Representation on NCS-3.24 scaffold with the bound Zn-Testo-BisPyPol complex and its application in HPNP hydrolysis.
Chapter 9: Hybrid Catalysts for C−H Activation and Other X−H Insertion Reactions
1. Scheme 9.1 Postulated mechanism of the [Biot–Cp*RhCl₂]₂ 1·Sav K121D/E catalyzed C−H activation reaction.
2. Scheme 9.2 Early reports of Myo-derived artificial metalloenzymes that catalyze C−H activation reactions in the presence of H₂O₂. (a) Stoichiometric aromatic hydroxylation and (b) guaiacol oxidation.
3. Scheme 9.3 Porphycene-reconstituted myoglobin catalyzes the hydroxylation of ethylbenzene. (a) Structure of porphycene and porphyrin and (b) reaction conditions.
4. Scheme 9.4 Covalent anchoring of an abiotic cofactor within the POP scaffold using strain-promoted azide–alkyne cycloaddition. The azidophenylalanine (Az) was engineered using the amber codon suppression methodology.
5. Scheme 9.5 Catalytic reaction of the tHisFAz176–Rh variant for an intermolecular carbene Si−H insertion.
6. Scheme 9.6 Engineered cytochrome P450_BM3 and myoglobin catalyze the cyclopropanation of styrene derivatives.
7. Scheme 9.7 Hstar catalyzes the enantioselective cyclopropanation of gem-disubstituted styrene 28 for the synthesis of levomilnacipran.
8. Figure 9.1 Close-up view of the active site of Myo (cartoon display). Relevant residues are displayed as stick: the heme moiety (in red), the proximal H93 (in orange), and the key residues lining the O₂-binding cavity that were targeted for mutagenesis (in yellow).
9. Scheme 9.8 C(sp³)−H amination of carbonazidates yields α-aminoalcohols upon hydrolysis.
10. Scheme 9.9 Postulated reaction mechanism for the carbenoid insertion into S−H bonds catalyzed by evolved myoglobin. S−H insertion product would then ensue via a proton transfer to the latter intermediate either prior to (path “a”) or after dissociation from the heme (path “b”).
11. Scheme 9.10 The electronic properties of the sulfide determine the fate of the iron–nitrenoid intermediate.
12. Scheme 9.11 A cascade consisting of an P411_BM3-catalyzed sulfimidation followed by a [2,3]-sigmatropic rearrangement affords enantioenriched allylic amine 90.
13. Scheme 9.12 Directed evolution of RebH for the regioselective chlorination of 7-deuterotryptamine relying on a mass spectrometry assay.
14. Figure 9.2 Directed evolution scheme of RebH leading to the identification of regioselective tryptamine halogenases.
Chapter 10: Hybrid Catalysts for Other C−C and C−X Bond Formation Reactions
1. Figure 10.1 Cartoon representing the potential induction of selectivity by substrate–catalyst interaction by hybrid catalysts.
2. Scheme 10.1 (a) General reaction scheme for transition metal-catalyzed allylic substitution reactions and (b) selected examples of chiral biomolecule-based ligands applied in this reaction.
3. Scheme 10.2 (a) Protected phosphane-modified amino acids for incorporation into synthetic oligopeptides and (b) synthetic oligopeptide-palladium catalyst for the palladium-catalyzed allylic alkylation of 3-acetoxycyclopentene with dimethylmalonate.
4. Scheme 10.3 Palladium-catalyzed allylic alkylation of 1,3-dimethylallylacetate with dimethylmalonate using amino acid-modified -3,4-diazaphospholane ligands.
5. Scheme 10.4 Palladium-catalyzed allylic alkylation of 1,3-diphenylallylacetate with dimethylmalonate using phosphane-modified gramicidin S ligands.
6. Scheme 10.5 Palladium-catalyzed allylic amination of 1,3-diphenylallylacetate with benzylamine using phosphane-modified photoactive yellow protein.
7. Scheme 10.6 (a) Palladium-catalyzed allylic alkylation of 1,3-diphenylallylacetate with diemethylmalonate using supramolecular (strept)avidin anchored phosphane-modified biotins and (b) results of the chemogenetic optimization displayed in a fingerprint display.
8. Scheme 10.7 (a) Phosphane-modified deoxyuridine containing monomeric and trimeric oligonucleotide structures and (b) their application as ligand in the palladium-catalyzed allylic amination of 1,3-diphenylallylacetate with benzylamine and N-benzylmethylamine.
