ArticleApplied and environmental microbiology2012
Characterization of the two Neurospora crassa cellobiose dehydrogenases and their connection to oxidative cellulose degradation.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 131 citations in OpenAlex.
- TrLPMO9A drives oxidative cellulose depolymerization in Trichoderma reesei and is enhanced by heterologous cellobiose dehydrogenase expression.Biotechnology for biofuels and bioproducts · 2026Article
- Plant Biomass Depolymerization by Oxidoreductases: Structural Characteristics, Synergy Mechanism, and Evolutionary Adaptation.Journal of agricultural and food chemistry · 2026Review
- G-protein signaling components differentially regulate the activity of multiple cellulase enzyme classes in Neurospora crassa.Biotechnology for biofuels and bioproducts · 2026Article
- Heterotrimeric G-proteins and cAMP regulate gene expression during growth on cellulose inmBio · 2026Article
- Interaction of class III cellobiose dehydrogenase with lytic polysaccharide monooxygenase.FEBS open bio · 2025Article
- The application of bacteria-derived dehydrogenases and oxidases in the synthesis of gold nanoparticles.Applied microbiology and biotechnology · 2024Article
- Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression.Microbial cell factories · 2024Article
- Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae.IUCrJ · 2024Article
- Electrochemical Monitoring of Heterogeneous Peroxygenase Reactions Unravels LPMO Kinetics.ACS catalysis · 2024Article
- Amino Acid Residues Controlling Domain Interaction and Interdomain Electron Transfer in Cellobiose Dehydrogenase.Chembiochem : a European journal of chemical biology · 2023Article
- Resolving domain positions of cellobiose dehydrogenase by small angle X-ray scattering.The FEBS journal · 2023Article
- Revisiting the role of electron donors in lytic polysaccharide monooxygenase biochemistry.Essays in biochemistry · 2023Review
- Characterization of a novel AA3_1 xylooligosaccharide dehydrogenase from Thermothelomyces myriococcoides CBS 398.93.Biotechnology for biofuels and bioproducts · 2022Article
- Investigating lytic polysaccharide monooxygenase-assisted wood cell wall degradation with microsensors.Nature communications · 2022Article
- Application of Causality Modelling for Prediction of Molecular Properties for Textile Dyes Degradation by LPMO.Molecules (Basel, Switzerland) · 2022Article
- Inhibition of the Peroxygenase Lytic Polysaccharide Monooxygenase by Carboxylic Acids and Amino Acids.Antioxidants (Basel, Switzerland) · 2022Article
- C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases.The Biochemical journal · 2021Article
- Insights into the HThe FEBS journal · 2021Article
- Novel molecular biological tools for the efficient expression of fungal lytic polysaccharide monooxygenases in Pichia pastoris.Biotechnology for biofuels · 2021Article
- Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase.ACS catalysis · 2021Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The genome of Neurospora crassa encodes two different cellobiose dehydrogenases (CDHs) with a sequence identity of only 53%. So far, only CDH IIA, which is induced during growth on cellulose and features a C-terminal carbohydrate binding module (CBM), was detected in the secretome of N. crassa and preliminarily characterized. CDH IIB is not significantly upregulated during growth on cellulosic material and lacks a CBM. Since CDH IIB could not be identified in the secretome, both CDHs were recombinantly produced in Pichia pastoris. With the cytochrome domain-dependent one-electron acceptor cytochrome c, CDH IIA has a narrower and more acidic pH optimum than CDH IIB. Interestingly, the catalytic efficiencies of both CDHs for carbohydrates are rather similar, but CDH IIA exhibits 4- to 5-times-higher apparent catalytic constants (k(cat) and K(m) values) than CDH IIB for most tested carbohydrates. A third major difference is the 65-mV-lower redox potential of the heme b cofactor in the cytochrome domain of CDH IIA than CDH IIB. To study the interaction with a member of the glycoside hydrolase 61 family, the copper-dependent polysaccharide monooxygenase GH61-3 (NCU02916) from N. crassa was expressed in P. pastoris. A pH-dependent electron transfer from both CDHs via their cytochrome domains to GH61-3 was observed. The different properties of CDH IIA and CDH IIB and their effect on interactions with GH61-3 are discussed in regard to the proposed in vivo function of the CDH/GH61 enzyme system in oxidative cellulose hydrolysis.
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