Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells

Bollella, Paolo; Gorton, Lo; Antiochia, Riccarda

doi:10.3390/s18051319

Cited by 84 publications

(56 citation statements)

References 170 publications

(207 reference statements)

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“…Based on its ability to perform DET, CDH has been studied to develop third generation biosensors and enzymatic biofuel cells ,. CDH from Basidiomycota are commonly used for lactose and cellobiose biosensors due to the high substrate specificity .…”

Section: Direct Electrochemistry Of Flavocytochromesmentioning

confidence: 99%

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Ludwig

2018

ChemElectroChem

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The direct electron transfer (DET) of enzymes has been utilized to develop biosensors and enzymatic biofuel cells on micro‐ and nanostructured electrodes. Whereas some enzymes exhibit direct electron transfer between their active‐site cofactor and an electrode, other oxidoreductases depend on acquired cytochrome domains or cytochrome subunits as built‐in redox mediators. The physiological function of these cytochromes is to transfer electrons between the active‐site cofactor and a redox partner protein. The exchange of the natural electron acceptor/donor by an electrode has been demonstrated for several cytochrome carrying oxidoreductases. These multi‐cofactor enzymes have been applied in third generation biosensors to detect glucose, lactate, and other analytes. This review investigates and classifies oxidoreductases with a cytochrome domain, enzyme complexes with a cytochrome subunit, and covers designed cytochrome fusion enzymes. The structurally and electrochemically best characterized proponents from each enzyme class carrying a cytochrome, that is, flavoenzymes, quinoenzymes, molybdenum‐cofactor enzymes, iron‐sulfur cluster enzymes, and multi‐haem enzymes, are featured, and their biochemical, kinetic, and electrochemical properties are compared. The cytochromes molecular and functional properties as well as their contribution to the interdomain electron transfer (IET, between active‐site and cytochrome) and DET (between cytochrome and electrode) with regard to the achieved current density is discussed. Protein design strategies for cytochrome‐fused enzymes are reviewed and the limiting factors as well as strategies to overcome them are outlined.

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Section: Direct Electrochemistry Of Flavocytochromesmentioning

confidence: 99%

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Ludwig

2018

ChemElectroChem

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“…Bioelectrocatalysis has also found application in fuel cells. Reviews concerning the bioelectrocatalysis of specific classes of proteins have recently appeared, [16,[25][26][27] yet only a few focus on hemeproteins and on the multiple roles that these species can play in chemical and technological fields, from sensors to fuel cell development. [19][20][21][22][23][24] Heme proteins, a large protein family including redox enzymes, ET proteins and O 2 transport and storage species, possess a large functional versatility and can easily be engineered.…”

Section: Introductionmentioning

confidence: 99%

“…For these reasons, they have largely been employed in bio(in)organic interfaces for sensing and catalysis either in their native or mutated form. Reviews concerning the bioelectrocatalysis of specific classes of proteins have recently appeared, [16,[25][26][27] yet only a few focus on hemeproteins and on the multiple roles that these species can play in chemical and technological fields, from sensors to fuel cell development. The goal of this minireview is to provide an overview on the latest achievements in the field of heme protein-based bioelectrocatalysis, to help the reader perceive the opportunities offered by these systems and figure out how to exploit their applicative potential.…”

Section: Introductionmentioning

confidence: 99%

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

et al. 2019

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Heme proteins encompass redox enzymes, electron transferases, and species for dioxygen transport and storage. Upon immobilization on a conductive surface, heme proteins can accomplish bioelectrocatalysis. In this process, they carry out oxidation or reduction of substrates at a solid electrode acting as electron acceptor or donor, respectively, thanks to electron transfer processes occurring at the interphase. The efficiency of bioelectrocatalysis depends on the electrical communication of the protein with the electrode surface, retention of protein structure upon adsorption and accessibility of the substrate to the active site. This Minireview outlines the main factors affecting bioelectrocatalysis by adsorbed heme proteins, highlights open issues, and summarizes recent advances in the field.

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“…In contrast to MET, DET is a more viable and effective approach, as electrons can be directly transported from/to the redox active site of oxidoreductase to/from the electrode, as demonstrated in Figure 1B. Some advantages of the DET approach have been demonstrated: the oxidation/reduction of the substrate typically occurs at a favorable electrochemical potential, close to the potential of the redox active site of the enzyme; leakage of potentially toxic redox mediator is avoided whatsoever; and the design of the biocatalytic system can be simplified [69,70]. However, DET is usually difficult to achieve, as the typical electron transfer distance is 1.5-2.0 nm [71].…”

Section: Principles Of the Det Mechanismmentioning

confidence: 99%

Nanocatalysts Containing Direct Electron Transfer-Capable Oxidoreductases: Recent Advances and Applications

Ratautas

Dagys

2019

Catalysts

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Direct electron transfer (DET)-capable oxidoreductases are enzymes that have the ability to transfer/receive electrons directly to/from solid surfaces or nanomaterials, bypassing the need for an additional electron mediator. More than 100 enzymes are known to be capable of working in DET conditions; however, to this day, DET-capable enzymes have been mainly used in designing biofuel cells and biosensors. The rapid advance in (semi) conductive nanomaterial development provided new possibilities to create enzyme-nanoparticle catalysts utilizing properties of DET-capable enzymes and demonstrating catalytic processes never observed before. Briefly, such nanocatalysts combine several cathodic and anodic catalysis performing oxidoreductases into a single nanoparticle surface. Hereby, to the best of our knowledge, we present the first review concerning such nanocatalytic systems involving DET-capable oxidoreductases. We outlook the contemporary applications of DET-capable enzymes, present a principle of operation of nanocatalysts based on DET-capable oxidoreductases, provide a review of state-of-the-art (nano) catalytic systems that have been demonstrated using DET-capable oxidoreductases, and highlight common strategies and challenges that are usually associated with those type catalytic systems. Finally, we end this paper with the concluding discussion, where we present future perspectives and possible research directions.

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Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells

Cited by 84 publications

References 170 publications

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

Nanocatalysts Containing Direct Electron Transfer-Capable Oxidoreductases: Recent Advances and Applications

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