9. Scheme 10.8 Iridium-catalyzed allylic amination of 1-phenylallylacetate with morpholine using diene-modified oligonucleotides with complementary RNA or DNA strands.
10. Scheme 10.9 General scheme for Pd-catalyzed cross-coupling reactions.
11. Scheme 10.10 The preparation of Pd(allyl)·apo-Fr and application in the Suzuki reaction of 4-iodoanaline and phenylboronic acid.
12. Scheme 10.11 (a) Suzuki reaction of 2-iodonaphthalene and 2-methoxy-1-naphthaleneboronic acid catalyzed by supramolecularly anchored biotinylated cofactors in (strept)avidin to give enantioenriched biaryls. WT, wild-type; Sav, streptavidin. (b) Fingerprint Figure showing the results using different mutants of Sav.
13. Figure 10.2 Phosphonate-based palladium pincer catalyst.
14. Scheme 10.12 Heck reaction of iodobenzene and ethyl acrylate catalyzed by 1 hybrids.
15. Scheme 10.13 Enantioselective Heck reaction of iodobenzene and dihydrofuran catalyzed by SP-CAL-B-C₈-1.
16. Scheme 10.14 Dehalogenation of BODIPY dyes and a cartoon showing the catalyst formation.
17. Scheme 10.15 Hydroformylation of different alkene substrates by rhodium-HSA dative complexes.
18. Scheme 10.16 (a) Formation of rhodium-substituted carbonic anhydrase II and (b) application in the hydroformylation of styrene.
19. Scheme 10.17 Phenylacetylene polymerization catalyzed by rhodium-modified ferritin cages.
20. Scheme 10.18 Phenylacetylene polymerization to predominantly trans-PPA catalyzed by nitrobindin covalently modified with a Rh(nbd)CP-maleimide complex.
21. Scheme 10.19 General reaction scheme for ROMP and RCM/ROM.
22. Figure 10.3 Examples of Schrock and Grubbs catalysts.
23. Figure 10.4 Hybrid catalyst derived from FhuA Δ D1-159 C545 protein and a Grubbs–Hoveyda type catalyst with a maleimide linking unit.
24. Scheme 10.20 Ring-opening metathesis polymerization (ROMP) of water-soluble oxanorbornene derivative catalyzed by hybrid Grubbs–Hoveyda type catalysts.
25. Scheme 10.21 Ring-opening metathesis polymerization catalyzed by Grubbs–Hoveyda-type catalyst modified nitrobindin. Illustration of the dimeric structure of NB-C3 calculated with YASARA.
26. Figure 10.5 Water-soluble RCM substrate GlcDAA.
27. Scheme 10.22 (a) RCM of N,N-diallyl p-toluenesulfonamide. (b) Cross metathesis of allylbenzene catalyzed by Ru-Cut catalysts.
28. Scheme 10.23 Grubbs catalyst modified G41C MjHSP for the RCM of N,N-diallyl p-toluenesulfonamide.
29. Scheme 10.24 Tethering a biotin anchor combined with a spacer on a Hoveyda–Grubbs-type catalyst ensures the localization of the metal moiety within the (strept)avidin and application in the RCM of N,N-diallyl p-toluenesulfonamide.
30. Scheme 10.25 Tethering an arylsulfonamide anchor to a Hoveyda–Grubbs type catalyst within human carbonic anhydrase II and application in the RCM of N,N-diallyl p-toluenesulfonamide.
Chapter 11: Metal–Enzyme Hybrid Catalysts in Cascade and Multicomponent Processes
1. Scheme 11.1 (a) Dynamic kinetic resolution of a racemic mixture of enantiomers by combining an enzyme and a metal catalyst. (b) Example of a cascade reaction in which a metal catalyst regenerates the cofactor required for the coupled enzymatic reaction.
2. Figure 11.1 (a) Schematic of the synthesis procedure for Au/SiO₂/glucosidase NP. (b) TEM of the hybrid catalyst. (c) Cascade reaction catalyzed by the hybrid catalyst.
3. Figure 11.2 (a) Schematic showing HRP–Au NP hybrid catalyst catalyzing the cascade reaction for glucose sensing.
4. Figure 11.3 (a) Preparation scheme for CalB–Pd hybrid catalyst. (b) Cascade reaction for the synthesis of aminoarene. (c) Dynamic kinetic resolution of racemic aryl amines catalyzed by the hybrid catalyst.
5. Scheme 11.2 Dynamic kinetic resolution of 1-phenylethylamine using CALB–Pd-AmP-MCF hybrid catalyst.
6. Figure 11.4 (a) Synthetic scheme of Te-Dps-Pd NP. (b) Cascade chemoenzymatic synthesis of chiral biaryl alcohols.
7. Figure 11.5 (a) Synthetic scheme of PepA–Pt NP. (b) Cascade reaction catalyzed by PepA–Pt NP hybrid catalyst to produce p-phenylenediamine from Glu-p-nitroanilide. (
