Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin

Collot, Jérôme; Gradinaru, Julieta; Humbert, Nicolas; Skander, Myriem; Zocchi, and Andrea; Ward, Thomas R.

doi:10.1021/ja035545i

Cited by 254 publications

(203 citation statements)

References 28 publications

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“…On the other hand, creating sufficiently hydrophobic domains around the catalytic sites to ensure compatibility of the homogeneous organo-or metal-based catalysts with aqueous environments has remained a major challenge. [1][2][3] For this reason, artificial metalloenzymes, [4][5][6] DNA-based catalysts, 7 amphiphilic copolymers, [8][9][10] star polymers, [11][12][13][14][15] micellar systems, [16][17][18][19][20] molecularly imprinted nano and microgels, [21][22][23] and dendrimers [24][25][26][27][28] were designed to achieve the necessary compartmentalization for efficient catalysis in water. Supramolecular folding of polymer chains into single chain polymeric nanoparticles (SCPNs) is an attractive alternative to prepare compartmentalized, water-soluble, nanometersized particles with a hydrophobic interior.…”

Section: Introductionmentioning

confidence: 99%

Understanding the catalytic activity of single‐chain polymeric nanoparticles in water

Artar

Terashima

Sawamoto

et al. 2013

J. Polym. Sci. Part A: Polym. Chem.

110

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ABSTRACT:The structuring role of benzene-1,3,5-tricarboxamide (BTA) groups for the catalytic activity of single chain polymeric nanoparticles in water was investigated in the transfer hydrogenation of ketones. To this end, a set of segmented, amphiphilic copolymers was prepared, which comprised oligo (ethylene glycol) side chains to impart water solubility, BTA and/or lauryl side chains to induce hydrophobicity and diphenylphosphinostyrene (SDP) units in the middle part as a ligand to bind a ruthenium catalyst. All copolymers were obtained by reversible addition-fragmentation chain transfer (RAFT) polymerization and showed low dispersities (M w /M n 5 1.23-1.38) and controlled molecular weights (M n 5 44-28 kDa). A combination of circular dichroism (CD) spectroscopy and dynamic light scattering (DLS) showed that all copolymers fold into a single chain polymeric nanoparticles (SCPNs) as a result of the helical selfassembly of the pendant BTA units and/or hydrophilic-hydrophobic phase separation. To create catalytic sites, RuCl 2 (PPh 3 ) 3 was incorporated into the copolymers. The Cotton effects of the copolymers before and after Ru(II) loading were identical, indicating that the helical self-assembly of the BTA units and the complexation of SDP ligands and Ru(II) occurs in an orthogonal manner. DLS revealed that after Ru(II) loading, SDP-bearing copolymers retained their single chain character in water, while copolymers lacking SDP units clustered into larger aggregates. The Ru(II) loaded SCPNs were tested in the transfer hydrogenation of cyclohexanone. This study reveals that BTA induced stack formation is not crucial for SCPN formation and catalytic activity; SDP-bearing copolymers folded by Ru(II) complexation and hydrophobic pendants suffice to provide hydrophobic, isolated reaction pockets around Ru(II) complexes. V C 2013 Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2014, 52,[12][13][14][15][16][17][18][19][20]

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Section: Introductionmentioning

confidence: 99%

Understanding the catalytic activity of single‐chain polymeric nanoparticles in water

Artar

Terashima

Sawamoto

et al. 2013

J. Polym. Sci. Part A: Polym. Chem.

110

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“…[23][24][25][26][27][28][29][30] Inspired by the early works of Whitesides and Wilson, [22] we recently reported artificial metalloenzymes based on the biotin-avidin technology. [31][32][33][34][35] Herein, we report our efforts to produce substrate-specific and S-selective artificial metalloenzymes based on the biotin-avidin technology for the hydrogenation of a-acetamidodehydroamino acids.The starting point for the chemogenetic-optimization procedure presented herein is the identification of [Rh(cod)-(biot-1)] + &S112G Sav (cod = 1,5-cyclooctadiene, biot =[*] Dr. …”

mentioning

confidence: 99%

Tailoring the Active Site of Chemzymes by Using a Chemogenetic‐Optimization Procedure: Towards Substrate‐Specific Artificial Hydrogenases Based on the Biotin–Avidin Technology

et al. 2005

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Dedicated to Professor George M. WhitesidesCatalysis offers efficient means to produce enantiopure products. Traditionally, enzymatic and homogeneous catalysis have evolved independently to afford mild, robust, active, and highly selective catalysts. [1, 2] Both systems are often considered complementary in terms of substrate and reaction scope, operating conditions, enantioselectivity mechanism, reaction medium, etc. For the optimization of activity and selectivity, directed-evolution methodologies (combined with an efficient selection or screening tool) outperform combinatorial ligand libraries. [3][4][5][6][7][8][9][10][11][12][13] With the hope of alleviating some of the inherent limitations of both enzymatic and organometallic catalysis, two approaches have recently witnessed a revival: 1) organocatalysis [14][15][16][17][18][19] and 2) artificial metalloenzymes based on either covalent [20,21] or supramolecular anchoring [22] of a catalytic moiety in a macromolecular host. [23][24][25][26][27][28][29][30] Inspired by the early works of Whitesides and Wilson, [22] we recently reported artificial metalloenzymes based on the biotin-avidin technology. [31][32][33][34][35] Herein, we report our efforts to produce substrate-specific and S-selective artificial metalloenzymes based on the biotin-avidin technology for the hydrogenation of a-acetamidodehydroamino acids.The starting point for the chemogenetic-optimization procedure presented herein is the identification of [Rh(cod)-(biot-1)] + &S112G Sav (cod = 1,5-cyclooctadiene, biot =[*] Dr.

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“…We are interested in producing artificial metalloenzymes based on the biotin-avidin technology [22]. The possibility, given by P. pastoris, to obtain active avidin directly in the medium provides an attractive alternative to other expression systems, thus allowing one to screen directly the culture medium as well as to conveniently perform directed-evolution experiments.…”

mentioning

confidence: 99%

Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris

Zocchi

Jobé

Neuhaus

et al. 2003

Protein Expression and Purification

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A recombinant glycosylated avidin (recGAvi) with an acidic isoelectric point was expressed and secreted by the methylotrophic yeast Pichia pastoris. The coding sequence for recGAvi was de novo synthesized based on the codon usage of P. pastoris. RecGAvi is secreted at approximately 330 mg/L of culture supernatant. RecGAvi monomer displays a molecular weight of 16.5 kDa, as assessed by ESI mass spectrometry. N-terminal amino acid sequencing indicates the presence of three additional amino acids (E-A-E), which contribute to further lowering the isoelectric point to 5.4. The data presented here demonstrate that the P. pastoris system is suitable for the production of recGAvi and that the recombinant avidin displays biotin-binding properties similar to those of the hen-egg white protein.

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Artificial Metalloenzymes for Enantioselective Catalysis Based on Biotin−Avidin

Cited by 254 publications

References 28 publications

Understanding the catalytic activity of single‐chain polymeric nanoparticles in water

Understanding the catalytic activity of single‐chain polymeric nanoparticles in water

Tailoring the Active Site of Chemzymes by Using a Chemogenetic‐Optimization Procedure: Towards Substrate‐Specific Artificial Hydrogenases Based on the Biotin–Avidin Technology

Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris

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