Artificial metalloenzymes as catalysts for oxidative lignin degradation

Megan Doble; Amanda Jarvis; Andy Ward; Jonathan David Colburn; Jan Philipp Goetze; Michael Buehl; Paul C J Kamer

doi:10.1021/acssuschemeng.8b03568

Artificial metalloenzymes as catalysts for oxidative lignin degradation

Megan Doble, Amanda Jarvis, Andy Ward, Jonathan David Colburn, Jan Philipp Goetze, Michael Buehl, Paul C J Kamer

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

Abstract

We report novel artificial metalloenzymes (ArMs), containing tris(pyridylmethyl)amine (TPA), for the atom economic oxidation of lignin β-O-4 model compounds, using hydrogen peroxide. The protein scaffold alters the selectivity of the reaction from a low yielding cleavage reaction when using the parent Fe-tpa complex to a high yielding benzylic alcohol oxidation when using the complex incorporated into a protein scaffold, SCP-2L A100C. Engineering the protein scaffold to incorporate glutamic acid was found to improve the ArM activity, showing that rational design of the protein environment using metal binding amino acids can be a first step towards improving the overall activity of an artificial metalloenzyme.

Original language	English
Pages (from-to)	15100-15107
Number of pages	8
Journal	ACS Sustainable Chemistry & Engineering
Volume	6
Issue number	11
Early online date	10 Oct 2018
DOIs	https://doi.org/10.1021/acssuschemeng.8b03568
Publication status	Published - 5 Nov 2018

Keywords

Lignin
Artificial metalloenzymes
Catalytic oxidation

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10.1021/acssuschemeng.8b03568

pubArM-LigninOx-finalrevised
Copyright © 2018 American Chemical Society. This work has been made available online in accordance with the publisher’s policies. This is the author created accepted version manuscript following peer review and as such may differ slightly from the final published version. The final published version of this work is available at https://doi.org/10.1021/acssuschemeng.8b03568
Accepted author manuscript, 1.25 MB

Artoxizymes: Artificial Oxidation Enzymes for Highly Selective Waste Free Hydroxylation of Alkanes
Kamer, P. C. J. (PI)
European Commission
1/10/15 → 30/09/17
Project: Fellowship
SUBICAT: SUBICAT
Kamer, P. C. J. (PI)
Marie Curie Fellowships
1/10/13 → 30/09/17
Project: Standard
Clean catalysis for sustainable develop: Clean catalysis for sustainable development
Kamer, P. C. J. (PI)
EPSRC
1/11/12 → 31/10/17
Project: Standard

Computational data for "Artificial Metalloenzymes as Catalysts for Oxidative Lignin Degradation"
Colburn, J. D. (Creator), Goetze, J. P. (Creator) & Buehl, M. (Creator), University of St Andrews, 2018
DOI: 10.17630/259affa7-75ae-495f-8d2a-7d9742d3ef13
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title = "Artificial metalloenzymes as catalysts for oxidative lignin degradation",

abstract = "We report novel artificial metalloenzymes (ArMs), containing tris(pyridylmethyl)amine (TPA), for the atom economic oxidation of lignin β-O-4 model compounds, using hydrogen peroxide. The protein scaffold alters the selectivity of the reaction from a low yielding cleavage reaction when using the parent Fe-tpa complex to a high yielding benzylic alcohol oxidation when using the complex incorporated into a protein scaffold, SCP-2L A100C. Engineering the protein scaffold to incorporate glutamic acid was found to improve the ArM activity, showing that rational design of the protein environment using metal binding amino acids can be a first step towards improving the overall activity of an artificial metalloenzyme. ",

keywords = "Lignin, Artificial metalloenzymes, Catalytic oxidation",

author = "Megan Doble and Amanda Jarvis and Andy Ward and Colburn, {Jonathan David} and Goetze, {Jan Philipp} and Michael Buehl and Kamer, {Paul C J}",

