Biocatalytic ATRP: controlled radical polymerizations mediated by enzymes

Kasper Renggli, Mariana Spulber, Jonas Pollard, Martin Rother, Nico Bruns

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

3 Citations (Scopus)

Abstract

The advent of controlled radical polymerizations has made polymer science a key discipline for the preparation of nano-, biomedical-, and high tech-materials. Atom transfer radical polymerization (ATRP) is one of the most widely applied controlled radical polymerization. However, an ongoing quest is to develop ATRP reaction conditions that allow reducing the amount of catalyst needed, or to replace the currently used transition metal complex catalysts with less toxic ones. Using enzymes as catalysts is a classic strategy in the green chemistry approach, and many enzymatic polymerizations are known. However, controlled radical polymerizations that are catalyzed by enzymes or proteins were not known until our discovery that the metalloproteins horseradish peroxidase and hemoglobin can polymerize vinyl-monomers under conditions of activators regenerated by electron transfer (ARGET) ATRP. In this book chapter, we review the emerging field of biocatalytic ATRP.

LanguageEnglish
Title of host publicationGreen Polymer Chem
Subtitle of host publicationBiocatalysis and Materials II
PublisherAmerican Chemical Society
Pages163-171
Number of pages9
Volume1144
ISBN (Print)9780841228955
DOIs
Publication statusPublished - 1 Jan 2013

Publication series

NameACS Symposium Series
Volume1144
ISSN (Print)0097-6156
ISSN (Electronic)1947-5918

Fingerprint

Atom transfer radical polymerization
Free radical polymerization
Enzymes
Catalysts
Metalloproteins
Poisons
Hemoglobin
Coordination Complexes
Horseradish Peroxidase
Metal complexes
Transition metals
Polymers
Hemoglobins
Monomers
Polymerization
Proteins
Electrons

Keywords

  • enzymatic polymerization
  • catalysts
  • enzymes
  • free radical polymerization
  • functional polymers
  • metal complexes
  • proteins
  • transition metal compounds
  • atom transfer radical polymerization
  • green chemistry approaches

Cite this

Renggli, K., Spulber, M., Pollard, J., Rother, M., & Bruns, N. (2013). Biocatalytic ATRP: controlled radical polymerizations mediated by enzymes. In Green Polymer Chem: Biocatalysis and Materials II (Vol. 1144, pp. 163-171). (ACS Symposium Series; Vol. 1144). American Chemical Society. https://doi.org/10.1021/bk-2013-1144.ch012
Renggli, Kasper ; Spulber, Mariana ; Pollard, Jonas ; Rother, Martin ; Bruns, Nico. / Biocatalytic ATRP : controlled radical polymerizations mediated by enzymes. Green Polymer Chem: Biocatalysis and Materials II. Vol. 1144 American Chemical Society, 2013. pp. 163-171 (ACS Symposium Series).
@inbook{d123d3ed62fe49db8d7145b688ff9d0d,
title = "Biocatalytic ATRP: controlled radical polymerizations mediated by enzymes",
abstract = "The advent of controlled radical polymerizations has made polymer science a key discipline for the preparation of nano-, biomedical-, and high tech-materials. Atom transfer radical polymerization (ATRP) is one of the most widely applied controlled radical polymerization. However, an ongoing quest is to develop ATRP reaction conditions that allow reducing the amount of catalyst needed, or to replace the currently used transition metal complex catalysts with less toxic ones. Using enzymes as catalysts is a classic strategy in the green chemistry approach, and many enzymatic polymerizations are known. However, controlled radical polymerizations that are catalyzed by enzymes or proteins were not known until our discovery that the metalloproteins horseradish peroxidase and hemoglobin can polymerize vinyl-monomers under conditions of activators regenerated by electron transfer (ARGET) ATRP. In this book chapter, we review the emerging field of biocatalytic ATRP.",
keywords = "enzymatic polymerization, catalysts, enzymes, free radical polymerization, functional polymers, metal complexes, proteins, transition metal compounds, atom transfer radical polymerization, green chemistry approaches",
author = "Kasper Renggli and Mariana Spulber and Jonas Pollard and Martin Rother and Nico Bruns",
year = "2013",
month = "1",
day = "1",
doi = "10.1021/bk-2013-1144.ch012",
language = "English",
isbn = "9780841228955",
volume = "1144",
series = "ACS Symposium Series",
publisher = "American Chemical Society",
pages = "163--171",
booktitle = "Green Polymer Chem",
address = "United States",

