Surface‐Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine‐Coordinated Heme Protein

Peng, Lei; Utesch, Tillmann; Yarman, Aysu; Jeoung, Jae‐Hun; Steinborn, Silke; Dobbek, Holger; Mroginski, María Andrea; Tanne, Johannes; Wollenberger, Ulla; Scheller, Frieder W.

doi:10.1002/chem.201405932

Cited by 15 publications

(21 citation statements)

References 36 publications

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“…Modeling studies highlight the crucial role played by the surface charge for effective reactions at the interface. For example, the hexameric tyrosine coordinated protein (HTHP) will adsorb in a nonproductive orientation for DET on positively charged SAMs [174]. In their work on sulfite oxidase adsorbing on SAMs, Utesch et al showed how the solution ionic strength impacts the enzyme adsorption [175].…”

Section: Importance Of Electrostatic Interactions To Drive the Orientmentioning

confidence: 99%

Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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Abstract:Redox enzymes, which catalyze reactions involving electron transfers in living organisms, are very promising components of biotechnological devices, and can be envisioned for sensing applications as well as for energy conversion. In this context, one of the most significant challenges is to achieve efficient direct electron transfer by tunneling between enzymes and conductive surfaces. Based on various examples of bioelectrochemical studies described in the recent literature, this review discusses the issue of enzyme immobilization at planar electrode interfaces. The fundamental importance of controlling enzyme orientation, how to obtain such orientation, and how it can be verified experimentally or by modeling are the three main directions explored. Since redox enzymes are sizable proteins with anisotropic properties, achieving their functional immobilization requires a specific and controlled orientation on the electrode surface. All the factors influenced by this orientation are described, ranging from electronic conductivity to efficiency of substrate supply. The specificities of the enzymatic molecule, surface properties, and dipole moment, which in turn influence the orientation, are introduced. Various ways of ensuring functional immobilization through tuning of both the enzyme and the electrode surface are then described. Finally, the review deals with analytical techniques that have enabled characterization and quantification of successful achievement of the desired orientation. The rich contributions of electrochemistry, spectroscopy (especially infrared spectroscopy), modeling, and microscopy are featured, along with their limitations.

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Section: Importance Of Electrostatic Interactions To Drive the Orientmentioning

confidence: 99%

Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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“…16,17 It has been proposed that mesoporous structures with porous radii close to the radius of an enzyme [18][19][20] and electrostatic interaction between the redox center of an enzyme and an electrode surface [21][22][23][24][25][26] are important to improve the performance of DET-type bioelectrocatalysis. Therefore, there seems to be some possibility to construct mesoporous electrodes suitable for DET reaction of POD.…”

Section: Introductionmentioning

confidence: 99%

Direct Electron Transfer-type Bioelectrocatalysis of Peroxidase at Mesoporous Carbon Electrodes and Its Application for Glucose Determination Based on Bienzyme System

et al. 2017

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Non-catalytic direct electron transfer (DET) signal of Compound I of horseradish peroxidase (POD) was first detected at 0.7 V on POD/carbon nanotube mixture-modified electrodes. Excellent performance of DET-type bioelectrocatalysis was achieved with POD immobilized with glutaraldehyde on Ketjen Black (KB)-modified electrodes for H2O2 reduction with an onset potential of 0.65 V (vs. Ag | AgCl | sat. KCl) without any electrode surface modification. The POD-immobilized KB electrode was found to be suitable for detecting H2O2 with a low detection limit (0.1 μM at S/N = 3) at -0.1 V. By co-immobilizing glucose oxidase (GOD) and POD on the KB-modified electrode, a bienzyme electrode was constructed to couple the oxidase reaction of GOD with the DET-type bioelectrocatalytic reduction of H2O2 by POD. The amperometric detection of glucose was performed with a high sensitivity (0.33 ± 0.01 μA cm -2 μM -1 ) and a low detection limit (2 μM at S/N = 3).

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“…Although some suitable redox mediators may assist electron transfer [34,35], several drawbacks arise [1-4, 10, 34, 35]: (a) the toxicity of the mediator, (b) leakage of the mediator, and (c) cell voltage loss to set up the driving force in the electron transfer between the enzyme and mediator. Therefore, multiple studies, such as creating novel electrode materials [36][37][38][39][40][41][42], functionalizing electrode surface [9,[43][44][45][46][47][48][49][50][51], and protein engineering [52][53][54], to improve DET-type bioelectrocatalysis have been reported.…”

Section: Introductionmentioning

confidence: 99%

Dual gas-diffusion membrane- and mediatorless dihydrogen/air-breathing biofuel cell operating at room temperature

Xia

Kitazumi

et al. 2016

Journal of Power Sources

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A membraneless direct electron transfer (DET)-type dihydrogen (H2)/air-breathing biofuel cell without any mediator was constructed wherein bilirubin oxidase from Myrothecium verrucaria (BOD) and membrane-bound [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F (MBH) were used as biocatalysts for the cathode and the anode, respectively, and Ketjen black-modified water proof carbon paper (KB/WPCC) was used as an electrode material. The KB/WPCC surface was modified with 2-aminobenzoic acid and p-phenylenediamine, respectively, to face the positively charged electron-accepting site of BOD and the negatively charged electron-donating site of MBH to the electrode surface. A gas-diffusion system was employed for the electrodes to realize high-speed substrate supply. As result, great improvement in the current density of O2 reduction with BOD and H2 reduction with MBH were realized at negatively and postively charged surfaces, repectively. Gas diffusion system also supressed the oxidative inactivation of MBH at high electrode potentials. Finally, based on the impoved bioanode and biocathode, a dual gas-diffusion membrane-and mediatorless H2/air-breathing biofuel cell was constructed. The maximum power density reached 6.1 mW cm −2 (at 0.72 V), and the open circuit voltage was 1.12 V using 1 atm of H2 gas as a fuel at room temperature and under passive and quiescent conditions.

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Surface‐Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine‐Coordinated Heme Protein

Cited by 15 publications

References 36 publications

Controlling Redox Enzyme Orientation at Planar Electrodes

Controlling Redox Enzyme Orientation at Planar Electrodes

Direct Electron Transfer-type Bioelectrocatalysis of Peroxidase at Mesoporous Carbon Electrodes and Its Application for Glucose Determination Based on Bienzyme System

Dual gas-diffusion membrane- and mediatorless dihydrogen/air-breathing biofuel cell operating at room temperature

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