Controlled/living radical polymerizations enable the synthesis of well-defined functional polymers with complex architectures and predetermined molecular weights, as well as narrow molecular weight distributions. Atom transfer radical polymerization (ATRP) has become one of the most widely used polymerization techniques due to its versatility: it can be applied using the majority of common monomers, it allows the addition of functional groups and it is compatible with numerous biomolecules. However, the transition metal catalysts required for ATRP can represent a challenge, as they can be toxic and potentially harmful to the environment. Moreover, the catalysts can have a negative impact on the polymer properties if not fully removed from the product. A �greener� approach involves the use of enzymes as catalysts, so-called �ATRPases�, rather than transition metals. We have discovered that metalloproteins such as horseradish peroxidase (HRP) and hemoglobin catalyze ATRP under activators regenerated by electron transfer (ARGET) conditions.We will present results on biocatalytic ATRP of N-ispopropyl acrylamide, poly(ethylene glycol) methacrylate and poly(ethylene glycol) acrylate. Moreover, mechanistic insights into this novel enzymatic activity will be reported. Last but not least, we will show how ATRPases can be used to conduct ATRP of vinylimidazoles that cannot be polymerized by conventional ATRP.

ATRPases: Iron- and copper-metalloenzymes that catalyze atom transfer radical polymerization

248th National Meeting (2014)

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