A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase

Liu, Yiwei; Harnden, Kevin A.; Van Stappen, Casey; Dikanov, Sergei A.; Lu, Yi

doi:10.1073/pnas.2308286120

Title: A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase

Journal Article · 16 October 2023 · Proceedings of the National Academy of Sciences of the United States of America

DOI: https://doi.org/10.1073/pnas.2308286120 · OSTI ID:2202499

^[1]; Harnden, Kevin A. ^[2];

^[3];

^[4];

^[1]

Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, Department of Chemistry, University of Texas at Austin, Austin, TX 78712
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801
Department of Chemistry, University of Texas at Austin, Austin, TX 78712
Department of Veterinary Clinical Medicine, University of Illinois at Urbana-Champaign, Urbana, IL 61801

The “Histidine-brace” (His-brace) copper-binding site, composed of Cu(His) ₂ with a backbone amine, is found in metalloproteins with diverse functions. A primary example is lytic polysaccharide monooxygenase (LPMO), a class of enzymes that catalyze the oxidative depolymerization of polysaccharides, providing not only an energy source for native microorganisms but also a route to more effective industrial biomass conversion. Despite its importance, how the Cu His-brace site performs this unique and challenging oxidative depolymerization reaction remains to be understood. To answer this question, we have designed a biosynthetic model of LPMO by incorporating the Cu His-brace motif into azurin, an electron transfer protein. Spectroscopic studies, including ultraviolet-visible (UV–Vis) absorption and electron paramagnetic resonance, confirm copper binding at the designed His-brace site. Moreover, the designed protein is catalytically active towards both cellulose and starch, the native substrates of LPMO, generating degraded oligosaccharides with multiturnovers by C1 oxidation. It also performs oxidative cleavage of the model substrate 4-nitrophenyl-D-glucopyranoside, achieving a turnover number ~9% of that of a native LPMO assayed under identical conditions. This work presents a rationally designed artificial metalloenzyme that acts as a structural and functional mimic of LPMO, which provides a promising system for understanding the role of the Cu His-brace site in LPMO activity and potential application in polysaccharide degradation.

View Journal Article

Cite

Export

Save

Sponsoring Organization:: USDOE

Grant/Contract Number:: FG02-08ER15960

OSTI ID:: 2202499

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 43 Vol. 120; ISSN 0027-8424

Publisher:: Proceedings of the National Academy of SciencesCopyright Statement

Country of Publication:: United States

Language:: English

References (99)

