15 publications
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A Highly Specific Metal-Activated Catalytic Antibody
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J. Am. Chem. Soc. 1993, 115, 4906-4907, 10.1021/ja00064a068
n/a
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An asymmetric catalyst
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Nature 1956, 178, 323-324, 10.1038/178323b0
Asymmetric synthesis has hitherto succeeded only by using reagents or solvents having the asymmetric configuration.
Metal: PdLigand type: UndefinedHost protein: Silk fibroin fibreAnchoring strategy: UndefinedOptimization: ---Notes: ---
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A Protein-Rhodium Complex as an Efficient Catalyst for Two-Phase Olefin Hydroformylation
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Tetrahedron Lett. 2000, 41, 3717-3720, 10.1016/S0040-4039(00)00473-1
A highly efficient and chemoselective biphasic hydroformylation of olefins was accomplished using water soluble complexes formed by the interaction between Rh(CO)2(acac) and human serum albumin (HSA), a readily available water soluble protein. A new type of shape-selectivity was observed in the hydroformylation of sterically hindered olefins.
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Aqueous Biphasic Hydroformylation Catalysed by Protein-Rhodium Complexes
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Adv. Synth. Catal. 2002, 344, 556, 10.1002/1615-4169(200207)344:5<556::AID-ADSC556>3.0.CO;2-E
The water‐soluble complex derived from Rh(CO)2(acac) and human serum albumin (HSA) proved to be efficient in the hydroformylation of several olefin substrates. The chemoselectivity and regioselectivity were generally higher than those obtained by using the classic catalytic systems like TPPTS‐Rh(I) (TPPTS=triphenylphosphine‐3,3′,3″‐trisulfonic acid trisodium salt). Styrene and 1‐octene, for instance, were converted in almost quantitative yields into the corresponding oxo‐aldehydes at 60 °C and 70 atm (CO/H2=1) even at very low Rh(CO)2(acac)/HSA catalyst concentrations. The possibility of easily recovering the Rh(I) compound makes the system environmentally friendly. The circular dichroism technique was useful for demonstrating the Rh(I) binding to the protein and to give information on the stability in solution of the catalytic system. Some other proteins have been used to replace HSA as complexing agent for Rh(I). The results were less impressive than those obtained using HSA and their complexes with Rh(I) were much less stable.
Metal: RhLigand type: UndefinedHost protein: Human serum albumin (HSA)Anchoring strategy: UndefinedOptimization: ---Notes: ---
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Asymmetric Catalytic Sulfoxidation by a Novel VIV8 Cluster Catalyst in the Presence of Serum Albumin: A Simple and Green Oxidation System
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RSC Adv. 2016, 6, 44154-44162, 10.1039/C6RA08153C
Enantioselective oxidation of a series of alkyl aryl sulfides catalyzed by a novel VIV8 cluster is tested in an aqueous medium in the presence of serum albumin. The procedure is simple, environmentally friendly, selective, and highly reactive.
Metal: VHost protein: Bovine serum albumin (BSA)Anchoring strategy: UndefinedOptimization: ChemicalNotes: Screening with different serum albumins.
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Enantioselective Sulfoxidation Mediated by Vanadium-Incorporated Phytase: A Hydrolase Acting as a Peroxidase
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Chem. Commun. 1998, 1891-1892, 10.1039/a804702b
Phytase (E.C. 3.1.3.8), which in vivo mediates the hydrolysis of phosphate esters, catalyses the enantioselective oxidation of thioanisole with H2O2, both in the presence and absence of vanadate ion, affording the S-sulfoxide in up to 66% ee at 100% conversion.
Metal: VLigand type: UndefinedHost protein: PhytaseAnchoring strategy: UndefinedOptimization: ---Notes: ---
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Metal Incorporated Horseradish Peroxidase (HRP) Catalyzed Oxidation of Resveratrol: Selective Dimerization or Decomposition
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RSC Adv. 2013, 3, 22976, 10.1039/c3ra43784a
Horseradish Peroxidase (HRP) is a commercially available and prevalently used peroxidase with no specific substrate binding domain. However, after being incorporated with different metal cations, new catalytic functions were found in biomimetic oxidation of resveratrol. Based on the results of screening, Ca, Cu, Fe and Mn incorporated enzymes showed distinctive effects, either decomposition or dimerization products were observed.
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Nature-Driven Photochemistry for Catalytic Solar Hydrogen Production: A Photosystem I-Transition Metal Catalyst Hybrid
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J. Am. Chem. Soc. 2011, 133, 16334-16337, 10.1021/ja206012r
Solar energy conversion of water into the environmentally clean fuel hydrogen offers one of the best long-term solutions for meeting future energy demands. Nature provides highly evolved, finely tuned molecular machinery for solar energy conversion that exquisitely manages photon capture and conversion processes to drive oxygenic water-splitting and carbon fixation. Herein, we use one of Nature’s specialized energy-converters, the Photosystem I (PSI) protein, to drive hydrogen production from a synthetic molecular catalyst comprised of inexpensive, earth-abundant materials. PSI and a cobaloxime catalyst self-assemble, and the resultant complex rapidly produces hydrogen in aqueous solution upon exposure to visible light. This work establishes a strategy for enhancing photosynthetic efficiency for solar fuel production by augmenting natural photosynthetic systems with synthetically tunable abiotic catalysts.
