Cellobiose dehydrogenase: Bioelectrochemical insights and applications

Scheiblbrandner, Stefan; Ludwig, Roland

doi:10.1016/j.bioelechem.2019.107345

Cited by 61 publications

(54 citation statements)

References 156 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[7g, 8b,9] However,t he long-range ET from CDH to LPMO is still poorly understood, which partially impedes our understanding toward the O 2 activation mechanism and the nature of the co-substrate in LPMO catalysis.CDH contains two domains, aC -terminal flavin adenine dinucleotide (FAD)-dependent dehydrogenase domain (DH) and the N-terminal heme b binding cytochrome domain (CYT,l eft panel of Figure 1). [11] TheDHdomain is responsible for the oxidation of cellobiose, where two electrons are released to reduce the FADcofactor. Afterwards,the reserved electrons on FADcan be transferred to the heme b cofactor, reducing heme-Fe III to heme-Fe II in the CYT domain.…”

Section: Introductionmentioning

confidence: 99%

How Oxygen Binding Enhances Long‐Range Electron Transfer: Lessons From Reduction of Lytic Polysaccharide Monooxygenases by Cellobiose Dehydrogenase

et al. 2020

View full text Add to dashboard Cite

Long‐range electron transfer (ET) in metalloenzymes is a general and fundamental process governing O2 activation and reduction. Lytic polysaccharide monooxygenases (LPMOs) are key enzymes for the oxidative cleavage of insoluble polysaccharides, but their reduction mechanism by cellobiose dehydrogenase (CDH), one of the most commonly used enzymatic electron donors, via long‐range ET is still an enigma. Using multiscale simulations, we reveal that interprotein ET between CDH and LPMO is mediated by the heme propionates of CDH and solvent waters. We also show that oxygen binding to the copper center of LPMO is coupled with the long‐range interprotein ET. This process, which is spin‐regulated and enhanced by the presence of O2, directly leads to LPMO−CuII−O2−, bypassing the formation of the generally assumed LPMO−CuI species. The uncovered ET mechanism rationalizes experimental observations and might have far‐reaching implications for LPMO catalysis as well as the O2‐ or CO‐binding‐enhanced long‐range ET processes in other metalloenzymes.

show abstract

Section: Introductionmentioning

confidence: 99%

How Oxygen Binding Enhances Long‐Range Electron Transfer: Lessons From Reduction of Lytic Polysaccharide Monooxygenases by Cellobiose Dehydrogenase

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Although degradation of recalcitrant polysaccharides using glycoside hydrolases (GHs) is a slow and complex process, the discovery of LPMOs has improved the efficiency to a great extent by boosting the activity of hydrolases towards recalcitrant cellulose and chitin (Vaaje-Kolstad et al, 2005;Merino and Cherry, 2007). The LPMO enzyme family was first discovered in 1992 (Raguz et al, 1992), but it was not until 2010 that scientist began to uncover their functional identity, which is distinct from the glycoside hydrolase family (Vaaje-Kolstad et al, 2010). The enzyme has been renamed and classified into the Auxiliary Activity family in the Carbohydrate-Active enZymes (CAZy) database (Levasseur et al, 2013;Lombard et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

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

Wang

Zheng

et al. 2021

Front. Chem.

View full text Add to dashboard Cite

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.

show abstract

“…Due to its high safety, good biocompatibility, and the use of renewable biocatalysts and high-density fuels, EBFC is believed to hold the promise as a next generation millior micro-power source for wearable and implantable electronic devices in the future (Barton et al 2004;Davis and Higson 2007;Mano et al 2003). In EBFCs, the key step for electricity generation is the oxidation catalyzed by various oxidases or dehydrogenases at the anode (Kang et al 2019;Kim et al 2013;Liang et al 2012;Scheiblbrandner and Ludwig 2019). Among such enzymes, NAD-dependent dehydrogenases account for a great portion.…”

Section: Introductionmentioning

confidence: 99%

Engineering a diaphorase via directed evolution for enzymatic biofuel cell application

Liu

You

et al. 2020

Bioresour. Bioprocess.

View full text Add to dashboard Cite

Background: Diaphorase (DI) has received wide attention as the key anodic enzyme mediating the electron transfer and electric energy generation in enzymatic biofuel cells (EBFCs). Lowering the anodic pH may be a useful strategy for constructing high-performance in EBFCs. However, most DI suffered from the poor activity at low pHs. Therefore, it is necessary to modify the activity and its acidic tolerance to further improve the performance of the EBFC. Results: This paper attempts to improve the enzyme activity of DI originated from Geobacillus stearothermophilus under acidic conditions through directed evolution. Three rounds of random mutagenesis by error-prone PCR of the GsDI gene followed by high-throughput screening allowed the identification of the mutant 3-8 (H37Q, S73T, F105L, S68T, G61S, D74V) exhibiting a 4-or 7-fold increase in the catalytic activity at pH 5.4 or 4.5 compared to that of the wild type. And the pH stability of mutant 3-8 was significantly better than that of wild type and showed a 1.3 times higher in the stability at pH 5.4. The EBFC anode equipped with 0.5 mg of mutant 3-8 achieved a maximum current of 40 μA at pH 5.4, much higher than that with the same loading of the wild type enzyme. Conclusion: The GsDI has been improved in the specific activity and pH stability by directed evolution which leads to the improvement of the EBFC performance. Also, the enlarged catalytic channel of mutant and decreased B-factor may be beneficial for the activity and stability. These results suggest that this engineered DI will be a useful candidate for the construction of enhanced EBFCs.

show abstract

Cellobiose dehydrogenase: Bioelectrochemical insights and applications

Cited by 61 publications

References 156 publications

How Oxygen Binding Enhances Long‐Range Electron Transfer: Lessons From Reduction of Lytic Polysaccharide Monooxygenases by Cellobiose Dehydrogenase

How Oxygen Binding Enhances Long‐Range Electron Transfer: Lessons From Reduction of Lytic Polysaccharide Monooxygenases by Cellobiose Dehydrogenase

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

Engineering a diaphorase via directed evolution for enzymatic biofuel cell application

Contact Info

Product

Resources

About