Oxygen Binding, Activation, and Reduction to Water by Copper Proteins Solomon, Edward I.; Chen, Peng; Metz, Markus Angewandte Chemie International Edition, Vol. 40, Issue 24 https://doi.org/10.1002/1521-3773(20011217)40:24<4570::AID-ANIE4570>3.0.CO;2-4	journal	December 2001
Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase O'Dell, William B.; Agarwal, Pratul K.; Meilleur, Flora Angewandte Chemie International Edition, Vol. 56, Issue 3 https://doi.org/10.1002/anie.201610502	journal	December 2016
Cellulose Depolymerization with LPMO‐inspired Cu Complexes Castillo, Ivan; Torres‐Flores, Andrea P.; Abad‐Aguilar, Diego F. ChemCatChem, Vol. 13, Issue 22 https://doi.org/10.1002/cctc.202101169	journal	September 2021
CuA centers and their biosynthetic models in azurin Savelieff, Masha G.; Lu, Yi JBIC Journal of Biological Inorganic Chemistry, Vol. 15, Issue 4 https://doi.org/10.1007/s00775-010-0625-2	journal	February 2010
Hyperfine sublevel correlation (hyscore) spectroscopy: a 2D ESR investigation of the squaric acid radical Höfer, P.; Grupp, A.; Nebenführ, H. Chemical Physics Letters, Vol. 132, Issue 3 https://doi.org/10.1016/0009-2614(86)80124-5	journal	December 1986
Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5·5 and pH 9·0 Nar, Herbert; Messerschmidt, Albrecht; Huber, Robert Journal of Molecular Biology, Vol. 221, Issue 3 https://doi.org/10.1016/0022-2836(91)80173-R	journal	October 1991
Tyrosinase: a comprehensive review of its mechanism Sánchez-Ferrer, Álvaro; Neptuno Rodríguez-López, José; García-Cánovas, Francisco Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol. 1247, Issue 1 https://doi.org/10.1016/0167-4838(94)00204-T	journal	February 1995
Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type‐3 dicopper center¹ Eicken, Christoph; Zippel, Frank; Büldt-Karentzopoulos, Klaudia FEBS Letters, Vol. 436, Issue 2 https://doi.org/10.1016/S0014-5793(98)01113-2	journal	October 1998
Review: lignin conversion by manganese peroxidase (MnP) Hofrichter, Martin Enzyme and Microbial Technology, Vol. 30, Issue 4, p. 454-466 https://doi.org/10.1016/S0141-0229(01)00528-2	journal	April 2002
Regioselective oxidative carbon-oxygen bond cleavage catalysed by copper(II) complexes: A relevant model study for lytic polysaccharides monooxygenases activity Muthuramalingam, Sethuraman; Maheshwaran, Duraiyarasu; Velusamy, Marappan Journal of Catalysis, Vol. 372 https://doi.org/10.1016/j.jcat.2019.03.019	journal	April 2019
EasySpin, a comprehensive software package for spectral simulation and analysis in EPR Stoll, Stefan; Schweiger, Arthur Journal of Magnetic Resonance, Vol. 178, Issue 1, p. 42-55 https://doi.org/10.1016/j.jmr.2005.08.013	journal	January 2006
Purification and characterization of tyrosinase from walnut leaves (Juglans regia) Zekiri, Florime; Molitor, Christian; Mauracher, Stephan G. Phytochemistry, Vol. 101 https://doi.org/10.1016/j.phytochem.2014.02.010	journal	May 2014
The framework of polysaccharide monooxygenase structure and chemistry Span, Elise A.; Marletta, Michael A. Current Opinion in Structural Biology, Vol. 35 https://doi.org/10.1016/j.sbi.2015.10.002	journal	December 2015
Structural Basis for Substrate Targeting and Catalysis by Fungal Polysaccharide Monooxygenases Li, Xin; Beeson, William T.; Phillips, Christopher M. Structure, Vol. 20, Issue 6, p. 1051-1061 https://doi.org/10.1016/j.str.2012.04.002	journal	June 2012
How to Build a Metalloenzyme: Lessons from a Protein-Based Model of Acetyl Coenzyme A Synthase Shafaat, Hannah S.; Manesis, Anastasia C.; Yerbulekova, Alina Accounts of Chemical Research, Vol. 56, Issue 9 https://doi.org/10.1021/acs.accounts.2c00824	journal	April 2023
LmrR: A Privileged Scaffold for Artificial Metalloenzymes Roelfes, Gerard Accounts of Chemical Research, Vol. 52, Issue 3 https://doi.org/10.1021/acs.accounts.9b00004	journal	February 2019
Understanding and Modulating Metalloenzymes with Unnatural Amino Acids, Non-Native Metal Ions, and Non-Native Metallocofactors Mirts, Evan N.; Bhagi-Damodaran, Ambika; Lu, Yi Accounts of Chemical Research, Vol. 52, Issue 4 https://doi.org/10.1021/acs.accounts.9b00011	journal	March 2019
