Enhanced direct electron transfer-type bioelectrocatalysis of bilirubin oxidase on negatively charged aromatic compound-modified carbon electrode

Xia, Hong-qi; Kitazumi, Yuki; Shirai, Osamu; Kano, Kenji

doi:10.1016/j.jelechem.2015.12.043

Cited by 73 publications

(78 citation statements)

References 44 publications

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“…In the enzyme, the electrode-active redox center locates at d from the electrode. When the orientation of the enzyme is random on the planar electrode, the electrode-active redox center in the enzyme is located at the distance between d min and the farthest approach (d = d max ) with a constant probability [18][19][20]. According to this model, the steady-state DET-type catalytic current by the randomly adsorbed enzyme is expressed by Equation 8:…”

Section: Theoretical Aspects For the Det-type Bioelectrocatalysismentioning

confidence: 99%

Direct Electron Transfer-Type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes

et al. 2020

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Direct electron transfer (DET)-type bioelectrocatalysis, which couples the electrode reactions and catalytic functions of redox enzymes without any redox mediator, is one of the most intriguing subjects that has been studied over the past few decades in the field of bioelectrochemistry. In order to realize the DET-type bioelectrocatalysis and improve the performance, nanostructures of the electrode surface have to be carefully tuned for each enzyme. In addition, enzymes can also be tuned by the protein engineering approach for the DET-type reaction. This review summarizes the recent progresses in this field of the research while considering the importance of nanostructure of electrodes as well as redox enzymes. This review also describes the basic concepts and theoretical aspects of DET-type bioelectrocatalysis, the significance of nanostructures as scaffolds for DET-type reactions, protein engineering approaches for DET-type reactions, and concepts and facts of bidirectional DET-type reactions from a cross-disciplinary viewpoint.

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Section: Theoretical Aspects For the Det-type Bioelectrocatalysismentioning

confidence: 99%

Direct Electron Transfer-Type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes

et al. 2020

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“…[5,6] The actives ite of this familyo fm etalloenzymes is based on as et of two copper-containing centers:as urface-located Type 1C uc entre, at which the substrate is activated and oxidizeda nd ab uried Type 2/Type 3t rinuclearc entre (TNC). [7,8] Substrate mimicking strategy has been also developedb ym odifying the surfaceo felectrode materialb yt he enzyme substrate bilirubin [9] or other types of molecules such as porphyrins [10] or syringaldazine. Several BODs have been immobilized on electrodes and have demonstrated exceptional lowoverpotential electrocatalytic activity towards ORR.…”

Section: Introductionmentioning

confidence: 99%

“…Different studies have shown that orientation of MvBOD through electrostatic interactions using positivelyo rn egatively charged surfaces could promote DETof MvBOD. [7,8] Substrate mimicking strategy has been also developedb ym odifying the surfaceo felectrode materialb yt he enzyme substrate bilirubin [9] or other types of molecules such as porphyrins [10] or syringaldazine. [11] This strategy has led to highly-performing biocathodes, which have been successfully integrated in glucose or hydrogen enzymatic fuel cells.…”

Section: Introductionmentioning

confidence: 99%

Direct Electrochemistry of Bilirubin Oxidase from Magnaporthe orizae on Covalently‐Functionalized MWCNT for the Design of High‐Performance Oxygen‐Reducing Biocathodes

Gentil

Carrière

Cosnier

et al. 2018

Chemistry A European J

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Herein, the direct electrochemistry of bilirubin oxidase from Magnaporthe orizae (MoBOD) was studied on CNTs functionalized by electrografting several types of diazonium salts. The functionalization induces favorable or unfavorable orientation of MoBOD, the latter being compared to the well-known BOD from Myrothecium verrucaria (MvBOD). On the same nanostructured electrodes, MoBOD can surpass MvBOD in terms of both current densities and minimal overpotentials. Added to the fact that MoBOD is also highly active at the gas-diffusion electrode (GDE), these findings make MoBOD one of the MCOs with the highest catalytic activity towards the oxygen reduction reaction (ORR).

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“…Direct electron transfer (DET) between BOD - or its parent enzyme laccase – and electrochemical interfaces was obtained via appropriate modifications of electrode surfaces. 12,13 The most targeted configuration involved electrical connection of the T1, characterized in the absence of O 2 by a non-catalytic redox signal at the expected potential of the T1 Cu. In the presence of O 2 , a single catalytic wave for O 2 reduction is observed, consistent with the electrode replacing the electron-donating substrate.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of Chloride Inhibition of Bilirubin Oxidases and Its Dependence on Potential and pH

et al. 2017

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Bilirubin oxidases (BODs) belong to the multi-copper oxidase (MCO) family and efficiently reduce O2 at neutral pH and in physiological conditions where chloride concentrations are over 100 mM. BODs were consequently considered to be Cl− resistant contrary to laccases. However, there has not been a detailed study on the related effect of chloride and pH on the redox state of immobilized BODs. Here, we investigate by electrochemistry the catalytic mechanism of O2 reduction by the thermostable Bacillus pumilus BOD immobilized on carbon nanofibers in the presence of NaCl. The addition of chloride results in the formation of a redox state of the enzyme, previously observed for different BODs and laccases, which is only active after a reductive step. This behavior has not been previously investigated. We show for the first time that the kinetics of formation of this state is strongly dependent on pH, temperature, Cl− concentration and on the applied redox potential. UV-visible spectroscopy allows us to correlate the inhibition process by chloride with the formation of the alternative resting form of the enzyme. We demonstrate that O2 is not required for its formation and show that the application of an oxidative potential is sufficient. In addition, our results suggest that the reactivation may proceed thought the T3 β.

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Enhanced direct electron transfer-type bioelectrocatalysis of bilirubin oxidase on negatively charged aromatic compound-modified carbon electrode

Cited by 73 publications

References 44 publications

Direct Electron Transfer-Type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes

Direct Electron Transfer-Type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes

Direct Electrochemistry of Bilirubin Oxidase from Magnaporthe orizae on Covalently‐Functionalized MWCNT for the Design of High‐Performance Oxygen‐Reducing Biocathodes

Mechanism of Chloride Inhibition of Bilirubin Oxidases and Its Dependence on Potential and pH

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