Structural Basis for Enantioselectivity in the Transfer Hydrogenation of a Ketone Catalyzed by an Artificial Metalloenzyme

Cherrier, M.V.; Engilberge, S.; Amara, Patricia; Chevalley, Alice; Salmain, Michèle; Fontecilla‐Camps, J.C.

doi:10.1002/ejic.201300592

Cited by 24 publications

(9 citation statements)

References 43 publications

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“…Notably, the organometallic heads of all of the considered ligands do not establish any strong interaction with the protein residues, thus suggesting the presence of different conformations after the formation of the protein–ligand complex. This is in full agreement with the electron‐density map derived from X‐ray diffraction of a similar metal complex bound to β‐LG (PDB code 4KII) . However, visual inspection of the obtained poses indicates the presence of polar and charged residues potentially able to establish strong H‐bond interactions with H‐bond acceptors or donors carried by the organometallic head.…”

Section: Resultssupporting

confidence: 83%

Supramolecular Anchoring of NCN‐Pincer Palladium Complexes into a β‐Barrel Protein Host: Molecular‐Docking and Reactivity Insights

et al. 2017

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Several prochiral NCN pincer complexes of palladium(II) including hemilabile ligands and a long aliphatic chain were synthesized and characterized spectroscopically. In some of the complexes, the presence of two different substituents on the N donor atoms made them stereogenic so that they were isolated as a mixture of diastereoisomers, which could be differentiated by 1 H NMR. Binding of some of these complexes to bovine b-lactoglobin by insertion within its inner cavity was theoretically investigated by molecular docking simulations and experimentally confirmed by CD spectroscopy.Adjunction of H-bond donor substituents on the ligand framework gave more stable supramolecular protein -complex assemblies. These constructs were shown to catalyze aldol condensation reactions in aqueous medium affording in some cases the less favorable cis-product. Since the corresponding complexes gave exclusively the trans product in the absence of b-lactoglobulin, this unusual diastereoselectivity was ensued by the second sphere of coordination brought by the protein host.2

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Section: Resultssupporting

confidence: 83%

Supramolecular Anchoring of NCN‐Pincer Palladium Complexes into a β‐Barrel Protein Host: Molecular‐Docking and Reactivity Insights

et al. 2017

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“…For example, Watanabe and coworkers reconstituted myoglobin (Mb) with various Schiff-base complexes, 328 including Cr-salophen 243, which has a similar size and shape to the native Fe-PPIX cofactor (222) Lu later reported on a dual anchoring strategy to fix the orientation of a Mn(salen) cofactor bearing two methane thiosulfonate groups (248,Scheme 76) within an apo myoglobin scaffold containing two cysteine mutations L72C-Y103C ( Figure 15). The resulting ArM catalyzed the sulfoxidation of thioanisole with higher enantioselectivity (51% ee) than an analogous system with only one anchoring point Mb(Y103C) ( Table 32, entries 14-15).…”

Section: Sulfoxidationmentioning

confidence: 99%

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

et al. 2017

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The incorporation of a synthetic, catalytically competent metallocofactor into a protein scaffold to generate an artificial metalloenzyme (ArM) has been explored since the late 1970's. Progress in the ensuing years was limited by the tools available for both organometallic synthesis and protein engineering. Advances in both of these areas, combined with increased appreciation of the potential benefits of combining attractive features of both homogeneous catalysis and enzymatic catalysis, led to a resurgence of interest in ArMs starting in the early 2000's. Perhaps the most intriguing of potential ArM properties is their ability to endow homogeneous catalysts with a genetic memory. Indeed, incorporating a homogeneous catalyst into a genetically encoded scaffold offers the opportunity to improve ArM performance by directed evolution. This capability could, in turn, lead to improvements in ArM efficiency similar to those obtained for natural enzymes, providing systems suitable for practical applications and greater insight into the role of second coordination sphere interactions in organometallic catalysis. Since its renaissance in the early 2000's, different aspects of artificial metalloenzymes have been extensively reviewed and highlighted. Our intent is to provide a comprehensive overview of all work in the field up to December 2016, organized according to reaction class. Because of the wide range of non-natural reactions catalyzed by ArMs, this was done using a functional-group transformation classification. The review begins with a summary of the proteins and the anchoring strategies used to date for the creation of ArMs, followed by a historical perspective. Then follows a summary of the reactions catalyzed by ArMs and a concluding critical outlook. This analysis allows for comparison of similar reactions catalyzed by ArMs constructed using different metallocofactor anchoring strategies, cofactors, protein scaffolds, and mutagenesis strategies. These data will be used to construct a searchable Web site on ArMs that will be updated regularly by the authors.

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“…As the structure of reference protein (BLG) complex with decanol was unknown we also crystallized BLG in the presence of DEC. The crystals of BLG-DEC complex had symmetry of P3 2 21 space group, which is typical for most of the BLG-ligand complexes (Cherrier et al, 2013;Loch et al, 2016;Rovoli et al, 2018). The flexible loops, EF and GH, were in open conformation which is common for bovine lactoglobulin structures determined at pH above 7.5 (Qin et al, 1998).…”

Section: Crystal Structures Of Slg and Blg Complexes With Decanolmentioning

confidence: 95%

Conformational flexibility and ligand binding properties of ovine β-lactoglobulin

2019

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Ovine β‑lactoglobulin was characterized by spectroscopic (CD), calorimetric (ITC) and X-ray structural studies. The structure of ovine β‑lactoglobulin complex with decanol showed that tight packing of molecules in the crystalline phase enforces a distortion of protein flexible loops resulting in the formation of an asymmetric dimer. The loops surrounding β-barrel in ovine lactoglobulin possessed the same conformational flexibility as observed previously in other lactoglobulins and the change of their conformation regulates the access to the binding pocket. The structure of asymmetric dimer revealed a new region in β-barrel where ligand polar group can be located. These findings indicated protein adaptability to ligand dimensions and inter- and intramolecular interactions in the crystalline phase. Calorimetric and crystallographic studies provided the experimental evidence that ovine lactoglobulin is able to bind aliphatic ligands. Thermodynamic parameters of sodium dodecyl sulfate binding determined by ITC at pH 7.5 had Ka, ΔH, TΔS and ΔG values similar to those observed for bovine and caprine protein indicating the same mechanism of ligand binding.

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Structural Basis for Enantioselectivity in the Transfer Hydrogenation of a Ketone Catalyzed by an Artificial Metalloenzyme

Abstract: International audienc

Cited by 24 publications

References 43 publications

Supramolecular Anchoring of NCN‐Pincer Palladium Complexes into a β‐Barrel Protein Host: Molecular‐Docking and Reactivity Insights

Supramolecular Anchoring of NCN‐Pincer Palladium Complexes into a β‐Barrel Protein Host: Molecular‐Docking and Reactivity Insights

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

Conformational flexibility and ligand binding properties of ovine β-lactoglobulin

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