Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding

Tandrup, Tobias; Muderspach, Sebastian J.; Banerjee, Sanchari; Santoni, Gianluca; Ipsen, Johan Ø.; Hernández-Rollán, Cristina; Nørholm, Morten H. H.; Johansen, Katja S.; Meilleur, Flora; Leggio, Leila Lo

doi:10.1107/s2052252522007175

Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding

Journal Article · Wed Aug 17 00:00:00 EDT 2022 · IUCrJ

DOI:https://doi.org/10.1107/s2052252522007175· OSTI ID:2471399

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University of Copenhagen (Denmark)
European Synchrotron Radiation Facility (ESRF), Grenoble (France)
University of Copenhagen, Frederiksberg (Denmark)
Technical University of Denmark, Lyngby (Denmark)
North Carolina State University, Raleigh, NC (United States); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first step in the LPMO reaction is the reduction of the active-site metal ion from Cu²⁺ to Cu⁺. Here we have used a systematic diffraction data collection method to monitor structural changes in two AA9 LPMOs, one from Lentinus similis (LsAA9_A) and one from Thermoascus aurantiacus (TaAA9_A), as the active-site Cu is photoreduced in the X-ray beam. For LsAA9_A, the protein produced in two different recombinant systems was crystallized to probe the effect of post-translational modifications and different crystallization conditions on the active site and metal photoreduction. We can recommend that crystallographic studies of AA9 LPMOs wishing to address the Cu²⁺ form use a total X-ray dose below 3 × 10⁴ Gy, while the Cu⁺ form can be attained using 1 × 10⁶ Gy. In all cases, we observe the transition from a hexacoordinated Cu site with two solvent-facing ligands to a T-shaped geometry with no exogenous ligands, and a clear increase of the θ₂ parameter and a decrease of the θ₃ parameter by averages of 9.2° and 8.4°, respectively, but also a slight increase in θ_T. Thus, the θ₂ and θ₃ parameters are helpful diagnostics for the oxidation state of the metal in a His-brace protein. On binding of cello-oligosaccharides to LsAA9_A, regardless of the production source, the θ_T parameter increases, making the Cu site less planar, while the active-site Tyr—Cu distance decreases reproducibly for the Cu²⁺ form. Thus, the θ_T increase found on copper reduction may bring LsAA9_A closer to an oligosaccharide-bound state and contribute to the observed higher affinity of reduced LsAA9_A for cellulosic substrates.

View Accepted Manuscript (DOE)

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: BioStruct-X; Danish Council for Independent Research; Danish Ministry of Higher Education and Science; Formas; Novo Nordisk Foundation HOPE project; Seventh Framework Programme; Swedish Governmental Agency for Innovation Systems; Swedish Research council; USDOE

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 2471399

Journal Information:: IUCrJ, Journal Name: IUCrJ Journal Issue: 5 Vol. 9; ISSN 2052-2525

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

References (93)