8. Figure 11.6 (a) Preparation scheme for the enzyme–Cu NP hybrid. (b) SEM image of CalB-Cu NPs. (c) Cascade reaction catalyzed by the hybrid catalyst.
9. Figure 11.7 (a) Schematic of the mono-oxygenation of myristic acid [R=(CH₂)₁₀CH₃] using P450_BSβ/QD nanohybrids.
10. Figure 11.8 (a) Schematic of reaction cascades resulting from combining an ATHase with a biocatalyst. (b) Colorimetric assay for the determination of ATHase activity in an enzyme cascade. The activity of the ATHase in the enzyme cascade was revealed by HRP.
11. Figure 11.9 (a) Schematic of the in vivo recombinant expression and encapsulation of the fusion product AdhD-SP inside a P22 capsid. (b) Cascade reaction catalyzed by AdhD and the rhodium hybrid catalyst.
12. Figure 11.10 Design reported by Wang et al. in which a Ga₄L₆ cage contains a gold complex for use in olefin isomerization (box).
13. Figure 11.11 (a) Proposed mechanism for conversion of CO₂ in a spatially separated multienzyme system.
14. Figure 11.12 Synthetic scheme of yolk–shell Ru–B/mSiO₂@air@SiO₂.
15. Figure 11.13 Cascade reaction of conversion of CO₂ to MeOH. FateDH, formate dehydrogenase; FaldDH, formaldehyde dehydrogenase; YADH, yeast alcohol dehydrogenase.
16. Figure 11.14 Mechanism of the metal-based reduction of a nitro group to amine.
17. Figure 11.15 Representation of an LADH active site with a benzyl alcohol substituent bound to the cofactor NAD⁺. PT = proton transfer for initial mechanistic steps.
18. Figure 11.16 General mechanisms for (a) inverting glycosidase and (b) retaining glycosidase.
Chapter 12: Metalloenzyme-Inspired Systems for Alternative Energy Harvest
1. Figure 12.1 Schematic depiction of a molecular assembly for overall water splitting consisting of a photosensitizer (PS), a water oxidation catalyst (WOC), and a hydrogen-evolving catalyst (HEC) for the production of solar fuels.
2. Figure 12.2 Noble () and earth-abundant metals () commonly used for constructing hydrogen-evolution catalysts.
3. Figure 12.3 Examples of earth-abundant hydrogen-evolution catalysts.
4. Figure 12.4 Structures of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F (a) and of the [FeFe] hydrogenase from Desulfovibrio desulfuricans (b). The electron transfer chain (via iron–sulfur centers) and pathways for the dihydrogen and the H⁺ transfer are depicted.
5. Figure 12.5 Structures of the active sites of [NiFe]- and [FeFe]-hydrogenases.
6. Figure 12.6 Simplified depiction of attachment of an enzyme to an electrode for conducting protein film electrochemistry (PFE).
7. Figure 12.7 Computed model of the [FeFe] cluster attached to the helical 19-mer peptide developed by Ghirlanda and coworkers.
8. Figure 12.8 Three-component system for light-driven H₂ evolution. bpy, 2,2′-bipyridine.
9. Figure 12.9 Syntheses of apo-cyt c containing an iron carbonyl cluster.
10. Figure 12.10 Structures of (a) the active center of [FeFe]-hydrogenase (H-cluster and [Fe4S4] cluster) and (b) wild-type cytochrome c₅₅₆ (cyt c₅₅₆).
11. Figure 12.11 Photoinduced H₂ evolution by an octadecapeptide fragment, a characteristic sequence of cytochrome c₅₅₆, linked to a diiron cluster and a ruthenium photosensitizer.
12. Figure 12.12 [FeFe]-hydrogenase-based photoelectrochemical biofuel cell for H₂ evolution.
13. Figure 12.13 Depiction of hybrid hydrogenase systems for visible light-induced H₂ evolution.
14. Figure 12.14 Photodriven H₂ production using a semibiological system consisting of amorphous carbon nitride (CN_x) and a [NiFeSe]-hydrogenase.
15. Figure 12.15 Representation of the bioinspired photoelectrochemical (PEC) cell.
16. Figure 12.16 Schematic representation of a fuel cell. A proton permeable membrane (dashed line) may be used to separate the electrode compartments.
17. Figure 12.17 Estimated output of current biofuel cells and biosensors, demonstrating the gap that needs to be bridged before they can be considered for use in fuel cells.
18. Figure 12.18 A bioelectrode composed of hybrid DNA-templated gold nanoclusters and bilirubin oxidase (BOD) for enhanced enzymatic reduction of O₂.
