ArticleBiochemistry2019
Interaction between Cellobiose Dehydrogenase and Lytic Polysaccharide Monooxygenase.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 40 citations in OpenAlex.
- Heterologously Expressed Cellobiose Dehydrogenase Acts as Efficient Electron-Donor of Lytic Polysaccharide Monooxygenase for Cellulose Degradation inInternational journal of molecular sciences · 2023Article
- The Role of the Residue at Position 2 in the Catalytic Activity of AA9 Lytic Polysaccharide Monooxygenases.International journal of molecular sciences · 2023Article
- Revisiting the role of electron donors in lytic polysaccharide monooxygenase biochemistry.Essays in biochemistry · 2023Review
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Inhibition of the Peroxygenase Lytic Polysaccharide Monooxygenase by Carboxylic Acids and Amino Acids.Antioxidants (Basel, Switzerland) · 2022Article
- Insights into the HThe FEBS journal · 2021Article
- A multi-omics approach to lignocellulolytic enzyme discovery reveals a new ligninase activity fromProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase.ACS catalysis · 2021Article
- A microalgal-based preparation with synergistic cellulolytic and detoxifying action towards chemical-treated lignocellulose.Plant biotechnology journal · 2021Article
- Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide.Molecular diversity · 2020Article
- Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase.ACS catalysis · 2020Article
- Draft Genome Sequence of Thermophilic Bacillus sp. TYF-LIM-B05 Directly Producing Ethanol from Various Carbon Sources Including Lignocellulose.Current microbiology · 2020Article
- Industrial Use of Cell Wall Degrading Enzymes: The Fine Line Between Production Strategy and Economic Feasibility.Frontiers in bioengineering and biotechnology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are ubiquitous oxidoreductases, facilitating the degradation of polymeric carbohydrates in biomass. Cellobiose dehydrogenase (CDH) is a biologically relevant electron donor in this process, with the electrons resulting from cellobiose oxidation being shuttled from the CDH dehydrogenase domain to its cytochrome domain and then to the LPMO catalytic site. In this work, we investigate the interaction of four Neurospora crassa LPMOs and five CDH cytochrome domains from different species using computational methods. We used HADDOCK to perform protein-protein docking experiments on all 20 combinations and subsequently to select four complexes for extensive molecular dynamics simulations. The potential of mean force is computed for a rotation of the cytochrome domain relative to LPMO. We find that the LPMO loops are largely responsible for the preferred orientations of the cytochrome domains. This leads us to postulate a hybrid version of NcLPMO9F, with exchanged loops and predicted altered cytochrome binding preferences for this variant. Our work provides insight into the possible mechanisms of electron transfer between the two protein systems, in agreement with and complementary to previously published experimental data.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.