293 - Electrocatalysis of a cathodic oxygen reduction by laccase

Тарасевич, М. Р.; Yaropolov, A. I.; Bogdanovskaya, V. A.; Варфоломеев, С. Д.

doi:10.1016/0302-4598(79)80006-9

Cited by 140 publications

(93 citation statements)

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“…DET in enzymes was first described in 1978 for laccase (Lc) [7][8]. Lc, together with ceruloplasmin, ascorbate oxidase, and bilirubin oxidase (BOx) belongs to the group of Cuproteins which are also known as blue multicopper oxidases.…”

Section: Introductionmentioning

confidence: 99%

“…Porous electrodes can be used to encapsulate the enzyme within a network of cavities, shortening the distance for electron transfer to the redox active site, which will promote more efficient and rapid rates of electron transfer [5]. However, the number of redox enzymes capable of interacting directly with the electrode while catalyzing the enzymatic reaction is limited, with estimates of approximately 5% of all enzymes exhibiting such a response [6].DET in enzymes was first described in 1978 for laccase (Lc) [7][8]. Lc, together with ceruloplasmin, ascorbate oxidase, and bilirubin oxidase (BOx) belongs to the group of Cuproteins which are also known as blue multicopper oxidases.…”

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confidence: 99%

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Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Salaj-Kośla

Pöller

Schuhmann

et al. 2013

Bioelectrochemistry

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The enzyme Trametes hirsuta laccase undergoes direct electron transfer at unmodified nanoporous gold electrodes, displaying a current density of 28 A/cm 2 . The response indicates that ThLc was immobilised at the surface of the nanopores in a manner which promoted direct electron transfer, in contrast to the absence of a response at unmodified polycrystalline gold electrodes. The bioelectrocatalytic activity of ThLc modified nanoporous gold electrodes was strongly dependent on the presence of halide ions. Fluoride completely inhibited the enzymatic response, whereas in the presence of 150 mM Cl -, the current was reduced to 50% of the response in the absence of Cl -. The current increased by 40% when the temperature was increased from 20°C to 37°C. The response is limited by enzymatic and/or enzyme electrode kinetics and is 30% of that observed for ThLc co-immobilised with an osmium redox polymer. Keywords: Laccase, direct electron transfer, nanoporous gold 2 IntroductionElectron transfer (ET) reactions are ubiquitous in nature. Controlling the rate of these reactions can be of significant benefit in developing biochemical systems that utilise redox proteins and enzymes and in particular, in applications that provide power for implanted or portable electronic devices. ET can be achieved directly (direct electron transfer, DET) or by the use of mediators (mediated electron transfer, MET) to shuttle electrons between the redox centre of the enzyme and the electrode. However, mediators are unselective and can also give rise to interfering effects [1][2][3]. DET-based devices offer high selectivity and sensitivity due to the absence of mediators. In addition, devices based on DET operate at potentials close to the redox potential of the enzyme, maximising the potential difference between the cathode and anode for biofuel cell applications [2]. Moreover, DET can be used to provide detailed information on the kinetics and thermodynamics of the ET process. However, the low stability of the enzyme layer together with the long distances over which ET occurs, represent major obstacles for DET based devices. In addition, the shielding mechanism of the enzymatic redox centre by the protein shell can disrupt DET [2,4]. One approach in optimizing and enabling rapid DET is to design the electrode surface with an architecture which promotes efficient rates of ET. In this way the electrode morphology ensures the most efficient orientation of the enzymatic redox centre and facilitates communication with the electroactive surface. Porous electrodes can be used to encapsulate the enzyme within a network of cavities, shortening the distance for electron transfer to the redox active site, which will promote more efficient and rapid rates of electron transfer [5]. However, the number of redox enzymes capable of interacting directly with the electrode while catalyzing the enzymatic reaction is limited, with estimates of approximately 5% of all enzymes exhibiting such a response [6].DET in enzymes was first described in 1978 fo...

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Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes

Salaj-Kośla

Pöller

Schuhmann

et al. 2013

Bioelectrochemistry

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“…This important feature, i.e. the absence of formation of H 2 O 2 during bioelectrocatalytic four-electron reduction of O 2 , was confirmed using the rotating ringdisk electrode method already in 1979 [7]. Detailed fundamental bioelectrochemical investigations of BMCO were performed using various planar electrodes [14].…”

Section: Introductionmentioning

confidence: 75%

“…At the end of the 1970s, direct electron transfer (DET) based bioelectrocatatalytic reduction of O 2 by a fungal laccase (Lc), an enzyme from the BMCO family, was discovered [6,7]. Later this occurrence was identified in many other redox enzymes including different BMCO, e.g.…”

Section: Introductionmentioning

confidence: 99%

Stable ‘Floating' Air Diffusion Biocathode Based on Direct Electron Transfer Reactions Between Carbon Particles and High Redox Potential Laccase

et al. 2010

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We report on the assembly and characterisation of a high potential, stable, mediator‐less and cofactor free biocathode based on a fungal laccase (Lc), adsorbed on highly dispersed carbonaceous materials. First, the stability and activity of Trametes hirsuta Lc immobilised on different carbon particles were studied and compared to the solubilised enzyme. Based on the experimental results and a literature analysis, the carbonaceous material BM‐4 was chosen to design efficient and stable biocatalysts for the production of a ‘floating' air diffusion Lc‐based biocathode. Voltammetric characteristics and operational stability of the biocathode were investigated. The current density of oxygen reduction at the motionless biocathode in a quiet, air saturated citrate buffer (100 mM, pH 4.5, 23 °C) reached values as high as 0.3 mA cm–2 already at 0.7 V versus NHE. The operational stability of the biocathode depended on the current density of the device. For example, at low current density (20 μA cm–2), the biocathode lost only 5× of its initial power after 1 month of continuous operation. However, when the device was polarised at 150 mV it lost more than 32× of its initial power in just 10 min. We also found that co‐immobilisation of Lc and peroxidase on highly dispersed carbon materials could protect the biocatalyst from rapid inactivation by hydrogen peroxide produced during electrocatalytic reactions at high‐current densities.

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“…c) also show efficient electron transfer with electrodes, e.g., cytochrome c peroxidase, cytochrome b 2 , cellobiose dehydrogenase, laccase and sulphite oxidase (Jin, et al, 1996, Fridman, et al, 2000, Ferapontova et al, 2003. In several additional cases researchers have proved that the natural electron acceptor/donor can be replaced by an electrode surface for some other redox enzymes, showing that a direct electronic communication can also occur between a redox enzyme and an electrode (Tarasevich, et al, 1979, Ghindilis, et al, 1997, Armstrong and Wilson, 2000. For heme containing redox enzymes, direct electron transfer (DET) between the heme group and the electrode has been postulated and in many cases demonstrated (Gorton, et al, 1999).…”

Section: Introductionmentioning

confidence: 99%