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ATRPases: enzymes as catalysts for atom transfer radical polymerization

Sigg, Severin J. and Seidi, Farzad and Renggli, Kasper and Silva, Tilana B. and Kali, Gergely and Bruns, Nico. (2012) ATRPases: enzymes as catalysts for atom transfer radical polymerization. Polymer preprints, Vol. 53, H. 2. pp. 292-293.

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Official URL: http://edoc.unibas.ch/dok/A6083321

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Abstract

Atom transfer radical polymn. (ATRP) is a powerful synthetic tool that is commonly used in polymer chem. This controlled radical polymn. leads to the synthesis of well-defined, end-functionalized polymers with complex mol. architectures. We discovered that heme proteins such as Hb (Hb) and horseradish peroxidase (HRP) catalyze the polymn. of vinyl monomers in the presence of ATRP-initiators and the reducing agent ascorbic acid under conditions typical of activators regenerated by electron transfer (ARGET) ATRP. We call this novel biocatalytic activity ATRPase activity. It yields bromine-terminated polymer chains with polydispersities as low as 1.2. The reaction kinetics were of first order, and for some monomers such as poly(ethylene glycol) Me ether acrylate (PEGA), the polymers' mol. wts. increased with conversion. These findings show that ATRPase activity is a controlled polymn. that involves reversible bromine-atom transfer between the growing polymer chain and the protein. ATRPases could become 'green' alternatives to the transition metal complexes that are currently used as catalysts for ATRP, because proteins are non-toxic, derived from renewable resources, and (e.g. in the case of Hb) cheap and abundantly available.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie
05 Faculty of Science > Departement Chemie > Chemie > Makromolekulare Chemie (Meier)
UniBasel Contributors:Bruns, Nico and Sigg, Severin and Renggli, Kasper
Item Type:Article
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:04 Sep 2015 14:31
Deposited On:24 May 2013 09:01

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