Progress, Challenges, and Opportunities with Artificial Metalloenzymes in Biosynthesis Bloomer, Brandon J.; Clark, Douglas S.; Hartwig, John F. Biochemistry, Vol. 62, Issue 2 https://doi.org/10.1021/acs.biochem.1c00829	journal	February 2022
Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions Hosseinzadeh, Parisa; Mirts, Evan N.; Pfister, Thomas D. Biochemistry, Vol. 55, Issue 10 https://doi.org/10.1021/acs.biochem.5b01299	journal	March 2016
The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins Lawton, Thomas J.; Kenney, Grace E.; Hurley, Joseph D. Biochemistry, Vol. 55, Issue 15 https://doi.org/10.1021/acs.biochem.6b00175	journal	April 2016
Pulsed Electron Paramagnetic Resonance Insights into the Ligand Environment of Copper in Drosophila Lysyl Oxidase Rao, Guodong; Bansal, Sandhya; Law, Wen Xuan Biochemistry, Vol. 56, Issue 29 https://doi.org/10.1021/acs.biochem.7b00308	journal	July 2017
Catalysis and Electron Transfer in De Novo Designed Metalloproteins Koebke, Karl J.; Pinter, Tyler B. J.; Pitts, Winston C. Chemical Reviews, Vol. 122, Issue 14 https://doi.org/10.1021/acs.chemrev.1c01025	journal	June 2022
Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere Van Stappen, Casey; Deng, Yunling; Liu, Yiwei Chemical Reviews, Vol. 122, Issue 14 https://doi.org/10.1021/acs.chemrev.2c00106	journal	July 2022
Copper–Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity Elwell, Courtney E.; Gagnon, Nicole L.; Neisen, Benjamin D. Chemical Reviews, Vol. 117, Issue 3 https://doi.org/10.1021/acs.chemrev.6b00636	journal	January 2017
Artificial Metalloenzymes: Reaction Scope and Optimization Strategies Schwizer, Fabian; Okamoto, Yasunori; Heinisch, Tillmann Chemical Reviews, Vol. 118, Issue 1 https://doi.org/10.1021/acs.chemrev.7b00014	journal	May 2017
Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars Meier, Katlyn K.; Jones, Stephen M.; Kaper, Thijs Chemical Reviews, Vol. 118, Issue 5 https://doi.org/10.1021/acs.chemrev.7b00421	journal	November 2017
Metalloglycosidase Mimics: Oxidative Cleavage of Saccharides Promoted by Multinuclear Copper Complexes under Physiological Conditions Yu, Zhen; Thompson, Zechariah; Behnke, Shelby L. Inorganic Chemistry, Vol. 59, Issue 16 https://doi.org/10.1021/acs.inorgchem.0c01193	journal	July 2020
Decoding the Ambiguous Electron Paramagnetic Resonance Signals in the Lytic Polysaccharide Monooxygenase from Photorhabdus luminescens Gómez-Piñeiro, Rogelio J.; Drosou, Maria; Bertaina, Sylvain Inorganic Chemistry, Vol. 61, Issue 20 https://doi.org/10.1021/acs.inorgchem.2c00766	journal	May 2022
Nitrite Reductase Activity in Engineered Azurin Variants Berry, Steven M.; Strange, Jacob N.; Bladholm, Erika L. Inorganic Chemistry, Vol. 55, Issue 9 https://doi.org/10.1021/acs.inorgchem.5b03006	journal	April 2016
Copper Complexes as Bioinspired Models for Lytic Polysaccharide Monooxygenases Concia, Alda Lisa; Beccia, Maria Rosa; Orio, Maylis Inorganic Chemistry, Vol. 56, Issue 3 https://doi.org/10.1021/acs.inorgchem.6b02165	journal	January 2017
AutoDock Vina 1.2.0: New Docking Methods, Expanded Force Field, and Python Bindings Eberhardt, Jerome; Santos-Martins, Diogo; Tillack, Andreas F. Journal of Chemical Information and Modeling, Vol. 61, Issue 8 https://doi.org/10.1021/acs.jcim.1c00203	journal	July 2021
Oxidative Cleavage of Glycosidic Bonds by Synthetic Mimics of Lytic Polysaccharide Monooxygenases Chen, Kaiqian; Zangiabadi, Milad; Zhao, Yan Organic Letters, Vol. 24, Issue 18 https://doi.org/10.1021/acs.orglett.2c01312	journal	May 2022
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
Molecular Mechanisms of Oxygen Activation and Hydrogen Peroxide Formation in Lytic Polysaccharide Monooxygenases Wang, Binju; Walton, Paul H.; Rovira, Carme ACS Catalysis, Vol. 9, Issue 6 https://doi.org/10.1021/acscatal.9b00778	journal	April 2019
Mimicking the Cu Active Site of Lytic Polysaccharide Monooxygenase Using Monoanionic Tridentate N-Donor Ligands Bouchey, Caitlin J.; Shopov, Dimitar Y.; Gruen, Aaron D. ACS Omega, Vol. 7, Issue 39 https://doi.org/10.1021/acsomega.2c04432	journal	September 2022
