scholarly journals Mechanism of hydrogen peroxide formation by lytic polysaccharide monooxygenase

2019 ◽  
Vol 10 (2) ◽  
pp. 576-586 ◽  
Author(s):  
Octav Caldararu ◽  
Esko Oksanen ◽  
Ulf Ryde ◽  
Erik D. Hedegård
Keyword(s):  
Hydrogen Peroxide ◽  
Peroxide Formation ◽  
Lytic Polysaccharide Monooxygenase ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases ◽  
Hydrogen Peroxide Formation ◽  
Polysaccharide Monooxygenase

A mechanism for the formation of hydrogen peroxide by lytic polysaccharide monooxygenases (LPMOs) in the absence of substrate is proposed.

scholarly journals Correction: Mechanism of hydrogen peroxide formation by lytic polysaccharide monooxygenase

2019 ◽  
Vol 10 (35) ◽  
pp. 8262-8263 ◽  
Author(s):  
Octav Caldararu ◽  
Esko Oksanen ◽  
Ulf Ryde ◽  
Erik D. Hedegård
Keyword(s):  
Hydrogen Peroxide ◽  
Peroxide Formation ◽  
Lytic Polysaccharide Monooxygenase ◽  
Hydrogen Peroxide Formation ◽  
Polysaccharide Monooxygenase

Correction for ‘Mechanism of hydrogen peroxide formation by lytic polysaccharide monooxygenase’ by Octav Caldararu et al., Chem. Sci., 2019, 10, 576–586.

scholarly journals Recent Advances in Screening Methods for the Functional Investigation of Lytic Polysaccharide Monooxygenases

2021 ◽  
Vol 9 ◽  
Author(s):  
Damao Wang ◽  
Yanping Li ◽  
Yuting Zheng ◽  
Yves S. Y. Hsieh
Keyword(s):  
Copper Ions ◽  
Biomass Conversion ◽  
Screening Methods ◽  
Lytic Polysaccharide Monooxygenase ◽  
Indirect Measurements ◽  
Glycosidic Bonds ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases ◽  
Functional Investigation ◽  
Polysaccharide Monooxygenase

Lytic polysaccharide monooxygenase (LPMO) is a newly discovered and widely studied enzyme in recent years. These enzymes play a key role in the depolymerization of sugar-based biopolymers (including cellulose, hemicellulose, chitin and starch), and have a positive significance for biomass conversion. LPMO is a copper-dependent enzyme that can oxidize and cleave glycosidic bonds in cellulose and other polysaccharides. Their mechanism of action depends on the correct coordination of copper ions in the active site. There are still difficulties in the analysis of LPMO activity, which often requires multiple methods to be used in concert. In this review, we discussed various LPMO activity analysis methods reported so far, including mature mass spectrometry, chromatography, labeling, and indirect measurements, and summarized the advantages, disadvantages and applicability of different methods.

scholarly journals Lytic polysaccharide monooxygenase (LPMO) mediated production of ultra-fine cellulose nanofibres from delignified softwood fibres

2019 ◽  
Vol 21 (21) ◽  
pp. 5924-5933 ◽  
Author(s):  
Salla Koskela ◽  
Shennan Wang ◽  
Dingfeng Xu ◽  
Xuan Yang ◽  
Kai Li ◽  
...  
Keyword(s):  
Efficient Method ◽  
Energy Efficient ◽  
Environmentally Friendly ◽  
Oxidative Enzymes ◽  
Lytic Polysaccharide Monooxygenase ◽  
Lytic Polysaccharide Monooxygenases ◽  
Cellulose Nanofibres ◽  
Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenase

An environmentally friendly, energy-efficient method for cellulose nanofibre (CNF) production from softwood holocellulose utilising oxidative enzymes, lytic polysaccharide monooxygenases (LPMOs).

scholarly journals The role of the active site tyrosine in the mechanism of lytic polysaccharide monooxygenase

2021 ◽  
Vol 12 (1) ◽  
pp. 352-362
Author(s):  
Aina McEvoy ◽  
Joel Creutzberg ◽  
Raushan K. Singh ◽  
Morten J. Bjerrum ◽  
Erik D. Hedegård
Keyword(s):  
Active Site ◽  
Lytic Polysaccharide Monooxygenase ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases ◽  
Active Site Tyrosine ◽  
Polysaccharide Monooxygenase

With QM/MM, we investigate the mechanism of tyrosine deprotonation in lytic polysaccharide monooxygenases. Our results support deprotonation and our calculated UV-vis spectra show that two isomers must be formed to match recent experiments.

Combination of MALDI-TOF MS and UHPLC-ESI-MS for the characterization of lytic polysaccharide monooxygenase activity

2020 ◽  
Vol 12 (2) ◽  
pp. 149-161 ◽  
Author(s):  
Caio de Oliveira Gorgulho Silva ◽  
Tallyta Santos Teixeira ◽  
Kelly Barreto Rodrigues ◽  
Amanda Araújo Souza ◽  
Antonielle Vieira Monclaro ◽  
...  
Keyword(s):  
Lytic Polysaccharide Monooxygenase ◽  
Monooxygenase Activity ◽  
Maldi Tof Ms ◽  
Esi Ms ◽  
Maldi Tof ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases ◽  
Tof Ms ◽  
Polysaccharide Monooxygenase

Two new mass spectrometry methods, MALDI-TOF MS and hydrophilic interaction UHPLC-ESI-MS, were developed for the characterization of cellulose-active lytic polysaccharide monooxygenases, expanding the analytical toolbox for the study of these enzymes.

scholarly journals Further structural studies of the lytic polysaccharide monooxygenase AoAA13 belonging to the starch-active AA13 family

Amylase ◽  
2019 ◽  
Vol 3 (1) ◽  
pp. 41-54 ◽  
Author(s):  
Sebastian J. Muderspach ◽  
Tobias Tandrup ◽  
Kristian E. H. Frandsen ◽  
Gianluca Santoni ◽  
Jens-Christian N. Poulsen ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Metal Binding ◽  
Binding Studies ◽  
Orthorhombic Crystal ◽  
Lytic Polysaccharide Monooxygenase ◽  
X Ray ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases ◽  
Triclinic Structure ◽  
Polysaccharide Monooxygenase

Abstract Lytic polysaccharide monooxygenases (LPMOs) are recently discovered copper enzymes that cleave recalcitrant polysaccharides by oxidation. The structure of an Aspergillus oryzae LPMO from the starch degrading family AA13 (AoAA13) has previously been determined from an orthorhombic crystal grown in the presence of copper, which is photoreduced in the structure. Here we describe how crystals reliably grown in presence of Zn can be Cu-loaded post crystallization. A partly photoreduced structure was obtained by severely limiting the X-ray dose, showing that this LPMO is much more prone to photoreduction than others. A serial synchrotron crystallography structure was also obtained, showing that this technique may be promising for further studies, to reduce even further photoreduction. We additionally present a triclinic structure of AoAA13, which has less occluded ligand binding site than the orthorhombic one. The availability of the triclinic crystals prompted new ligand binding studies, which lead us to the conclusion that small starch analogues do not bind to AoAA13 to an appreciable extent. A number of disordered conformations of the metal binding histidine brace have been encountered in this and other studies, and we have previously hypothesized that this disorder may be a consequence of loss of copper. We performed molecular dynamics in the absence of active site metal, and showed that the dynamics in solution differ somewhat from the disorder observed in the crystal, though the extent is equally dramatic.

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