19. Figure 12.19 Illustration of assembly of the ternary hybrid and fabrication of the membrane- and mediator-less glucose/O₂ enzyme biofuel cell (EBFC).
20. Figure 12.20 Mitochondrial electron transport metabolon immobilized onto an electrode surface.
Chapter 13: Synthesis and Application of Hybrid Catalysts with Metalloenzyme-Like Properties
1. Figure 13.1 Scheme of preparation of Pd nanobiohybrids.
2. Figure 13.2 Physicochemical characterization of Pd nanobiohybrid performed in the presence of DMF as cosolvent. (a) SEM images, (b) EDX pattern, (c) XRD pattern, (d) XPS image, and (e) TEM images. In the inset, HRTEM image and (f) size distribution of PdNPs dispersed onto the CAL-B framework.
3. Figure 13.3 Physicochemical characterization of Pd nanobiohybrid performed in the presence of methanol as cosolvent. (a) SEM images, (b) EDX pattern, (c) TEM image, and (d) size distribution of PdNPs dispersed onto the CAL-B framework.
4. Figure 13.4 Physicochemical characterization of Au–CAL-B nanobiohybrids. (a) TEM image of the biohybrid synthesized in 100% water. (b) Size distribution of AuNPs dispersed onto the CAL-B framework. (c) TEM image of the biohybrid synthesized in the presence of 20% methanol. (d) Size distribution of AuNPs dispersed onto the CAL-B framework.
5. Figure 13.5 Structural characterization of AuNPs–urease biohybrid. (a) pH change of the medium by native urease, AuNPs–urease biohybrid, denatured urease, and functionalized Au nanoparticles with urease. (b) Emission spectra of ANS in native urease, AuNPs–urease biohybrid, and citrate-capped Au nanoparticles–urease composite. (c) Circular dichroism spectrum of native urease and AuNPs–urease biohybrid in water. (d) UV–visible spectrum of DTNB-treated urease after incubation with HAuCl₄ for 48 h, showing the absence of SPR band of AuNPs.
6. Figure 13.6 (a) TEM image, (b) HRTEM of AuNPs–laccase hybrids, (c) Au nanoparticle size distribution based on TEM characterization shown in part a, and (d) UV–Vis absorbance spectrum of laccase (black trace), AuNPs–laccase hybrids (red trace), and AuNPs (blue trace). Digital photographs (inset) of laccase and laccase−Au hybrids.
7. Figure 13.7 Scheme of the synthesis of heterogeneous AgNPs–silica-ROE biohybrid.
8. Figure 13.8 (a) SEM image and (b) TEM of AgNPs–nanosilica-RO hybrid.
9. Figure 13.9 SEM images of the different urease–Cu nanoflowers at different Cu²⁺ concentration, (a) 0.8 mM, (b) 8 mM, and (c) 80 mM.
10. Figure 13.10 (a) SEM image of CAL-B–Cu nanostructure (inset is the SEM image showing the 3D nanostructure of composites at high resolution); (b) SEM image of CAL-B–copper nanoparticles without PVP (CAL-B@Cu); (c) SEM image of CAL-B–copper nanoparticles with PVP (CAL-B&PVP@Cu); (d) TEM image of CAL-B–copper nanoparticles with PVP (CAL-B&PVP@Cu); (e) DLS of CAL-B–copper nanoparticles with PVP (CAL-B&PVP@Cu).
11. Figure 13.11 The size-controlled evolution of the PepA–PtNPs biohybrids. Pt precursors were incubated with PepA at a 1000 : 1 molar ratio. Varying incubation times of 1 min (a), 5 (b), 15 (c), 30 (d), and 5 h (e) yielded average complex sizes of 0.9, 1.4, 1.7, 1.9, and 2.1 nm, respectively. Ratio-controlled synthesis of PepA–PtNPs. Pt precursors were incubated with PepA at varying molar ratios of 50 : 1 (f), 100 : 1 (g), 250 : 1 (h), 500 : 1 (i), and 1000 : 1 (j) for 60 min, yielding average complex sizes of 0.9, 1.1, 1.5, 1.7, and 2.0 nm, respectively. Each scale bar represents 20 nm.
12. Scheme 13.1 Synergistic effect on the enzymatic and metal activity on the laccase–AuNP biohybrid in the oxidation of ABTS (2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)). The intensity of the UV–Vis absorption peak, resulting from the oxidation of ABTS, is proportional to the activity of biocatalyst.
13. Scheme 13.2 Transformation of p-nitrophenyl butyrate (1) in p-aminophenol (3) catalyzed by nanobiohybrids.
14. Scheme 13.3 Transformation of glutamic acid–p-nitroanilide (4) in p-phenylenediamine (6) catalyzed by nanobiohybrids.
15. Scheme 13.4 Dynamic kinetic resolution of rac-phenylethylamine (7) via transesterification using different CAL-B–PdNPs biohybrids.