Oxidative Cleavage of Cellobiose by Lytic Polysaccharide Monooxygenase (LPMO)-Inspired Copper Complexes Neira, Andrea. C.; Martínez-Alanis, Paulina R.; Aullón, Gabriel ACS Omega, Vol. 4, Issue 6 https://doi.org/10.1021/acsomega.9b00785	journal	June 2019
Artificial Metalloenzymes as Catalysts for Oxidative Lignin Degradation Doble, Megan V.; Jarvis, Amanda G.; Ward, Andrew C. C. ACS Sustainable Chemistry & Engineering, Vol. 6, Issue 11 https://doi.org/10.1021/acssuschemeng.8b03568	journal	October 2018
Spectroscopy of Binuclear Dioxygen Complexes Solomon, Edward I.; Tuczek, Felix; Root, David E. Chemical Reviews, Vol. 94, Issue 3 https://doi.org/10.1021/cr00027a013	journal	May 1994
Free Radical Catalysis by Galactose Oxidase Whittaker, James W. Chemical Reviews, Vol. 103, Issue 6 https://doi.org/10.1021/cr020425z	journal	June 2003
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
Multicopper Oxidases and Oxygenases Solomon, Edward I.; Sundaram, Uma M.; Machonkin, Timothy E. Chemical Reviews, Vol. 96, Issue 7 https://doi.org/10.1021/cr950046o	journal	January 1996
Dissimilatory Nitrite and Nitric Oxide Reductases Averill, Bruce A. Chemical Reviews, Vol. 96, Issue 7 https://doi.org/10.1021/cr950056p	journal	January 1996
Spectroscopic studies of stellacyanin, plastocyanin, and azurin. Electronic structure of the blue copper sites Solomon, Edward I.; Hare, Jeffrey W.; Dooley, David M. Journal of the American Chemical Society, Vol. 102, Issue 1 https://doi.org/10.1021/ja00521a029	journal	January 1980
Determinants of Regioselective Hydroxylation in the Fungal Polysaccharide Monooxygenases Vu, Van V.; Beeson, William T.; Phillips, Christopher M. Journal of the American Chemical Society, Vol. 136, Issue 2 https://doi.org/10.1021/ja409384b	journal	December 2013
Hydrogen Atom Abstraction from Hydrocarbons by a Copper(III)-Hydroxide Complex Dhar, Debanjan; Tolman, William B. Journal of the American Chemical Society, Vol. 137, Issue 3 https://doi.org/10.1021/ja512014z	journal	January 2015
Copper Centers in the Cryo-EM Structure of Particulate Methane Monooxygenase Reveal the Catalytic Machinery of Methane Oxidation Chang, W. -H.; Lin, H. -H.; Tsai, I-K. Journal of the American Chemical Society, Vol. 143, Issue 26 https://doi.org/10.1021/jacs.1c04082	journal	June 2021
Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins Mann, Samuel I.; Heinisch, Tillmann; Ward, Thomas R. Journal of the American Chemical Society, Vol. 139, Issue 48 https://doi.org/10.1021/jacs.7b10452	journal	November 2017
Shift from Entropic Cu²⁺ Binding to Enthalpic Cu⁺ Binding Determines the Reduction Thermodynamics of Blue Copper Proteins North, Molly L.; Wilcox, Dean E. Journal of the American Chemical Society, Vol. 141, Issue 36 https://doi.org/10.1021/jacs.9b06836	journal	August 2019
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
Rationally tuning the reduction potential of a single cupredoxin beyond the natural range Marshall, Nicholas M.; Garner, Dewain K.; Wilson, Tiffany D. Nature, Vol. 462, Issue 7269 https://doi.org/10.1038/nature08551	journal	November 2009
Reversible S-nitrosylation in an engineered azurin Tian, Shiliang; Liu, Jing; Cowley, Ryan E. Nature Chemistry, Vol. 8, Issue 7 https://doi.org/10.1038/nchem.2489	journal	April 2016
Type-zero copper proteins Lancaster, Kyle M.; George, Serena DeBeer; Yokoyama, Keiko Nature Chemistry, Vol. 1, Issue 9 https://doi.org/10.1038/nchem.412	journal	November 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
Lytic xylan oxidases from wood-decay fungi unlock biomass degradation Couturier, Marie; Ladevèze, Simon; Sulzenbacher, Gerlind Nature Chemical Biology, Vol. 14, Issue 3 https://doi.org/10.1038/nchembio.2558	journal	January 2018
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
An ancient family of lytic polysaccharide monooxygenases with roles in arthropod development and biomass digestion Sabbadin, Federico; Hemsworth, Glyn R.; Ciano, Luisa Nature Communications, Vol. 9, Issue 1 https://doi.org/10.1038/s41467-018-03142-x	journal	February 2018