Quantum Refinement Does Not Support Dinuclear Copper Sites in Crystal Structures of Particulate Methane Monooxygenase Cao, Lili; Caldararu, Octav; Rosenzweig, Amy C. Angewandte Chemie International Edition, Vol. 57, Issue 1 https://doi.org/10.1002/anie.201708977	journal	December 2017
Detection and Characterization of a Novel Copper‐Dependent Intermediate in a Lytic Polysaccharide Monooxygenase Singh, Raushan K.; Blossom, Benedikt M.; Russo, David A. Chemistry – A European Journal, Vol. 26, Issue 2 https://doi.org/10.1002/chem.201903562	journal	November 2019
Targeting the reactive intermediate in polysaccharide monooxygenases Hedegård, Erik D.; Ryde, Ulf JBIC Journal of Biological Inorganic Chemistry, Vol. 22, Issue 7 https://doi.org/10.1007/s00775-017-1480-1	journal	July 2017
Monitoring and validating active site redox states in protein crystals Antonyuk, Svetlana V.; Hough, Michael A. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1814, Issue 6 https://doi.org/10.1016/j.bbapap.2010.12.017	journal	June 2011
Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH Frandsen, Kristian E. H.; Poulsen, Jens-Christian N.; Tandrup, Tobias Carbohydrate Research, Vol. 448 https://doi.org/10.1016/j.carres.2017.03.010	journal	August 2017
Copper active site in polysaccharide monooxygenases Vu, Van V.; Ngo, Son Tung Coordination Chemistry Reviews, Vol. 368 https://doi.org/10.1016/j.ccr.2018.04.005	journal	August 2018
Estimating the accuracy of calculated electron paramagnetic resonance hyperfine couplings for a lytic polysaccharide monooxygenase Theibich, Yusuf A.; Sauer, Stephan P. A.; Leggio, Leila Lo Computational and Structural Biotechnology Journal, Vol. 19 https://doi.org/10.1016/j.csbj.2020.12.014	journal	January 2021
Copper: An essential metal in biology Festa, Richard A.; Thiele, Dennis J. Current Biology, Vol. 21, Issue 21 https://doi.org/10.1016/j.cub.2011.09.040	journal	November 2011
The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family Udagedara, Saumya R.; Wijekoon, Chathuri J. K.; Xiao, Zhiguang Journal of Inorganic Biochemistry, Vol. 195 https://doi.org/10.1016/j.jinorgbio.2019.03.007	journal	June 2019
Advances in kinetic protein crystallography Bourgeois, Dominique; Royant, Antoine Current Opinion in Structural Biology, Vol. 15, Issue 5 https://doi.org/10.1016/j.sbi.2005.08.002	journal	October 2005
Recent insights into copper-containing lytic polysaccharide mono-oxygenases Hemsworth, Glyn R.; Davies, Gideon J.; Walton, Paul H. Current Opinion in Structural Biology, Vol. 23, Issue 5, p. 660-668 https://doi.org/10.1016/j.sbi.2013.05.006	journal	October 2013
Metalloprotein Crystallography: More than a Structure Bowman, Sarah E. J.; Bridwell-Rabb, Jennifer; Drennan, Catherine L. Accounts of Chemical Research, Vol. 49, Issue 4 https://doi.org/10.1021/acs.accounts.5b00538	journal	March 2016
Oligosaccharide Binding and Thermostability of Two Related AA9 Lytic Polysaccharide Monooxygenases Tandrup, Tobias; Tryfona, Theodora; Frandsen, Kristian Erik Høpfner Biochemistry, Vol. 59, Issue 36 https://doi.org/10.1021/acs.biochem.0c00312	journal	August 2020
A Random-Sequential Kinetic Mechanism for Polysaccharide Monooxygenases Hangasky, John A.; Marletta, Michael A. Biochemistry, Vol. 57, Issue 22 https://doi.org/10.1021/acs.biochem.8b00129	journal	April 2018
Targeting Metalloenzymes for Therapeutic Intervention Chen, Allie Y.; Adamek, Rebecca N.; Dick, Benjamin L. Chemical Reviews, Vol. 119, Issue 2 https://doi.org/10.1021/acs.chemrev.8b00201	journal	September 2018
Catalytic Mechanism of Fungal Lytic Polysaccharide Monooxygenases Investigated by First-Principles Calculations Bertini, Luca; Breglia, Raffaella; Lambrughi, Matteo Inorganic Chemistry, Vol. 57, Issue 1 https://doi.org/10.1021/acs.inorgchem.7b02005	journal	December 2017
