Cellobiose Dehydrogenase Enzyme Dynamics in Wood-Degrading Fungi
Summary
The extracellular oxidoreductase cellobiose dehydrogenase (CDH) plays a pivotal role in fungal wood degradation by facilitating oxidative cleavage of cellulose and hemicellulose. CDH comprises a flavodehydrogenase domain harbouring a flavin adenine dinucleotide (FAD) cofactor and a haem-containing cytochrome domain connected by a flexible linker. Substrate oxidation at the FAD centre generates electrons that are transferred intramolecularly to the haem centre in a conformationally regulated process known as interdomain electron transfer (IET). The reduced cytochrome then donates electrons to copper-dependent lytic polysaccharide monooxygenases (LPMOs), initiating oxidative depolymerisation of recalcitrant polysaccharides. Dynamic transitions between open and closed CDH conformations govern IET efficiency and LPMO activation, thereby enhancing biomass conversion. Detailed understanding of these enzyme dynamics underpins advances in biorefineries, biofuel production and carbon cycling in forest ecosystems worldwide.
Research from Nature Portfolio
Structural analyses have provided a comprehensive view of CDH conformers and their impact on electron transfer. High-resolution crystal structures revealed closed-state assemblies in which a haem propionate group is tightly enclosed by the flavodehydrogenase domain, enabling rapid IET. Site-directed mutagenesis and rapid kinetics further clarified how flavin-to-haem transfer is orchestrated by specific residues at the domain interface. Molecular docking studies demonstrated that, following flavin reduction, the cytochrome domain effectively reduces LPMOs to trigger copper-mediated oxygen activation and subsequent cellulose depolymerisation. These findings establish the structural basis for the oxidative mechanism of fungal biomass degradation.
Cellobiose Dehydrogenase Enzyme Dynamics in Wood-Degrading Fungi publication trend
The graph below shows the total number of articles in cellobiose dehydrogenase enzyme dynamics in wood-degrading fungi across all publications each year (not limited to Nature Index journals).
Technical terms
Cellobiose dehydrogenase (CDH): A dual-domain flavocytochrome secreted by fungi that oxidises cellobiose and transfers electrons to partner enzymes.
Flavodehydrogenase domain: The FAD-binding module of CDH responsible for substrate oxidation.
Cytochrome domain: The haem-containing module of CDH that accepts electrons from the flavodehydrogenase domain and donates them to external acceptors.
Interdomain electron transfer (IET): The intramolecular transfer of electrons between the flavin and haem redox centres in CDH.
Lytic polysaccharide monooxygenase (LPMO): A copper-dependent enzyme that oxidatively cleaves polysaccharides, requiring electron donors such as CDH for activation.
References
- Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression. Microbial Cell Factories (2024).
- Resolving domain positions of cellobiose dehydrogenase by small angle X‐ray scattering. The FEBS Journal (2023).
- Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis. Chemical Science (2017).
- Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation. Nature Communications (2015).
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