Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose

R. Jason Quinlan; Matt D. Sweeney; Leila Lo Leggio; Harm Otten; Jens-Christian Navarro Poulsen; Katja Salomon Johansen; Kristian B. R. M. Krogh; Christian Isak Jørgensen; Morten Tovborg; Annika Anthonsen; Theodora Tryfona; Theodora Tryfona; Clive P. Walter; Paul Dupree; Feng Xu; Gideon J. Davies; Paul H. Walton

Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose

R. Jason Quinlan, Matt D. Sweeney, Leila Lo Leggio, Harm Otten, Jens-Christian Navarro Poulsen, Katja Salomon Johansen, Kristian B. R. M. Krogh, Christian Isak Jørgensen, Morten Tovborg, Annika Anthonsen, Theodora Tryfona, Theodora Tryfona, Clive P. Walter, Paul Dupree, Feng Xu, Gideon J. Davies, Paul H. Walton

Kemisk Institut

561 Citationer (Scopus)

Abstract

The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of "cellulase-enhancing factors," such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis.

Originalsprog	Engelsk
Tidsskrift	Proceedings of the National Academy of Sciences of the United States of America
Vol/bind	108
Sider (fra-til)	15079-15084
ISSN	0027-8424
Status	Udgivet - 13 sep. 2011

Citationsformater

Quinlan, R. J., Sweeney, M. D., Lo Leggio, L., Otten, H., Poulsen, J-C. N., Johansen, K. S., Krogh, K. B. R. M., Jørgensen, C. I., Tovborg, M., Anthonsen, A., Tryfona, T., Tryfona, T., Walter, C. P., Dupree, P., Xu, F., Davies, G. J., & Walton, P. H. (2011). Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose. Proceedings of the National Academy of Sciences of the United States of America, 108, 15079-15084.

Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose. / Quinlan, R. Jason; Sweeney, Matt D.; Lo Leggio, Leila et al.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 108, 13.09.2011, s. 15079-15084.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Quinlan, RJ, Sweeney, MD, Lo Leggio, L, Otten, H, Poulsen, J-CN, Johansen, KS, Krogh, KBRM, Jørgensen, CI, Tovborg, M, Anthonsen, A, Tryfona, T, Tryfona, T, Walter, CP, Dupree, P, Xu, F, Davies, GJ & Walton, PH 2011, 'Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose', Proceedings of the National Academy of Sciences of the United States of America, bind 108, s. 15079-15084.

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title = "Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose",

abstract = "The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of {"}cellulase-enhancing factors,{"} such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis.",

author = "Quinlan, {R. Jason} and Sweeney, {Matt D.} and {Lo Leggio}, Leila and Harm Otten and Poulsen, {Jens-Christian Navarro} and Johansen, {Katja Salomon} and Krogh, {Kristian B. R. M.} and J{\o}rgensen, {Christian Isak} and Morten Tovborg and Annika Anthonsen and Theodora Tryfona and Theodora Tryfona and Walter, {Clive P.} and Paul Dupree and Feng Xu and Davies, {Gideon J.} and Walton, {Paul H.}",

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T1 - Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose

AU - Quinlan, R. Jason

AU - Sweeney, Matt D.

AU - Lo Leggio, Leila

AU - Otten, Harm

AU - Poulsen, Jens-Christian Navarro

AU - Johansen, Katja Salomon

AU - Krogh, Kristian B. R. M.

AU - Jørgensen, Christian Isak

AU - Tovborg, Morten

AU - Anthonsen, Annika

AU - Tryfona, Theodora

AU - Walter, Clive P.

AU - Dupree, Paul

AU - Xu, Feng

AU - Davies, Gideon J.

AU - Walton, Paul H.

PY - 2011/9/13

Y1 - 2011/9/13

N2 - The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of "cellulase-enhancing factors," such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis.

AB - The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of "cellulase-enhancing factors," such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis.

M3 - Journal article

SN - 0027-8424

VL - 108

SP - 15079

EP - 15084

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

ER -

Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components to cleave cellulose

Abstract

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Citationsformater