Activation of O ₂ and H ₂ O ₂ by Lytic Polysaccharide Monooxygenases Wang, Binju; Wang, Zhanfeng; Davies, Gideon J. ACS Catalysis, Vol. 10, Issue 21 https://doi.org/10.1021/acscatal.0c02914	journal	October 2020
Scission of Glucosidic Bonds by a Lentinus similis Lytic Polysaccharide Monooxygenases Is Strictly Dependent on H₂O₂ while the Oxidation of Saccharide Products Depends on O₂ Brander, Søren; Tokin, Radina; Ipsen, Johan Ø. ACS Catalysis, Vol. 11, Issue 22 https://doi.org/10.1021/acscatal.1c04248	journal	October 2021
LyGo: A Platform for Rapid Screening of Lytic Polysaccharide Monooxygenase Production Hernández-Rollán, Cristina; Falkenberg, Kristoffer B.; Rennig, Maja ACS Synthetic Biology, Vol. 10, Issue 4 https://doi.org/10.1021/acssynbio.1c00034	journal	April 2021
Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61 Structure and Function of a Large, Enigmatic Family Harris, Paul; Welner, Ditte; McFarland, K. Biochemistry, Vol. 49, Issue 15, p. 3305-3316 https://doi.org/10.1021/bi100009p	journal	April 2010
Copper Active Sites in Biology Solomon, Edward I.; Heppner, David E.; Johnston, Esther M. Chemical Reviews, Vol. 114, Issue 7 https://doi.org/10.1021/cr400327t	journal	January 2014
Formation of a Copper(II)–Tyrosyl Complex at the Active Site of Lytic Polysaccharide Monooxygenases Following Oxidation by H₂O₂ Paradisi, Alessandro; Johnston, Esther M.; Tovborg, Morten Journal of the American Chemical Society, Vol. 141, Issue 46 https://doi.org/10.1021/jacs.9b09833	journal	November 2019
Metalloproteins and metal sensing Waldron, Kevin J.; Rutherford, Julian C.; Ford, Dianne Nature, Vol. 460, Issue 7257 https://doi.org/10.1038/nature08300	journal	August 2009
The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases Frandsen, Kristian E. H.; Simmons, Thomas J.; Dupree, Paul Nature Chemical Biology, Vol. 12, Issue 4 https://doi.org/10.1038/nchembio.2029	journal	February 2016
Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2 Bissaro, Bastien; Røhr, Åsmund K.; Müller, Gerdt Nature Chemical Biology, Vol. 13, Issue 10 https://doi.org/10.1038/nchembio.2470	journal	August 2017
Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase Lo Leggio, Leila; Simmons, Thomas J.; Poulsen, Jens-Christian N. Nature Communications, Vol. 6, Issue 1 https://doi.org/10.1038/ncomms6961	journal	January 2015
Characterizing metal-binding sites in proteins with X-ray crystallography Handing, Katarzyna B.; Niedzialkowska, Ewa; Shabalin, Ivan G. Nature Protocols, Vol. 13, Issue 5 https://doi.org/10.1038/nprot.2018.018	journal	April 2018
Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates Simmons, T. J.; Frandsen, K. E. H.; Ciano, L. Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/s41467-017-01247-3	journal	October 2017
A lytic polysaccharide monooxygenase-like protein functions in fungal copper import and meningitis Garcia-Santamarina, Sarela; Probst, Corinna; Festa, Richard A. Nature Chemical Biology, Vol. 16, Issue 3 https://doi.org/10.1038/s41589-019-0437-9	journal	January 2020
A fungal family of lytic polysaccharide monooxygenase-like copper proteins Labourel, Aurore; Frandsen, Kristian E. H.; Zhang, Feng Nature Chemical Biology, Vol. 16, Issue 3 https://doi.org/10.1038/s41589-019-0438-8	journal	January 2020
Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace Brander, Søren; Horvath, Istvan; Ipsen, Johan Ø. Scientific Reports, Vol. 10, Issue 1 https://doi.org/10.1038/s41598-020-73266-y	journal	October 2020
Conformations, structural transitions and visible near-infrared absorption spectra of four-, five- and six-coordinated Cu( ii ) aqua complexes de Almeida, Katia Júlia; Murugan, N. Arul; Rinkevicius, Zilvinas Phys. Chem. Chem. Phys., Vol. 11, Issue 3 https://doi.org/10.1039/B806423G	journal	January 2009