Notes: Recalculated TON
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Optimization of and Mechanistic Considerations for the Enantioselective Dihydroxylation of Styrene Catalyzed by Osmate-Laccase-Poly(2-Methyloxazoline) in Organic Solvents
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ChemCatChem 2016, 8, 593-599, 10.1002/cctc.201501083
The Sharpless dihydroxylation of styrene with the artificial metalloenzyme osmate‐laccase‐poly(2‐methyloxazoline) was investigated to find reaction conditions that allow this unique catalyst to reveal its full potential. After changing the co‐oxidizing agent to tert‐butyl hydroperoxide and optimizing the osmate/enzyme ratio, the turnover frequency and the turnover number could be increased by an order of magnitude, showing that the catalyst can compete with classical organometallic catalysts. Varying the metal in the active center showed that osmate is by far the most active catalytic center, but the reaction can also be realized with permanganate and iron(II) salts.
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Protein Delivery of a Ni Catalyst to Photosystem I for Light-Driven Hydrogen Production
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J. Am. Chem. Soc. 2013, 135, 13246-13249, 10.1021/ja405277g
The direct conversion of sunlight into fuel is a promising means for the production of storable renewable energy. Herein, we use Nature’s specialized photosynthetic machinery found in the Photosystem I (PSI) protein to drive solar fuel production from a nickel diphosphine molecular catalyst. Upon exposure to visible light, a self-assembled PSI-[Ni(P2PhN2Ph)2](BF4)2 hybrid generates H2 at a rate 2 orders of magnitude greater than rates reported for photosensitizer/[Ni(P2PhN2Ph)2](BF4)2 systems. The protein environment enables photocatalysis at pH 6.3 in completely aqueous conditions. In addition, we have developed a strategy for incorporating the Ni molecular catalyst with the native acceptor protein of PSI, flavodoxin. Photocatalysis experiments with this modified flavodoxin demonstrate a new mechanism for biohybrid creation that involves protein-directed delivery of a molecular catalyst to the reducing side of Photosystem I for light-driven catalysis. This work further establishes strategies for constructing functional, inexpensive, earth-abundant solar fuel-producing PSI hybrids that use light to rapidly produce hydrogen directly from water.
Metal: NiLigand type: PhosphineHost protein: Flavodoxin (Fld)Anchoring strategy: SupramolecularOptimization: ---Notes: Recalculated TON
Metal: NiLigand type: PhosphineHost protein: Photosystem I (PSI)Anchoring strategy: UndefinedOptimization: ---Notes: Recalculated TON
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Proteins as Macromolecular Ligands for Metal-Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium
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Eur. J. Inorg. Chem. 2018, 2018, 1383-1393, 10.1002/ejic.201701359
Biohybrid catalysts resulting from the dative anchoring of half‐sandwich organometallic complexes [M(arene)(H2O)x(Cl)y]n+ (M = RuII, arene = η6‐benzene, p‐cymene or mesitylene; M = IrIII, RhIII, arene = η5‐Cp*; x = 1–3, y = 0–2, n = 0–2) to bovine beta‐lactoglobulin (βLG) or hen egg white lysozyme showed unprecedented behaviour. These constructs were shown to catalyse the asymmetric transfer hydrogenation of aryl ketones in water with sodium formate as hydrogen donor at a much faster rate than the complexes alone. Full conversion of the benchmark substrate 2,2,2‐trifluoroacetophenone was reached with an ee of 86 % for the most selective biohybrid. Surprisingly, even the crude biohybrid gave a good ee despite the presence of non‐protein‐bound metal species in the reaction medium. Other aryl ketones were reduced in the same way, and the highest ee was obtained for ortho‐substituted acetophenone derivatives. Furthermore, treatment of βLG with dimethyl pyrocarbonate resulted in a noticeable decrease of the activity and selectivity of the biohybrid, indicating that the sole accessible histidine residue (His146) was probably involved in the coordination and activation of Ru(benzene). This work underscores that protein scaffolds are efficient chiral ligands for asymmetric catalysis. The use of sodium formate instead of dihydrogen makes this approach safe, inexpensive and environmentally friendly.