note = "M.V.D thanks the BBSRC for support through an EastBio studentship BB/J01446X/1. The authors thank the EPSRC for funding through the EPSRC critical mass grant “Clean catalysis for sustainable development” (EP/J018139/1). This work was supported by the EU the European Union (Marie Curie ITN “SuBiCat” PITN-GA-2013-60704 (P.C.J.K), and through a Marie Curie Individual Fellowship project ArtOxiZymes to A.G.J. (H2020-MSCA-IF-2014- 657755). A.G.J would also like to thank the University of Edinburgh for funding through a Christina Miller Fellowship. The UK Catalysis Hub is kindly thanked for resources and support provided via our membership of the UK Catalysis Hub Consortium, which is funded by the EPSRC (EP/K014706/2, EP/K014668/1, EP/K014854/1, EP/K014714/1, and EP/M013219/1).",

year = "2018",

month = nov,

day = "5",

doi = "10.1021/acssuschemeng.8b03568",

language = "English",

volume = "6",

pages = "15100--15107",

journal = "ACS Sustainable Chemistry & Engineering",

issn = "2168-0485",

publisher = "American Chemical Society (ACS)",

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T1 - Artificial metalloenzymes as catalysts for oxidative lignin degradation

AU - Doble, Megan

AU - Jarvis, Amanda

AU - Ward, Andy

AU - Colburn, Jonathan David

AU - Goetze, Jan Philipp

AU - Buehl, Michael

AU - Kamer, Paul C J

N1 - M.V.D thanks the BBSRC for support through an EastBio studentship BB/J01446X/1. The authors thank the EPSRC for funding through the EPSRC critical mass grant “Clean catalysis for sustainable development” (EP/J018139/1). This work was supported by the EU the European Union (Marie Curie ITN “SuBiCat” PITN-GA-2013-60704 (P.C.J.K), and through a Marie Curie Individual Fellowship project ArtOxiZymes to A.G.J. (H2020-MSCA-IF-2014- 657755). A.G.J would also like to thank the University of Edinburgh for funding through a Christina Miller Fellowship. The UK Catalysis Hub is kindly thanked for resources and support provided via our membership of the UK Catalysis Hub Consortium, which is funded by the EPSRC (EP/K014706/2, EP/K014668/1, EP/K014854/1, EP/K014714/1, and EP/M013219/1).

PY - 2018/11/5

Y1 - 2018/11/5

N2 - We report novel artificial metalloenzymes (ArMs), containing tris(pyridylmethyl)amine (TPA), for the atom economic oxidation of lignin β-O-4 model compounds, using hydrogen peroxide. The protein scaffold alters the selectivity of the reaction from a low yielding cleavage reaction when using the parent Fe-tpa complex to a high yielding benzylic alcohol oxidation when using the complex incorporated into a protein scaffold, SCP-2L A100C. Engineering the protein scaffold to incorporate glutamic acid was found to improve the ArM activity, showing that rational design of the protein environment using metal binding amino acids can be a first step towards improving the overall activity of an artificial metalloenzyme.

AB - We report novel artificial metalloenzymes (ArMs), containing tris(pyridylmethyl)amine (TPA), for the atom economic oxidation of lignin β-O-4 model compounds, using hydrogen peroxide. The protein scaffold alters the selectivity of the reaction from a low yielding cleavage reaction when using the parent Fe-tpa complex to a high yielding benzylic alcohol oxidation when using the complex incorporated into a protein scaffold, SCP-2L A100C. Engineering the protein scaffold to incorporate glutamic acid was found to improve the ArM activity, showing that rational design of the protein environment using metal binding amino acids can be a first step towards improving the overall activity of an artificial metalloenzyme.

KW - Lignin

KW - Artificial metalloenzymes

KW - Catalytic oxidation

U2 - 10.1021/acssuschemeng.8b03568

DO - 10.1021/acssuschemeng.8b03568

M3 - Article

SN - 2168-0485

VL - 6

SP - 15100

EP - 15107

JO - ACS Sustainable Chemistry & Engineering

JF - ACS Sustainable Chemistry & Engineering

IS - 11

ER -

Artificial metalloenzymes as catalysts for oxidative lignin degradation

Abstract

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Artoxizymes: Artificial Oxidation Enzymes for Highly Selective Waste Free Hydroxylation of Alkanes

SUBICAT: SUBICAT

Clean catalysis for sustainable develop: Clean catalysis for sustainable development

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Computational data for "Artificial Metalloenzymes as Catalysts for Oxidative Lignin Degradation"

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