Interaction between bilirubin oxidase and Au nanoparticles distributed over dimpled titanium foil towards oxygen reduction reaction

Lipińska, Wiktoria; Saska, Vita; Siuzdak, Katarzyna; Karczewski, Jakub; Załęski, Karol; Coy, Emerson; de Poulpiquet, Anne; Mazurenko, Ievgen; Lojou, Elisabeth

doi:10.1016/j.electacta.2023.143535

Cited by 2 publications

(2 citation statements)

References 46 publications

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“…The small values obtained for the orientation dispersion parameter (8.8 for McoA WT and 7.2 for the 2F4 variant) are in line with literature reports highlighting strategies for high and controlled enzyme orientation. 16,30 As a consequence, it can be concluded that a rather narrow orientation dispersion is achieved through the immobilization strategy used, thanks to the Met-rich loop acting as an anchoring point. This was also consistent with the high reproducibility observed between different modified electrodes, which is ascribed to the spontaneously directed immobilization of enzymes during electrode modification.…”

Section: Resultsmentioning

confidence: 99%

“…To reach high electron transfer rates in direct electron transfer (DET), an adequate orientation of the enzyme over the electrode is required, ensuring the indispensable short distance between the redox center of an immobilized enzyme and the electrode . In the case of MCOs, this implies that their T1 Cu site must be in close proximity to the electrode surface. − …”

Section: Introductionmentioning

confidence: 99%

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Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O₂ Reduction

Rizzo,

Brissos,

Villain

et al. 2024

ACS Catal.

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The integration of multicopper oxidases with electrodes enables exploitation of the substantial activity of these biocatalysts for the reduction of molecular oxygen. To date, many different strategies have been explored for the fabrication of bioelectrodes, aiming at a stable and favored orientation of immobilized enzymes for ensuring an adequate biocatalytic performance. In this work, we present electrochemical studies of the hyperthermostable Aquifex aeolicus multicopper oxidase (McoA) spontaneously adsorbed over gold surfaces. An extremely simple enzyme immobilization strategy is used, taking advantage of the protein structure, which integrates a loop rich in methionine residues (Met-loop) close to the active site. As a result, enzyme orientation for efficient direct electron transfer is ensured without requiring any prior electrode modification. Detailed analysis of the electrochemical responses supports a minimal dispersion of the enzyme orientation over the electrode. Moreover, using an enzyme variant obtained by directed evolution that shows a preferential conformation of the Met-loop over the active site in closed states is shown to improve the interaction with the electrode, resulting in enhanced performance. The obtained results highlight avenues for the use of multicopper oxidases under electrochemical communication with electrode surfaces and showcase the possibility of bioelectrochemical performance improvement, not only through stable and oriented enzyme immobilization but also by tuning the protein structure for improved electron transfer.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O₂ Reduction

Rizzo,

Brissos,

Villain

et al. 2024

ACS Catal.

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Electrode Nanopatterning for Bioelectroanalysis and Bioelectrocatalysis

CONTALDO,

POULPIQUET,

MAZURENKO

et al. 2024

Electrochemistry

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During his PhD project he developed an efficient method for overproducing an engineered carbon monoxide dehydrogenase (CODH). In this way, he achieved the stable and favorable orientation of the CODH on non-covalently functionalized carbon nanotubes (CNTs) with the final integration into an efficient gasdiffusion bioelectrode for the CO/CO2 interconversion with catalytic efficiency comparable to inorganic catalysts. Since September 2022, he is working on a subfamily of multi-copper oxidase known as copper efflux oxidases (CueOs). CueOs are involved in copper homeostasis, catalyzing the oxidation of Cu + to

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Interaction between bilirubin oxidase and Au nanoparticles distributed over dimpled titanium foil towards oxygen reduction reaction

Cited by 2 publications

References 46 publications

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O₂ Reduction

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O₂ Reduction

Electrode Nanopatterning for Bioelectroanalysis and Bioelectrocatalysis

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Interaction between bilirubin oxidase and Au nanoparticles distributed over dimpled titanium foil towards oxygen reduction reaction

Cited by 2 publications

References 46 publications

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O2 Reduction

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O2 Reduction

Electrode Nanopatterning for Bioelectroanalysis and Bioelectrocatalysis

Contact Info

Product

Resources

About

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O₂ Reduction

Simple and Directed Immobilization of a Multicopper Oxidase on Flat Bare Gold Electrodes Provides High Catalytic Currents for O₂ Reduction