Molecular mechanism of lytic polysaccharide monooxygenases Hedegård, Erik Donovan; Ryde, Ulf Chemical Science, Vol. 9, Issue 15 https://doi.org/10.1039/C8SC00426A	journal	January 2018
The role of the active site tyrosine in the mechanism of lytic polysaccharide monooxygenase McEvoy, Aina; Creutzberg, Joel; Singh, Raushan K. Chemical Science, Vol. 12, Issue 1 https://doi.org/10.1039/D0SC05262K	journal	January 2021
Discovery and industrial applications of lytic polysaccharide mono-oxygenases Johansen, Katja S. Biochemical Society Transactions, Vol. 44, Issue 1 https://doi.org/10.1042/BST20150204	journal	February 2016
Recent insights into lytic polysaccharide monooxygenases (LPMOs) Tandrup, Tobias; Frandsen, Kristian E. H.; Johansen, Katja S. Biochemical Society Transactions, Vol. 46, Issue 6 https://doi.org/10.1042/BST20170549	journal	October 2018
Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications Ipsen, Johan Ø.; Hallas-Møller, Magnus; Brander, Søren Biochemical Society Transactions, Vol. 49, Issue 1 https://doi.org/10.1042/BST20201031	journal	January 2021
X-ray damage to the Mn4Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography Yano, J.; Kern, J.; Irrgang, K. -D. Proceedings of the National Academy of Sciences, Vol. 102, Issue 34 https://doi.org/10.1073/pnas.0505207102	journal	August 2005
Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components Quinlan, R. J.; Sweeney, M. D.; Lo Leggio, L. Proceedings of the National Academy of Sciences, Vol. 108, Issue 37, p. 15079-15084 https://doi.org/10.1073/pnas.1105776108	journal	August 2011
Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallography Schotte, F.; Cho, H. S.; Kaila, V. R. I. Proceedings of the National Academy of Sciences, Vol. 109, Issue 47 https://doi.org/10.1073/pnas.1210938109	journal	November 2012
Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism Kim, S.; Stahlberg, J.; Sandgren, M. Proceedings of the National Academy of Sciences, Vol. 111, Issue 1 https://doi.org/10.1073/pnas.1316609111	journal	December 2013
Spectroscopic and computational insight into the activation of O2 by the mononuclear Cu center in polysaccharide monooxygenases Kjaergaard, C. H.; Qayyum, M. F.; Wong, S. D. Proceedings of the National Academy of Sciences, Vol. 111, Issue 24 https://doi.org/10.1073/pnas.1408115111	journal	June 2014
Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase Courtade, Gaston; Wimmer, Reinhard; Røhr, Åsmund K. Proceedings of the National Academy of Sciences, Vol. 113, Issue 21 https://doi.org/10.1073/pnas.1602566113	journal	May 2016
Reactivity of O 2 versus H 2 O 2 with polysaccharide monooxygenases Hangasky, John A.; Iavarone, Anthony T.; Marletta, Michael A. Proceedings of the National Academy of Sciences, Vol. 115, Issue 19 https://doi.org/10.1073/pnas.1801153115	journal	April 2018
Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures de la Mora, Eugenio; Coquelle, Nicolas; Bury, Charles S. Proceedings of the National Academy of Sciences, Vol. 117, Issue 8 https://doi.org/10.1073/pnas.1821522117	journal	February 2020
Molecular mechanism of the chitinolytic peroxygenase reaction Bissaro, Bastien; Streit, Bennett; Isaksen, Ingvild Proceedings of the National Academy of Sciences, Vol. 117, Issue 3 https://doi.org/10.1073/pnas.1904889117	journal	January 2020
Mechanistic basis of substrate–O₂coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study Courtade, Gaston; Ciano, Luisa; Paradisi, Alessandro Proceedings of the National Academy of Sciences, Vol. 117, Issue 32 https://doi.org/10.1073/pnas.2004277117	journal	July 2020
Structural and Electronic Snapshots during the Transition from a Cu(II) to Cu(I) Metal Center of a Lytic Polysaccharide Monooxygenase by X-ray Photoreduction Gudmundsson, Mikael; Kim, Seonah; Wu, Miao Journal of Biological Chemistry, Vol. 289, Issue 27, p. 18782-18792 https://doi.org/10.1074/jbc.M114.563494	journal	May 2014
Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability Kracher, Daniel; Andlar, Martina; Furtmüller, Paul G. Journal of Biological Chemistry, Vol. 293, Issue 5 https://doi.org/10.1074/jbc.RA117.000109	journal	December 2017
Kinetic protein crystallography: a tool to watch proteins in action Bourgeois, D.; Weik, M. Crystallography Reviews, Vol. 15, Issue 2 https://doi.org/10.1080/08893110802604868	journal	April 2009
Synchrotron X-radiation protein crystallography: instrumentation, methods and applications Helliwell, J. R. Reports on Progress in Physics, Vol. 47, Issue 11 https://doi.org/10.1088/0034-4885/47/11/001	journal	November 1984
Biopython: freely available Python tools for computational molecular biology and bioinformatics Cock, P. J. A.; Antao, T.; Chang, J. T. Bioinformatics, Vol. 25, Issue 11 https://doi.org/10.1093/bioinformatics/btp163	journal	March 2009
The carbohydrate-active enzymes database (CAZy) in 2013 Lombard, Vincent; Golaconda Ramulu, Hemalatha; Drula, Elodie Nucleic Acids Research, Vol. 42, Issue D1 https://doi.org/10.1093/nar/gkt1178	journal	November 2013
RADDOSE-3D : time- and space-resolved modelling of dose in macromolecular crystallography Zeldin, Oliver B.; Gerstel, Markus; Garman, Elspeth F. Journal of Applied Crystallography, Vol. 46, Issue 4 https://doi.org/10.1107/S0021889813011461	journal	June 2013
MOLREP an Automated Program for Molecular Replacement Vagin, A.; Teplyakov, A. Journal of Applied Crystallography, Vol. 30, Issue 6, p. 1022-1025 https://doi.org/10.1107/S0021889897006766	journal	December 1997
Coot model-building tools for molecular graphics Emsley, Paul; Cowtan, Kevin Acta Crystallographica Section D Biological Crystallography, Vol. 60, Issue 12, p. 2126-2132 https://doi.org/10.1107/S0907444904019158	journal	November 2004
Scaling and assessment of data quality Evans, Philip Acta Crystallographica Section D Biological Crystallography, Vol. 62, Issue 1, p. 72-82 https://doi.org/10.1107/S0907444905036693	journal	December 2005
Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation Corbett, Mary C.; Latimer, Matthew J.; Poulos, Thomas L. Acta Crystallographica Section D Biological Crystallography, Vol. 63, Issue 9 https://doi.org/10.1107/S0907444907035160	journal	August 2007
XDS Kabsch, Wolfgang Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2 https://doi.org/10.1107/S0907444909047337	journal	January 2010
Overview of the CCP 4 suite and current developments Winn, Martyn D.; Ballard, Charles C.; Cowtan, Kevin D. Acta Crystallographica Section D Biological Crystallography, Vol. 67, Issue 4 https://doi.org/10.1107/S0907444910045749	journal	March 2011
How good are my data and what is the resolution? Evans, Philip R.; Murshudov, Garib N. Acta Crystallographica Section D Biological Crystallography, Vol. 69, Issue 7 https://doi.org/10.1107/S0907444913000061	journal	June 2013
Refinement of Macromolecular Structures by the Maximum-Likelihood Method Murshudov, G. N.; Vagin, A. A.; Dodson, E. J. Acta Crystallographica Section D Biological Crystallography, Vol. 53, Issue 3 https://doi.org/10.1107/S0907444996012255	journal	May 1997
SFCHECK : a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Vaguine, Alexei A.; Richelle, Jean; Wodak, S. J. Acta Crystallographica Section D Biological Crystallography, Vol. 55, Issue 1 https://doi.org/10.1107/S0907444998006684	journal	January 1999
ID29: a high-intensity highly automated ESRF beamline for macromolecular crystallography experiments exploiting anomalous scattering de Sanctis, Daniele; Beteva, Antonia; Caserotto, Hugo Journal of Synchrotron Radiation, Vol. 19, Issue 3 https://doi.org/10.1107/S0909049512009715	journal	March 2012