List of Tables

Chapter 1: Preparation of Artificial Metalloenzymes
1. Table 1.1 Covalent modification of hydrolase scaffolds
2. Table 1.2 Covalent modification of amino acids
Chapter 2: Preparation of MetalloDNAzymes
1. Table 2.1 A summary of different metalloDNAzymes catagorized by reaction type and metal ion cofactor
2. Table 2.2 Cu(II) bipy-based metal complexes, binding constant, catalytic enantioselectivity, and complex interaction
Chapter 3: Experimental Characterization Techniques of Hybrid Catalysts
1. Table 3.1 EPR anisotropic g₁ and g₂ values and magnetic hyperfine coupling tensors (A₁ and A₂) of both subspecies found in Cu^II/HHD-4×ala and Cu^II/CN-4×ala
Chapter 5: Directed Evolution of Artificial Metalloenzymes
1. Table 5.1 Improvement of P450_BM3 for a nonnatural cyclopropanation reaction
2. Table 5.2 Stereoselective cyclopropanation with myoglobin variants
Chapter 7: Hybrid Catalysts for Oxidation Reactions
1. Table 7.1 Hybrid reactivity in oxygen atom transfer
2. Table 7.2 HRP activity of the hybrids cited in this chapter
Chapter 9: Hybrid Catalysts for C−H Activation and Other X−H Insertion Reactions
1. Table 9.1 Selected results for an artificial enantioselective benzannulase based on the biotin–streptavidin technology
2. Table 9.2 Intramolecular C−H insertion using Ir(Me)-Myo variants
3. Table 9.3 Cyclopropanation using evolved Ir(Me)-Myo variants
4. Table 9.4 POP-AzA₄-Rh variants catalyze the asymmetric cyclopropanation of styrene derivatives
5. Table 9.5 Engineered cytochrome P450_BM3 catalyzes carbine transfer reaction for the cyclopropanation of styrene derivatives.^a
6. Table 9.6 Selected results for the cyclopropanation of styrene 23 with EDA 17 using mutated myoglobin as repurposed protein.^a
7. Table 9.7 Selected results for the aziridination using tosyl azide 35 and 4-methylstyrene 34 in E. coli resuspended in M9-N buffer under anaerobic conditions.^a
8. Table 9.8 Engineered cytochrome P450_BM3 variants for benzylic C−H amination reactions
9. Table 9.9 Selected results for the regio-divergent production of enantioenriched sultams employing evolved cytochrome P411_BM3 variants.^a
10. Table 9.10 Evolved myoglobin catalyzes the C−H amination of sulfonylazides 37 and 38 (see Table 9.8 for structures).^a
11. Table 9.11 Cytochrome P450_BM3 catalyzes N−H insertion aniline 53
12. Table 9.12 Myoglobin catalyzes the carbene insertion in aniline derivatives to afford secondary amines.^a,b
13. Table 9.13 Evolved myoglobin catalyzes the carbene S−H insertion in thiophenol.^a
14. Table 9.14 Enantioselectivity of evolved myoglobin for the carbene S−H insertion reaction in the presence of ethyl α-diazopropanoate.^a
15. Table 9.15 Cytochrome P411_BM3 catalyzes the asymmetric nitrene transfer to prochiral sulfides