Metal: RuLigand type: Benzene derivativesHost protein: Bovine β-lactoglobulin (βLG)Anchoring strategy: UndefinedOptimization: ---Notes: ---
Metal: RhLigand type: Cp*Host protein: Bovine β-lactoglobulin (βLG)Anchoring strategy: UndefinedOptimization: ---Notes: ---
Metal: IrLigand type: Cp*Host protein: Bovine β-lactoglobulin (βLG)Anchoring strategy: UndefinedOptimization: ---Notes: ---
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Stereoselective Sulfoxidation Catalyzed by Achiral Schiff Base Complexes in the Presence of Serum Albumin in Aqueous Media
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Tetrahedron: Asymmetry 2017, 28, 1700-1707, 10.1016/j.tetasy.2017.10.021
Four coordination complexes ML derived from an achiral Schiff base ligand (H2L = 2,2′-[(1,2-ethanediyl)bis(nitrilopropylidyne)]bisphenol) have been synthesized and characterized. A method is described for the enantioselective oxidation of a series of aryl alkyl sulfides using the coordination complexes in the presence of serum albumins (SAs) in an aqueous medium at ambient temperature. The mixture of metal complexes with serum albumins is useful for inducing asymmetric catalysis. The complex, albumin source and substrate influence stereoselective sulfoxidation. At optimal pH with the appropriate oxidant, some of ML/SA systems are identified as very efficient catalysts, giving the corresponding sulfoxides in excellent chemical yield (up to 100%) and good enantioselectivity (up to 94% ee) in certain cases. UV–visible spectroscopic data provide evidence that stronger binding between the complex and serum albumin lead to higher enantioselectivity.
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The Bovine Serum Albumin-2-Phenylpropane-1,2-diolatodioxoosmium(VI) Complex as an Enantioselective Catalyst for cis-Hydroxylation of Alkenes
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J. Chem. Soc., Chem. Commun. 1983, 0, 769-770, 10.1039/C39830000769
The 1:1 complex between an osmate ester and bovine serum albumin was found to be effective as an enantioselective catalyst in the cis-hydroxylation of alkenes, affording diols in up to 68% e.e. and turnover of the catalyst with t-butyl hydroperoxide.
Metal: OsLigand type: UndefinedHost protein: Bovine serum albumin (BSA)Anchoring strategy: UndefinedOptimization: ---Notes: ---
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The Rational Design of Semisynthetic Peroxidases
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Biotechnol. Bioeng. 2000, 67, 87-96, 10.1002/(SICI)1097-0290(20000105)67:1<87::AID-BIT10>3.0.CO;2-8
A semisynthetic peroxidase was designed by exploiting the structural similarity of the active sites of vanadium dependent haloperoxidases and acid phosphatases. Incorporation of vanadate ion into the active site of phytase (E.C. 3.1.3.8), which mediates in vivo the hydrolysis of phosphate esters, leads to the formation of a semisynthetic peroxidase, which catalyzes the enantioselective oxidation of prochiral sulfides with H2O2 affording the S‐sulfoxide, e.g. in 66% ee at 100% conversion for thioanisole. Under reaction conditions the semi‐synthetic vanadium peroxidase is stable for over 3 days with only a slight decrease in turnover frequency. Polar water‐miscible cosolvents, such as methanol, dioxane, and dimethoxyethane, can be used in concentrations of 30% (v/v) at a small penalty in activity and enantioselectivity. Among the transition metal oxoanions that are known to be potent inhibitors, only vanadate resulted in a semisynthetic peroxidase when incorporated into phytase. A number of other acid phosphatases and hydrolases were tested for peroxidase activity, when incorporated with vanadate ion. Phytases from Aspergillus ficuum, A. fumigatus, and A. nidulans, sulfatase from Helix pomatia, and phospholipase D from cabbage catalyzed enantioselective oxygen transfer reactions when incorporated with vanadium. However, phytase from A. ficuum was unique in also catalyzing the enantioselective sulfoxidation, albeit at a lower rate, in the absence of vanadate ion.
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Vanadium-Catalysed Enantioselective Sulfoxidations: Rational Design of Biocatalytic and Biomimetic Systems
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Top. Catal. 2000, 13, 259-265, 10.1023/A:1009094619249
Approaches to the rational design of vanadium-based biocatalytic and biomimetic model systems as catalysts for enantioselective oxidations are reviewed. Incorporation of vanadate ion into the active site of phytase (E.C. 3.1.3.8), which in vivo mediates the hydrolysis of phosphate esters, afforded a relatively stable and inexpensive semi-synthetic peroxidase. It catalysed the enantioselective oxidation of prochiral sulfides with H2O2 affording the S-sulfoxide, e.g., in 68% ee at 100% conversion for thioanisole. Amongst the transition metal oxoanions that are known to be potent inhibitors of phosphatases, only vanadate resulted in a semi-synthetic peroxidase, when incorporated into phytase. In a biomimetic approach, vanadium complexes of chiral Schiff's base complexes were encapsulated in the super cages of a hydrophobic zeolite Y. Unfortunately, these ship-in-a-bottle complexes afforded only racemic sulfoxide in the catalytic oxidation of thioanisole with H2O2.