Towards accurate structural characterization of metal centres in protein crystals: the structures of Ni and Cu T ₆ bovine insulin derivatives Frankaer, Christian Grundahl; Mossin, Susanne; Ståhl, Kenny Acta Crystallographica Section D Biological Crystallography, Vol. 70, Issue 1 https://doi.org/10.1107/S1399004713029040	journal	December 2013
MeshAndCollect : an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines Zander, Ulrich; Bourenkov, Gleb; Popov, Alexander N. Acta Crystallographica Section D Biological Crystallography, Vol. 71, Issue 11 https://doi.org/10.1107/S1399004715017927	journal	October 2015
Online_DPI : a web server to calculate the diffraction precision index for a protein structure Kumar, K. S. Dinesh; Gurusaran, M.; Satheesh, S. N. Journal of Applied Crystallography, Vol. 48, Issue 3 https://doi.org/10.1107/S1600576715006287	journal	April 2015
Hierarchical clustering for multiple-crystal macromolecular crystallography experiments: the ccCluster program Santoni, Gianluca; Zander, Ulrich; Mueller-Dieckmann, Christoph Journal of Applied Crystallography, Vol. 50, Issue 6 https://doi.org/10.1107/S1600576717015229	journal	November 2017
BioMAX – the first macromolecular crystallography beamline at MAX IV Laboratory Ursby, Thomas; Åhnberg, Karl; Appio, Roberto Journal of Synchrotron Radiation, Vol. 27, Issue 5 https://doi.org/10.1107/S1600577520008723	journal	August 2020
Lytic polysaccharide monooxygenases: a crystallographer's view on a new class of biomass-degrading enzymes Frandsen, Kristian E. H.; Lo Leggio, Leila IUCrJ, Vol. 3, Issue 6 https://doi.org/10.1107/S2052252516014147	journal	October 2016
Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins Ebrahim, Ali; Moreno-Chicano, Tadeo; Appleby, Martin V. IUCrJ, Vol. 6, Issue 4 https://doi.org/10.1107/S2052252519003956	journal	May 2019
Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography Schröder, Gabriela C.; Meilleur, Flora Acta Crystallographica Section D Structural Biology, Vol. 77, Issue 10 https://doi.org/10.1107/S2059798321009025	journal	September 2021
Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison Mehrabi, P.; Bücker, R.; Bourenkov, G. Science Advances, Vol. 7, Issue 12 https://doi.org/10.1126/sciadv.abf1380	journal	March 2021
An Oxidative Enzyme Boosting the Enzymatic Conversion of Recalcitrant Polysaccharides Vaaje-Kolstad, Gustav; Westereng, Bjørge; Horn, Svein J. Science, Vol. 330, Issue 6001, p. 219-222 https://doi.org/10.1126/science.1192231	journal	October 2010
Extracellular electron transfer systems fuel cellulose oxidative degradation Kracher, D.; Scheiblbrandner, S.; Felice, A. K. G. Science, Vol. 352, Issue 6289 https://doi.org/10.1126/science.aaf3165	journal	April 2016
Secreted pectin monooxygenases drive plant infection by pathogenic oomycetes Sabbadin, Federico; Urresti, Saioa; Henrissat, Bernard Science, Vol. 373, Issue 6556 https://doi.org/10.1126/science.abj1342	journal	August 2021
The Pyrroloquinoline-Quinone-Dependent Pyranose Dehydrogenase from Coprinopsis cinerea Drives Lytic Polysaccharide Monooxygenase Action Várnai, Anikó; Umezawa, Kiwamu; Yoshida, Makoto Applied and Environmental Microbiology, Vol. 84, Issue 11 https://doi.org/10.1128/AEM.00156-18	journal	June 2018
Status of the crystallography beamlines at PETRA III Burkhardt, Anja; Pakendorf, Tim; Reime, Bernd The European Physical Journal Plus, Vol. 131, Issue 3 https://doi.org/10.1140/epjp/i2016-16056-0	journal	March 2016
Cellulose Degradation by Polysaccharide Monooxygenases Beeson, William T.; Vu, Van V.; Span, Elise A. Annual Review of Biochemistry, Vol. 84, Issue 1 https://doi.org/10.1146/annurev-biochem-060614-034439	journal	June 2015
Harnessing the potential of LPMO-containing cellulase cocktails poses new demands on processing conditions Müller, Gerdt; Várnai, Anikó; Johansen, Katja Salomon Biotechnology for Biofuels, Vol. 8, Issue 1 https://doi.org/10.1186/s13068-015-0376-y	journal	November 2015
