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  • 1. Ackermann, Yvonne
    et al.
    Guschin, Dmitrii
    Eckhard, Kathrin
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Schuhmann, Wolfgang
    Design of a bioelectrocatalytic electrode interface for oxygen reduction in biofuel cells based on a specifically adapted Os-complex containing redox polymer with entrapped Trametes hirsuta laccase2010Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 12, nr 5, s. 640-643Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The design of the coordination shell of an Os-complex and its integration within an electrodeposition polymer enables fast electron transfer between an electrode and a polymer entrapped high-potential laccase from the basidiomycete Trametes hirsuta. The redox potential of the Os3+/2+-centre tethered to the polymer backbone (+720 mV vs. NHE) is perfectly matching the potential of the enzyme (+780 mV vs. NHE at pH 6.5). The laccase and the Os-complex modified anodic electrodeposition polymer were simultaneously precipitated on the surface of a glassy carbon electrode by means of a pH-shift to 2.5. The modified electrode was investigated with respect to biocatalytic oxygen reduction to water. The proposed modified electrode has potential applications as biofuel cell cathode.

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  • 2.
    Aleksejeva, Olga
    et al.
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Mateljak, Ivan
    Department of Biocatalysis, Institute of Catalysis, CSIC, Cantoblanco, Madrid, 28094, Spain.
    Ludwig, Roland
    Department of Food Sciences and Technology, VIBT – Vienna Institute of Biotechnology, BOKU – University of Natural Resources and Life Sciences, Vienna, A-1190, Austria.
    Alcalde, Miguel
    Department of Biocatalysis, Institute of Catalysis, CSIC, Cantoblanco, Madrid, 28094, Spain.
    Shleev, Sergey
    Malmö universitet, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Electrochemistry of a high redox potential laccase obtained by computer-guided mutagenesis combined with directed evolution2019Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 106, artikel-id UNSP 106511Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Electrochemical characterization of the GreeDo variant of a high redox potential fungal laccase obtained by laboratory evolution together with computer-guided mutagenesis, in comparison to its parental variety (the OB-1 mutant), is presented. Both laccases, when immobilized on graphite electrodes either by direct physical adsorption or covalently attached via gold nanoparticles, were capable of both non-mediated and mediator-based bioelectroreduction of molecular oxygen at low overpotentials. GreeDo exhibited higher open circuit potential values and onset potentials for oxygen bioelectroreduction compared to OB-1. However, even though in homogeneous catalysis GreeDo outperforms OB-1 in terms of turnover numbers and catalytic efficiency, when exposed to high redox potential substrates, direct electron transfer based bioelectrocatalytic currents of GreeDo and OB-1 modified electrodes were similar. High operational stability of freely diffusing GreeDo and also the immobilized enzyme in the acidic electrolyte was registered, in agreement with high storage stability of GreeDo in acidic solutions.

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  • 3. Beyl, Yvonne
    et al.
    Guschin, Dmitrii
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Schuhmann, Wolfgang
    A chloride resistant high potential oxygen reducing biocathode based on a fungal laccase incorporated into an optimized Os-complex modified redox hydrogel2011Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 13, nr 5, s. 474-476Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A chloride-resistant high-potential biocathode based on Trametes hirsuta laccase incorporated into an optimized Os-complex modified redox hydrogel (80 mV potential difference to the T1 Cu) is described. The bioelectrocatalytic activity towards O2 reduction is due to an intimate access of the polymer-bound Os-complex to the T1 Cu site. The chloride resistance of the biocathode is due to the tight binding of the polymer-bound Os-complex to the T1 Cu site.

  • 4. Clot, Sylvain
    et al.
    Gutierrez-Sanchez, Cristina
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    De Lacey, Antonio
    Pita, Marcos
    Laccase cathode approaches to physiological conditions by local pH acidification2012Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 18, s. 37-40Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A new conceptual approach to improve the performance of a laccase-based cathode at neutral pH is presented. The working pH of Trametes hirsuta laccase, typically acidic, can be achieved by oxidn. of biol. compds. such as glucose catalyzed by a second enzyme immobilized in the vicinity of the laccase electrode.

