Biomimetic and bioinspired approaches for wiring enzymes to electrode interfaces

Saboe, Patrick O.; Conte, Emelia; Farell, Megan; Bazan, Guillermo C.; Kumar, Manish

doi:10.1039/c6ee02801b

Cited by 73 publications

(57 citation statements)

References 297 publications

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“…Many hydrogenases oxidize and produce hydrogen at very high rates (in excess of thousands per second, table 4 in ref [75]), and therefore a catalytic current may be detected even if the amount of enzyme that is attached to the electrode is very low. This explains the diversity of electrode materials that have proven useful in this context, listed in table 1 (see also refs [76][77][78] for reviews). Finely designed architectures for embedding membrane-bound hydrogenases have also been developed [79][80][81].…”

Section: Electrodes For Direct Electron Transfermentioning

confidence: 99%

New perspectives in hydrogenase direct electrochemistry

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et al. 2017

Current Opinion in Electrochemistry

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Section: Electrodes For Direct Electron Transfermentioning

confidence: 99%

New perspectives in hydrogenase direct electrochemistry

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Baffert

et al. 2017

Current Opinion in Electrochemistry

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“…The influence of ionic strength as well as various cationic and anionic species on enzymes has already been proven to modulate enzymatic activity or stability in different ways [ 56 , 57 ]; e.g., CDH has two redox domains connected through a flexible linker [ 58 – 60 ], with an ET mechanism similar to FDH but with only one heme in its cytochrome domain as electron acceptor. Moreover, Sezer et al showed an increase in terms of catalytic current of SOx by increasing the ionic strength of the buffer solution [ 61 ], while Feng et al reported on the influence of the viscosity on the rate of the IET [ 62 ].…”

Section: Introductionmentioning

confidence: 99%

The influence of pH and divalent/monovalent cations on the internal electron transfer (IET), enzymatic activity, and structure of fructose dehydrogenase

et al. 2018

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We report on the influence of pH and monovalent/divalent cations on the catalytic current response, internal electron transfer (IET), and structure of fructose dehydrogenase (FDH) by using amperometry, spectrophotometry, and circular dichroism (CD). Amperometric measurements were performed on graphite electrodes, onto which FDH was adsorbed and the effect on the response current to fructose was investigated when varying the pH and the concentrations of divalent/monovalent cations in the contacting buffer. In the presence of 10 mM CaCl2, a current increase of up to ≈ 240% was observed, probably due to an intra-complexation reaction between Ca2+ and the aspartate/glutamate residues found at the interface between the dehydrogenase domain and the cytochrome domain of FDH. Contrary to CaCl2, addition of MgCl2 did not show any particular influence, whereas addition of monovalent cations (Na+ or K+) led to a slight linear increase in the maximum response current. To complement the amperometric investigations, spectrophotometric assays were carried out under homogeneous conditions in the presence of a 1-electron non-proton-acceptor, cytochrome c, or a 2-electron-proton acceptor, 2,6-dichloroindophenol (DCIP), respectively. In the case of cytochrome c, it was possible to observe a remarkable increase in the absorbance up to 200% when 10 mM CaCl2 was added. However, by further increasing the concentration of CaCl2 up to 50 mM and 100 mM, a decrease in the absorbance with a slight inhibition effect was observed for the highest CaCl2 concentration. Addition of MgCl2 or of the monovalent cations shows, surprisingly, no effect on the electron transfer to the electron acceptor. Contrary to the case of cytochrome c, with DCIP none of the cations tested seem to affect the rate of catalysis. In order to correlate the results obtained by amperometric and spectrophotometric measurements, CD experiments have been performed showing a great structural change of FDH when increasing the concentration CaCl2 up to 50 mM, at which the enzyme molecules start to agglomerate, hindering the substrate access to the active site probably due to a chelation reaction occurring at the enzyme surface with the glutamate/aspartate residues. Graphical AbstractFructose dehydrogenase (FDH) consists of three subunits, but only two are involved in the electron transfer process: (I) 2e−/2H+ fructose oxidation, (II) internal electron transfer (IET), (III) direct electron transfer (DET) through 2 heme c; FDH activity either in solution or when immobilized onto an electrode surface is enhanced about 2.5-fold by adding 10 mM CaCl2 to the buffer solution, whereas MgCl2 had an “inhibition” effect. Moreover, the additions of KCl or NaCl led to a slight current increase Electronic supplementary materialThe online version of this article (10.1007/s00216-018-0991-0) contains supplementary material, which is available to authorized users.

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“…Full EFCs with a maximum power density (P max ) greater than 1 mW cm -2 Glucose Moreover, as a typical enzyme-catalyzed system, EFCs suffer from poor operational stability, resulting in short lifetimes and higher costs. 77,78 Instability arises not just with the enzyme, but also arises from the use of cofactors such as nicotinamide adenine dinucleotide (NAD + ), adenosine triphosphate (ATP), and coenzyme A (CoA), which are necessary for many redox enzymes, and of other components that include mediators. The complexity of biological systems can pose additional detrimental effects on the stability of EFCs, such as biofouling of the electrode in implantable EFCs, or enzyme inhibition by O 2 for H 2 /O 2 EFCs.…”

Section: Identification Of Main Challenges In Efcsmentioning

confidence: 99%

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

et al. 2019

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The ever-increasing demands for clean and sustainable energy sources combined with rapid advances in bio-integrated portable or implantable electronic devices have stimulated intensive research activities in enzymatic (bio)fuel cells (EFCs). The use of renewable biocatalysts, the utilization of abundant green, safe, and high energy density fuels, together with the capability of working at modest and biocompatible conditions, make EFCs promising as next generation alternative power sources. However, the main challenges (low energy density, relatively low power density, poor operational stability and limited voltage output) hinder future applications of EFCs. This review aims at exploring the underlying mechanism of EFCs and providing possible practical strategies, methodologies and insights to tackle of these issues. Firstly, this review summarizes approaches in achieving high energy densities in EFCs, particularly, employing enzyme cascades for the deep/complete oxidation of fuels. Secondly, strategies for increasing power densities in EFCs, including increasing enzyme activities, facilitating electron transfers, employing nanomaterials, and designing more efficient enzyme-electrode interfaces, are described. The potential of EFCs/(super)capacitor combination is discussed. Thirdly, the review evaluates a range of strategies for improving the stability of EFCs, including the use of different enzyme immobilization approaches, tuning enzyme properties, designing protective matrixes, and using microbial surface displaying enzymes. Fourthly, approaches for the improvement of the cell voltage of EFCs are highlighted. Finally, future developments and a prospective on EFCs are envisioned.

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Biomimetic and bioinspired approaches for wiring enzymes to electrode interfaces

Abstract: Our review focuses on biomimetic and bioinspired ideas to improve enzyme-driven bioelectrochemical systems for applications in energy, biomedical and environmental fields.

Cited by 73 publications

References 297 publications

New perspectives in hydrogenase direct electrochemistry

New perspectives in hydrogenase direct electrochemistry

The influence of pH and divalent/monovalent cations on the internal electron transfer (IET), enzymatic activity, and structure of fructose dehydrogenase

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

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