}

Renggli, K, Spulber, M, Pollard, J, Rother, M & Bruns, N 2013, Biocatalytic ATRP: controlled radical polymerizations mediated by enzymes. in Green Polymer Chem: Biocatalysis and Materials II. vol. 1144, ACS Symposium Series, vol. 1144, American Chemical Society, pp. 163-171. https://doi.org/10.1021/bk-2013-1144.ch012

Biocatalytic ATRP : controlled radical polymerizations mediated by enzymes. / Renggli, Kasper; Spulber, Mariana; Pollard, Jonas; Rother, Martin; Bruns, Nico.

Green Polymer Chem: Biocatalysis and Materials II. Vol. 1144 American Chemical Society, 2013. p. 163-171 (ACS Symposium Series; Vol. 1144).

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

TY - CHAP

T1 - Biocatalytic ATRP

T2 - controlled radical polymerizations mediated by enzymes

AU - Renggli, Kasper

AU - Spulber, Mariana

AU - Pollard, Jonas

AU - Rother, Martin

AU - Bruns, Nico

PY - 2013/1/1

Y1 - 2013/1/1

N2 - The advent of controlled radical polymerizations has made polymer science a key discipline for the preparation of nano-, biomedical-, and high tech-materials. Atom transfer radical polymerization (ATRP) is one of the most widely applied controlled radical polymerization. However, an ongoing quest is to develop ATRP reaction conditions that allow reducing the amount of catalyst needed, or to replace the currently used transition metal complex catalysts with less toxic ones. Using enzymes as catalysts is a classic strategy in the green chemistry approach, and many enzymatic polymerizations are known. However, controlled radical polymerizations that are catalyzed by enzymes or proteins were not known until our discovery that the metalloproteins horseradish peroxidase and hemoglobin can polymerize vinyl-monomers under conditions of activators regenerated by electron transfer (ARGET) ATRP. In this book chapter, we review the emerging field of biocatalytic ATRP.

AB - The advent of controlled radical polymerizations has made polymer science a key discipline for the preparation of nano-, biomedical-, and high tech-materials. Atom transfer radical polymerization (ATRP) is one of the most widely applied controlled radical polymerization. However, an ongoing quest is to develop ATRP reaction conditions that allow reducing the amount of catalyst needed, or to replace the currently used transition metal complex catalysts with less toxic ones. Using enzymes as catalysts is a classic strategy in the green chemistry approach, and many enzymatic polymerizations are known. However, controlled radical polymerizations that are catalyzed by enzymes or proteins were not known until our discovery that the metalloproteins horseradish peroxidase and hemoglobin can polymerize vinyl-monomers under conditions of activators regenerated by electron transfer (ARGET) ATRP. In this book chapter, we review the emerging field of biocatalytic ATRP.

KW - enzymatic polymerization

KW - catalysts

KW - enzymes

KW - free radical polymerization

KW - functional polymers

KW - metal complexes

KW - proteins

KW - transition metal compounds

KW - atom transfer radical polymerization

KW - green chemistry approaches

UR - http://www.scopus.com/inward/record.url?scp=84905223160&partnerID=8YFLogxK

U2 - 10.1021/bk-2013-1144.ch012

DO - 10.1021/bk-2013-1144.ch012

M3 - Chapter (peer-reviewed)

SN - 9780841228955

VL - 1144

T3 - ACS Symposium Series

SP - 163

EP - 171

BT - Green Polymer Chem

PB - American Chemical Society

ER -

Renggli K, Spulber M, Pollard J, Rother M, Bruns N. Biocatalytic ATRP: controlled radical polymerizations mediated by enzymes. In Green Polymer Chem: Biocatalysis and Materials II. Vol. 1144. American Chemical Society. 2013. p. 163-171. (ACS Symposium Series). https://doi.org/10.1021/bk-2013-1144.ch012