2 publications
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A Chaperonin as Protein Nanoreactor for Atom-Transfer Radical Polymerization
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Angew. Chem. Int. Ed. 2014, 53, 1443-1447, 10.1002/anie.201306798
The group II chaperonin thermosome (THS) from the archaea Thermoplasma acidophilum is reported as nanoreactor for atom‐transfer radical polymerization (ATRP). A copper catalyst was entrapped into the THS to confine the polymerization into this protein cage. THS possesses pores that are wide enough to release polymers into solution. The nanoreactor favorably influenced the polymerization of N‐isopropyl acrylamide and poly(ethylene glycol)methylether acrylate. Narrowly dispersed polymers with polydispersity indices (PDIs) down to 1.06 were obtained in the protein nanoreactor, while control reactions with a globular protein–catalyst conjugate only yielded polymers with PDIs above 1.84.
Metal: CuLigand type: N,N,N’,N’-tetraethyldiethylene triamine (TEDETA)Host protein: Thermosome (THS)Anchoring strategy: CovalentOptimization: ---Notes: Non-ROMP
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Catalyst Design in Oxidation Chemistry; from KMnO4 to Artificial Metalloenzymes
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Bioorg. Med. Chem. 2014, 22, 5657-5677, 10.1016/j.bmc.2014.07.002
Oxidation reactions are an important part of the synthetic organic chemist’s toolkit and continued advancements have, in many cases, resulted in high yields and selectivities. This review aims to give an overview of the current state-of-the-art in oxygenation reactions using both chemical and enzymatic processes, the design principles applied to date and a possible future in the direction of hybrid catalysts combining the best of chemical and natural design.
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