  • 5. Dagys, Marius
    et al.
    Haberska, Karolina
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Arnebrant, Thomas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Kulys, Juozas
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Laccase-gold nanoparticle assisted bioelectrocatalytic reduction of oxygen2010Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 12, nr 7, s. 933-935Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    It was found that homogeneous activity of Trametes hirsuta laccase is considerably diminished in the presence of gold nanoparticles (Au-NPs). Heterogeneous electron transfer studies revealed that Au-NPs facilitate direct electron transfer (DET) between the T1 copper site of the laccase and the surface of Au-NP modified electrodes. DET was characterized by the standard heterogeneous ET constant of 0.5 +/- 0.6 s(-1) at Au-NPs with an average diameter of 50 nm. As a consequence of this a well pronounced DET based bioelectrocatalytic oxygen reduction with current densities of 5-30 mu A cm(-2) has been achieved at the laccase-Au-NP modified electrodes.

  • 6.
    Gonzalez-Arribas, Elena
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Aleksejeva, Olga
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Bobrowski, Tim
    Analytical Chemistry – Center for Electrochemical Sciences (CES), Ruhr-Universität Bochum, Universitätsstr. 150, Bochum, 44780, Germany.
    Toscano, Miguel
    Novozymes A/S, Krogshoejvej 36, Bagsvaerd, 2880, Denmark.
    Gorton, Lo
    Department of Biochemistry and Structural Biology, Lund University, P.O. Box 124, Lund, 22100, Sweden.
    Schuhmann, Wolfgang
    Analytical Chemistry – Center for Electrochemical Sciences (CES), Ruhr-Universität Bochum, Universitätsstr. 150, Bochum, 44780, Germany.
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Solar biosupercapacitor2016Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 74, s. 9-13Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Here we report on an entirely new kind of bioelectronic device - a solar biosupercapacitor, which is built from a dual-​feature photobioanode combined with a double-​function enzymic cathode. The self-​charging biodevice, based on transparent nanostructured indium tin oxide electrodes modified with biol. catalysts, i.e. thylakoid membranes and bilirubin oxidase, is able to capacitively store electricity produced by direct conversion of radiant energy into elec. energy. When self-​charged during 10 min, using ambient light only, the biosupercapacitor provided a max. of 6 mW m-​ 2 at 0.20 V.

  • 7.
    Khlupova, M.
    et al.
    Laboratory of Chemical Enzymology, Bach Institute of Biochemistry, 119071 Moscow, Russia.
    Kuznetsov, B.
    Laboratory of Chemical Enzymology, Bach Institute of Biochemistry, 119071 Moscow, Russia.
    Gonchar, M.
    Department of Cell Regulatory Systems, Institute of Cell Biology, Drahomanov Street 14/16, 79005 Lviv, Ukraine.
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS). Laboratory of Chemical Enzymology, Bach Institute of Biochemistry, 119071 Moscow, Russia; Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
    Amperometric monitoring of redox activity in intact, permeabilised and lyophilised cells of the yeast Hansenula polymorpha2007Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 9, nr 7, s. 1480-1485Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    An effect of permeabilisation and lyophilisation of the yeast cells Hansenula polymorpha on their electrochemical behaviour in the presence of mediators, substrates (formaldehyde, glucose, methanol, ethanol), and cofactors (NAD+, NADP+, NADH, NADPH, glutathione) has been studied. Two amperometric techniques differing in the cell immobilisation methods were applied. The cells of a wild strain (356) and mutant strains (C-105 and KCA 33) of the yeast, grown in the presence of glucose or methanol, were used in the experiments. The intact cells revealed the highest reduction rates of mediators, 2,6-dichlorphenolindophenol (DCIP) and 2,4-benzoquinone (BQ), as measured by amperometry. The addition of formaldehyde significantly enhanced the response, if the cells were grown in the presence of glucose. The permeabilised cells showed the lowest current level in the presence of DCIP and BQ and no response to the addition of formaldehyde and NAD+. However, the addition of NADH gave significant current surge. All these phenomena imply that the permeabilised cells lost cofactors and the activity of dehydrogenases producing NADH, but they remained the activity of NADH-ubiquinone oxidoreductase and of some components of the electron transport chain. The electrochemical behaviour of the lyophilised cells shows they are heterogeneous. The partial degradation of the outer membrane of the cells after their lyophilisation was electrochemically confirmed.