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection Askarian, Fatemeh; Uchiyama, Satoshi; Masson, Helen Nature Communications, Vol. 12, Issue 1 https://doi.org/10.1038/s41467-021-21473-0	journal	February 2021
De novo metalloprotein design Chalkley, Matthew J.; Mann, Samuel I.; DeGrado, William F. Nature Reviews Chemistry, Vol. 6, Issue 1 https://doi.org/10.1038/s41570-021-00339-5	journal	December 2021
The road to fully programmable protein catalysis Lovelock, Sarah L.; Crawshaw, Rebecca; Basler, Sophie Nature, Vol. 606, Issue 7912 https://doi.org/10.1038/s41586-022-04456-z	journal	June 2022
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
Bracing copper for the catalytic oxidation of C–H bonds Ciano, Luisa; Davies, Gideon J.; Tolman, William B. Nature Catalysis, Vol. 1, Issue 8 https://doi.org/10.1038/s41929-018-0110-9	journal	August 2018
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
Modelling a ‘histidine brace’ motif in mononuclear copper monooxygenases Fukatsu, Arisa; Morimoto, Yuma; Sugimoto, Hideki Chemical Communications, Vol. 56, Issue 38 https://doi.org/10.1039/D0CC01392G	journal	January 2020
Peptide-based chemical models for lytic polysaccharide monooxygenases Hassoon, Azza A.; Szorcsik, Attila; Fülöp, Lívia Dalton Transactions, Vol. 51, Issue 45 https://doi.org/10.1039/D2DT02836K	journal	January 2022
Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase Schröder, Gabriela C.; O'Dell, William B.; Webb, Simon P. Chemical Science, Vol. 13, Issue 45 https://doi.org/10.1039/D2SC05031E	journal	January 2022
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
The nuclear modulation effect in electron spin echoes for complexes of Cu ²⁺ and imidazole with ¹⁴ N and ¹⁵ N Mims, W. B.; Peisach, J. The Journal of Chemical Physics, Vol. 69, Issue 11 https://doi.org/10.1063/1.436479	journal	December 1978
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
Flexibility of the metal-binding region in apo-cupredoxins Zaballa, María-Eugenia; Abriata, Luciano A.; Donaire, Antonio Proceedings of the National Academy of Sciences, Vol. 109, Issue 24 https://doi.org/10.1073/pnas.1119460109	journal	May 2012
NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions Aachmann, F. L.; Sorlie, M.; Skjak-Braek, G. Proceedings of the National Academy of Sciences, Vol. 109, Issue 46 https://doi.org/10.1073/pnas.1208822109	journal	October 2012
Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin Sieracki, N. A.; Tian, S.; Hadt, R. G. Proceedings of the National Academy of Sciences, Vol. 111, Issue 3 https://doi.org/10.1073/pnas.1316483111	journal	January 2014
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
Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation Agger, J. W.; Isaksen, T.; Varnai, A. Proceedings of the National Academy of Sciences, Vol. 111, Issue 17 https://doi.org/10.1073/pnas.1323629111	journal	April 2014
A family of starch-active polysaccharide monooxygenases Vu, V. V.; Beeson, W. T.; Span, E. A. Proceedings of the National Academy of Sciences, Vol. 111, Issue 38 https://doi.org/10.1073/pnas.1408090111	journal	September 2014
Design of a single protein that spans the entire 2-V range of physiological redox potentials Hosseinzadeh, Parisa; Marshall, Nicholas M.; Chacón, Kelly N. Proceedings of the National Academy of Sciences, Vol. 113, Issue 2 https://doi.org/10.1073/pnas.1515897112	journal	December 2015
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
Kinetic analysis of amino acid radicals formed in H ₂ O ₂ -driven Cu ^I LPMO reoxidation implicates dominant homolytic reactivity Jones, Stephen M.; Transue, Wesley J.; Meier, Katlyn K. Proceedings of the National Academy of Sciences, Vol. 117, Issue 22 https://doi.org/10.1073/pnas.1922499117	journal	May 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
Photoinduced hole hopping through tryptophans in proteins Záliš, Stanislav; Heyda, Jan; Šebesta, Filip Proceedings of the National Academy of Sciences, Vol. 118, Issue 11 https://doi.org/10.1073/pnas.2024627118	journal	March 2021