16. Table 9.16 Substrate scope of the P-5 catalyzed sulfimidation followed by a spontaneous [2,3]-sigmatropic rearrangement.^a
17. Table 9.17 Halogenation of tryptamine derivatives with evolved 8F and 10S RebH enzymes.^a,b
Chapter 10: Hybrid Catalysts for Other C−C and C−X Bond Formation Reactions
1. Table 10.1 Results of the allylic amination of 1,3-diphenylallylacetate with benzylamine and N-benzylmethylamine catalyzed by phosphane-modified deoxyuridine containing monomeric and trimeric oligonucleotide structures
2. Table 10.2 Enantioselectivity of substrate and product of iridium-catalyzed allylic amination of 1-phenylacetate with morpholine diene-modified oligonucleotides with complementary RNA or DNA strands
3. Table 10.3 Comparison of the equivalents of Pd atoms per ferritin and the TOF of the Suzuki reaction of 4-iodoaniline and phenylboronic acid
4. Table 10.4 Enantioselectivities and activities of the different biotinylated cofactors in the synthesis of enantioenriched 2-methoxy-1,1′-binaphthyl.^a
5. Table 10.5 Heck reaction of iodobenzene and ethylacrylate catalyzed by different lipase-based artificial metalloenzymes.^a
6. Table 10.6 Hydroformylation of styrene catalyzed by rhodium-substituted carbonic anhydrase II
7. Table 10.7 Phenylacetylene polymerization catalyzed by different rhodium-modified proteins
8. Table 10.8 Summary of the catalytic performance of different artificial metatheases
Chapter 11: Metal–Enzyme Hybrid Catalysts in Cascade and Multicomponent Processes
1. Table 11.1 Representative metal-based materials for hybridizing with enzymes used in cascade and multicomponent processes
Chapter 13: Synthesis and Application of Hybrid Catalysts with Metalloenzyme-Like Properties
1. Table 13.1 Synthesis of Au–CAL-B bionanohybrids
2. Table 13.2 Synthesis of Ag–CAL-B bionanohybrids
3. Table 13.3 Enzymatic and reductive activities of the different CAL-B–MetalNP biohybrids in transformation of 1 to 3
4. Table 13.4 Enzymatic and reductive activities of the different PepA–PtNPs biohybrids in transformation of 4 to 6

Artificial Metalloenzymes and MetalloDNAzymes in Catalysis

From Design to Applications

Edited by

Montserrat Diéguez
Jan-E. Bäckvall
Oscar Pàmies

The Editors

Professor Montserrat Diéguez

Universitat Rovira i Virgili

Dep. de Química Física i Inorgànica

Campus Sescelades

C/ Marcel.lí Domingo

1. 43007 Tarragona

43007 Tarragona

Spain

Professor Jan-E. Bäckvall

Stockholm University

Department of Organic Chemistry

Arrhenius Laboratory

SE- 106 91 Stockholm

106 91 Stockholm

Sweden

Professor Oscar Pàmies

Universitat Rovira i Virgili

Dep. de Química Física i Inorgànica

Campus Sescelades

C/ Marcel.lí Domingo

1. 43007 Tarragona

43007 Tarragona

Spain

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