  • 8.
    Pita, Marcos
    et al.
    Instituto de Catálisis y Petroleoquímica CSIC, Marie Curie 2, 28049 Madrid, Spain.
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS). Lund University, Department of Analytical Chemistry, SE-221 00 Lund, Sweden; Institute of Biochemistry, Laboratory of Chemical Enzymology, 119071 Moscow, Russia.
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Fernandez, Victor M
    Instituto de Catálisis y Petroleoquímica CSIC, Marie Curie 2, 28049 Madrid, Spain.
    Yaropolov, Alexander
    Institute of Biochemistry, Laboratory of Chemical Enzymology, 119071 Moscow, Russia.
    Gorton, Lo
    Lund University, Department of Analytical Chemistry, SE-221 00 Lund, Sweden.
    Direct heterogeneous electron transfer reactions of fungal laccases at bare and thiol-modified gold electrodes2006Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 8, nr 5, s. 747-753Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Mediatorless (direct) electron transfer between bare and thiol-modified gold electrodes and fungal laccases from different sources has been demonstrated. The electrochemical activity of the enzymes from basidiomycetes Trametes hirsuta, Trametes ochracea, and Cerrena maxima under aerobic and anaerobic conditions can clearly be observed using cyclic voltammetry and spectroelectrochemistry. Bioelectroreduction of oxygen by T. hirsuta laccase immobilized on amino-thiophenol-modified gold electrodes, starting at +625 mV vs. NHE, is demonstrated and differences in bioelectrocatalysis of the enzyme immobilized on bare and thiol-modified electrodes are shown. It was found that hydrogen peroxide was one of the products of oxygen electroreduction on gold electrodes modified with fungal laccases, whereas no significant peroxide formation was observed for T. hirsuta laccase immobilised on thiol-modified gold electrodes. Thus, a hypothesis about two different mechanisms of oxygen electroreduction by fungal laccases adsorbed on bare and thiol-modified electrodes is proposed.

  • 9. Salaj-Kosla, Urszula
    et al.
    Poeller, Sascha
    Beyl, Yvonne
    Scanlon, Micheal
    Beloshapkin, Sergey
    Shleev, Sergey
    Malmö högskola, Fakulteten för hälsa och samhälle (HS), Institutionen för biomedicinsk vetenskap (BMV).
    Schuhmann, Wolfgang
    Magner, Edmond
    Direct electron transfer of bilirubin oxidase (Myrothecium verrucaria) at an unmodified nanoporous gold biocathode2012Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 16, nr 1, s. 92-95Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Well defined mediatorless bioelectrocatalytic redn. of oxygen with high current densities of 0.8 mA cm- 2 was obtained on nanoporous gold electrodes modified with Myrothecium verrucaria bilirubin oxidase. A stable faradaic response was obsd. when the enzyme modified electrode was coated with a specifically designed electrodeposition polymer layer. The response of the enzyme electrode was only slightly inhibited by the addn. of F-.

  • 10.
    Shleev, Sergey
    et al.
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    El Kasmi, A
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Gorton, L D
    Direct heterogeneous electron transfer reactions of bilirubin oxidase at a spectrographic graphite electrode2004Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 6, nr 9, s. 934-939Artikel i tidskrift (Refereegranskat)
  • 11.
    Tkac, Jan
    et al.
    Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden; Institute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 812 37 Bratislava, Slovak Republic.
    Ruzgas, Tautgirdas
    Malmö högskola, Fakulteten för hälsa och samhälle (HS).
    Dispersion of single walled carbon nanotubes. Comparison of different dispersing strategies for preparation of modified electrodes toward hydrogen peroxide detection2006Ingår i: Electrochemistry communications, ISSN 1388-2481, E-ISSN 1873-1902, Vol. 8, nr 5, s. 899-903Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Four different dispersing agents for solubilisation of single walled carbon nanotubes (SWNT) are here compared. Dispersing agents used here can be divided into the group of organic solvents (dimethylformamide and cyclohexanone) and charged polymers (Nafion and chitosan). Charged polymers are more efficient dispersing agents allowing quicker dispersion of nanotubes compared to solvents. Moreover charged polymers offer higher stability of dispersion. Cyclic voltammograms of hydrogen peroxide at SWNT-modified electrodes highly depended on the dispersing agent and dispersion procedure used to disintegrate SWNT aggregates for electrode modification. The best performance for detection of hydrogen peroxide was obtained on a nanotube film cast from a chitosan solution offering a quick dispersion and high dispersion stability as well as high sensitivity of detection and mechanical stability of the nanotube film.

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