Boosting LPMO-driven lignocellulose degradation by polyphenol oxidase-activated lignin building blocks Frommhagen, Matthias; Mutte, Sumanth Kumar; Westphal, Adrie H. Biotechnology for Biofuels, Vol. 10, Issue 1 https://doi.org/10.1186/s13068-017-0810-4	journal	May 2017
Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9 Brenelli, Lívia; Squina, Fabio M.; Felby, Claus Biotechnology for Biofuels, Vol. 11, Issue 1 https://doi.org/10.1186/s13068-017-0985-8	journal	January 2018
Redox processes acidify and decarboxylate steam-pretreated lignocellulosic biomass and are modulated by LPMO and catalase Peciulyte, Ausra; Samuelsson, Louise; Olsson, Lisbeth Biotechnology for Biofuels, Vol. 11, Issue 1 https://doi.org/10.1186/s13068-018-1159-z	journal	June 2018
The impact of hydrogen peroxide supply on LPMO activity and overall saccharification efficiency of a commercial cellulase cocktail Müller, Gerdt; Chylenski, Piotr; Bissaro, Bastien Biotechnology for Biofuels, Vol. 11, Issue 1 https://doi.org/10.1186/s13068-018-1199-4	journal	July 2018
On the functional characterization of lytic polysaccharide monooxygenases (LPMOs) Eijsink, Vincent G. H.; Petrovic, Dejan; Forsberg, Zarah Biotechnology for Biofuels, Vol. 12, Issue 1 https://doi.org/10.1186/s13068-019-1392-0	journal	March 2019
The H2O2-dependent activity of a fungal lytic polysaccharide monooxygenase investigated with a turbidimetric assay Filandr, Frantisek; Man, Petr; Halada, Petr Biotechnology for Biofuels, Vol. 13, Issue 1 https://doi.org/10.1186/s13068-020-01673-4	journal	March 2020
A new synergistic relationship between xylan-active LPMO and xylobiohydrolase to tackle recalcitrant xylan Zerva, Anastasia; Pentari, Christina; Grisel, Sacha Biotechnology for Biofuels, Vol. 13, Issue 1 https://doi.org/10.1186/s13068-020-01777-x	journal	August 2020
Colorimetric LPMO assay with direct implication for cellulolytic activity Brander, Søren; Lausten, Stine; Ipsen, Johan Ø. Biotechnology for Biofuels, Vol. 14, Issue 1 https://doi.org/10.1186/s13068-021-01902-4	journal	February 2021
Hydrated metal ions in aqueous solution: How regular are their structures? Persson, Ingmar Pure and Applied Chemistry, Vol. 82, Issue 10 https://doi.org/10.1351/PAC-CON-09-10-22	journal	August 2010
Further structural studies of the lytic polysaccharide monooxygenase AoAA13 belonging to the starch-active AA13 family Muderspach, Sebastian J.; Tandrup, Tobias; Frandsen, Kristian E. H. Amylase, Vol. 3, Issue 1 https://doi.org/10.1515/amylase-2019-0004	journal	January 2019
Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding Tandrup, Tobias; Lo Leggio, Leila University of Copenhagen https://doi.org/10.17894/ucph.354e520a-e193-41a3-ac3f-87259db10fda	dataset	January 2022
Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases Banerjee, Sanchari; Muderspach, Sebastian J.; Tandrup, Tobias Biomolecules, Vol. 12, Issue 2 https://doi.org/10.3390/biom12020194	journal	January 2022
Deciphering Structural Photophysics of Fluorescent Proteins by Kinetic Crystallography Bourgeois, Dominique International Journal of Molecular Sciences, Vol. 18, Issue 6 https://doi.org/10.3390/ijms18061187	journal	June 2017

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Purification and characterization of a native lytic polysaccharide monooxygenase from Thermoascus aurantiacus

Journal Article · Sun Jun 14 20:00:00 EDT 2020 · Biotechnology Letters · OSTI ID:1844511

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
LPMO
Lentinus similis
Thermoascus aurantiacus
X-ray photoreduction
active-site copper
active-site geometry
chemistry
crystallography
lytic polysaccharide monooxygenases
materials science
saccharide binding

Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding

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