Horseradish peroxidase as a catalyst for atom transfer radical polymerization

Severin J. Sigg; Farzad Seidi; Kasper Renggli; Tilana B. Silva; Gergely Kali; Nico Bruns

doi:10.1002/marc.201100349

Horseradish peroxidase as a catalyst for atom transfer radical polymerization

Severin J. Sigg, Farzad Seidi, Kasper Renggli, Tilana B. Silva, Gergely Kali, Nico Bruns^*

^*Corresponding author for this work

Pure And Applied Chemistry

Research output: Contribution to journal › Article › peer-review

130 Citations (Scopus)

Abstract

The hemoprotein horseradish peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, M̄ _n and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.

Original language	English
Pages (from-to)	1710-1715
Number of pages	6
Journal	Macromolecular Rapid Communications
Volume	32
Issue number	21
DOIs	https://doi.org/10.1002/marc.201100349
Publication status	Published - 1 Nov 2011

Keywords

atom transfer radical polymerization (ATRP)
catalysts
enzymes
green chemistry
heme proteins

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title = "Horseradish peroxidase as a catalyst for atom transfer radical polymerization",

abstract = "The hemoprotein horseradish peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, {\=M} n and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.",

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T1 - Horseradish peroxidase as a catalyst for atom transfer radical polymerization

AU - Sigg, Severin J.

AU - Seidi, Farzad

AU - Renggli, Kasper

AU - Silva, Tilana B.

AU - Kali, Gergely

AU - Bruns, Nico

PY - 2011/11/1

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N2 - The hemoprotein horseradish peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, M̄ n and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.

AB - The hemoprotein horseradish peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.44 are obtained. The polymerization follows first order kinetics, but the evolution of molecular weight and the PDI upon increasing conversion deviate from the results expected for an ATRP mechanism. Conversion, M̄ n and PDI depend on the pH and on the concentration of the reducing agent, sodium ascorbate. HRP is stable during the polymerization and does not unfold or form conjugates.

KW - atom transfer radical polymerization (ATRP)

KW - catalysts

KW - enzymes

KW - green chemistry

KW - heme proteins

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Horseradish peroxidase as a catalyst for atom transfer radical polymerization

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Keywords

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