ArticleThe FEBS journal2015
Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations.
Article in The FEBS journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 59 citations in OpenAlex.
- Structural insights into cellobiose dehydrogenases of a non-lignocellulolytic fungus and their transcriptional dynamics across different nutritional modes.Microbiology spectrum · 2026Article
- Construction and Characterization of a Novel Direct Electron Transfer Type Enzymatic Sensor Using Spermidine Dehydrogenase.Biosensors · 2025Article
- 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
- Interface engineering of cellobiose dehydrogenase improves interdomain electron transfer.Protein science : a publication of the Protein Society · 2023Article
- Revisiting the role of electron donors in lytic polysaccharide monooxygenase biochemistry.Essays in biochemistry · 2023Review
- Investigating lytic polysaccharide monooxygenase-assisted wood cell wall degradation with microsensors.Nature communications · 2022Article
- Engineering the Turnover Stability of Cellobiose Dehydrogenase toward Long-Term Bioelectronic Applications.ACS sustainable chemistry & engineering · 2021Article
- Chimeric Cellobiose Dehydrogenases Reveal the Function of Cytochrome Domain Mobility for the Electron Transfer to Lytic Polysaccharide Monooxygenase.ACS catalysis · 2021Article
- Enzyme-Based Biosensors: Tackling Electron Transfer Issues.Sensors (Basel, Switzerland) · 2020Review
- Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase.ACS catalysis · 2020Article
- Polysaccharide oxidation by lytic polysaccharide monooxygenase is enhanced by engineered cellobiose dehydrogenase.The FEBS journal · 2020Article
- Determination of the Distance Between the Cytochrome and Dehydrogenase Domains of Immobilized Cellobiose Dehydrogenase by Using Surface Plasmon Resonance with a Center of Mass Based Model.Analytical chemistry · 2020Article
- Crystal Structure of the Catalytic and CytochromeApplied and environmental microbiology · 2019Article
- Interaction between Cellobiose Dehydrogenase and Lytic Polysaccharide Monooxygenase.Biochemistry · 2019Article
- Direct Electron Transfer of Enzymes Facilitated by Cytochromes.ChemElectroChem · 2019Review
- Studying direct electron transfer by site-directed immobilization of cellobiose dehydrogenase.ChemElectroChem · 2019Article
- The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases.Biotechnology for biofuels · 2019Article
- Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018Review
- The influence of pH and divalent/monovalent cations on the internal electron transfer (IET), enzymatic activity, and structure of fructose dehydrogenase.Analytical and bioanalytical chemistry · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The flavocytochrome cellobiose dehydrogenase (CDH) is secreted by wood-decomposing fungi, and is the only known extracellular enzyme with the characteristics of an electron transfer protein. Its proposed function is reduction of lytic polysaccharide mono-oxygenase for subsequent cellulose depolymerization. Electrons are transferred from FADH2 in the catalytic flavodehydrogenase domain of CDH to haem b in a mobile cytochrome domain, which acts as a mediator and transfers electrons towards the active site of lytic polysaccharide mono-oxygenase to activate oxygen. This vital role of the cytochrome domain is little understood, e.g. why do CDHs exhibit different pH optima and rates for inter-domain electron transfer (IET)? This study uses kinetic techniques and docking to assess the interaction of both domains and the resulting IET with regard to pH and ions. The results show that the reported elimination of IET at neutral or alkaline pH is caused by electrostatic repulsion, which prevents adoption of the closed conformation of CDH. Divalent alkali earth metal cations are shown to exert a bridging effect between the domains at concentrations of > 3 mm, thereby neutralizing electrostatic repulsion and increasing IET rates. The necessary high ion concentration, together with the docking results, show that this effect is not caused by specific cation binding sites, but by various clusters of Asp, Glu, Asn, Gln and the haem b propionate group at the domain interface. The results show that a closed conformation of both CDH domains is necessary for IET, but the closed conformation also increases the FAD reduction rate by an electron pulling effect.
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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.