Geometric and electronic structure of oxyhemocyanin: spectral and chemical correlations to met apo, half met, met, and dimer active sites. Eickman, N. C.; Himmelwright, R. S.; Solomon, E. I. Proceedings of the National Academy of Sciences, Vol. 76, Issue 5 https://doi.org/10.1073/pnas.76.5.2094	journal	May 1979
Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase. Hay, M.; Richards, J. H.; Lu, Y. Proceedings of the National Academy of Sciences, Vol. 93, Issue 1 https://doi.org/10.1073/pnas.93.1.461	journal	January 1996
A C4-oxidizing Lytic Polysaccharide Monooxygenase Cleaving Both Cellulose and Cello-oligosaccharides Isaksen, Trine; Westereng, Bjørge; Aachmann, Finn L. Journal of Biological Chemistry, Vol. 289, Issue 5 https://doi.org/10.1074/jbc.M113.530196	journal	December 2013
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
Engineering chitinolytic activity into a cellulose-active lytic polysaccharide monooxygenase provides insights into substrate specificity Jensen, Marianne Slang; Klinkenberg, Geir; Bissaro, Bastien Journal of Biological Chemistry, Vol. 294, Issue 50 https://doi.org/10.1074/jbc.RA119.010056	journal	December 2019
Apo‐azurin folds via an intermediate that resembles the molten‐globule Sandberg, Anders; Leckner, Johan; Karlsson, B. Göran Protein Science, Vol. 13, Issue 10 https://doi.org/10.1110/ps.04848204	journal	October 2004
Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome c551 and nitrite reductase Kamp, Mart; Silvestrini, Maria Chiara; Brunori, Maurizio European Journal of Biochemistry, Vol. 194, Issue 1 https://doi.org/10.1111/j.1432-1033.1990.tb19434.x	journal	November 1990
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
Particulate methane monooxygenase contains only mononuclear copper centers Ross, Matthew O.; MacMillan, Fraser; Wang, Jingzhou Science, Vol. 364, Issue 6440 https://doi.org/10.1126/science.aav2572	journal	May 2019
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
Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer Koo, Christopher W.; Tucci, Frank J.; He, Yuan Science, Vol. 375, Issue 6586 https://doi.org/10.1126/science.abm3282	journal	March 2022
In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper. Ensign, S. A.; Hyman, M. R.; Arp, D. J. Journal of Bacteriology, Vol. 175, Issue 7 https://doi.org/10.1128/jb.175.7.1971-1980.1993	journal	April 1993
Electron Transfer in Proteins Gray, Harry B.; Winkler, Jay R. Annual Review of Biochemistry, Vol. 65, Issue 1 https://doi.org/10.1146/annurev.bi.65.070196.002541	journal	June 1996
The Biochemistry of Methane Oxidation Hakemian, Amanda S.; Rosenzweig, Amy C. Annual Review of Biochemistry, Vol. 76, Issue 1 https://doi.org/10.1146/annurev.biochem.76.061505.175355	journal	June 2007
Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species Li, James; Solhi, Laleh; Goddard-Borger, Ethan D. Biotechnology for Biofuels, Vol. 14, Issue 1 https://doi.org/10.1186/s13068-020-01860-3	journal	January 2021
Lignin Biodegradation with Laccase-Mediator Systems Christopher, Lew Paul; Yao, Bin; Ji, Yun Frontiers in Energy Research, Vol. 2 https://doi.org/10.3389/fenrg.2014.00012	journal	March 2014
Oxidative Power: Tools for Assessing LPMO Activity on Cellulose Calderaro, Federica; Bevers, Loes E.; van den Berg, Marco A. Biomolecules, Vol. 11, Issue 8 https://doi.org/10.3390/biom11081098	journal	July 2021

Similar Records

Insights into an unusual Auxiliary Activity 9 family member lacking the histidine brace motif of lytic polysaccharide monooxygenases

Journal Article · 2019 · Journal of Biological Chemistry · OSTI ID:1619137

Frandsen, Kristian E. H.; Tovborg, Morten; Jørgensen, Christian I.; +15 more

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

Journal Article · 2020 · Biotechnology Letters · OSTI ID:1844511

Fritsche, Susanne; Hopson, Cynthia; Gorman, Jennifer; +2 more

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

Journal Article · 2022 · IUCrJ · OSTI ID:2471399

Tandrup, Tobias; Muderspach, Sebastian J.; Banerjee, Sanchari; +7 more

Title: A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase

Citation Formats

References (99)

Similar Records

Related Subjects