메뉴 건너뛰기




Volumn 107, Issue , 2016, Pages 30-36

Laccase-modified gold nanorods for electrocatalytic reduction of oxygen

Author keywords

Biocathode; Biofuel cell; Gold nanorod; Graphite; Laccase

Indexed keywords

BIOLOGICAL FUEL CELLS; ELECTROCHEMICAL ELECTRODES; ELECTRODES; ELECTROLYTIC REDUCTION; ELECTRON TRANSITIONS; ENZYMES; GRAPHITE; GRAPHITE ELECTRODES; NANORODS; PLASMONS;

EID: 84944462952     PISSN: 15675394     EISSN: 1878562X     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2015.10.003     Document Type: Article
Times cited : (22)

References (41)
  • 2
    • 7744236144 scopus 로고    scopus 로고
    • Multicopper oxidases and oxygenases
    • Solomon E., Sundaram U., Machonkin T. Multicopper oxidases and oxygenases. Chem. Rev. 1996, 96:2563-2606.
    • (1996) Chem. Rev. , vol.96 , pp. 2563-2606
    • Solomon, E.1    Sundaram, U.2    Machonkin, T.3
  • 3
    • 84863550109 scopus 로고    scopus 로고
    • On the possibility of uphill intramolecular electron transfer in multicopper oxidases: electrochemical and quantum chemical study of bilirubin oxidase
    • Shleev S., Andoralov V., Falk M., Reimann C.T., Ruzgas T., Srnec M., Ryde U., Rulisek L. On the possibility of uphill intramolecular electron transfer in multicopper oxidases: electrochemical and quantum chemical study of bilirubin oxidase. Electroanalysis 2012, 24:1524-1540.
    • (2012) Electroanalysis , vol.24 , pp. 1524-1540
    • Shleev, S.1    Andoralov, V.2    Falk, M.3    Reimann, C.T.4    Ruzgas, T.5    Srnec, M.6    Ryde, U.7    Rulisek, L.8
  • 4
    • 77958607481 scopus 로고    scopus 로고
    • Mechanistic studies of the 'blue' Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction
    • dos Santos L., Climent V., Blanford C.F., Armstrong F.A. Mechanistic studies of the 'blue' Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction. Phys. Chem. Chem. Phys. 2010, 12:13962-13974.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 13962-13974
    • dos Santos, L.1    Climent, V.2    Blanford, C.F.3    Armstrong, F.A.4
  • 7
    • 7544227821 scopus 로고    scopus 로고
    • Enzymatic biofuel cells for implantable and microscale devices
    • Barton S.C., Gallaway J., Atanassov P. Enzymatic biofuel cells for implantable and microscale devices. Chem. Rev. 2004, 104:4867-4886.
    • (2004) Chem. Rev. , vol.104 , pp. 4867-4886
    • Barton, S.C.1    Gallaway, J.2    Atanassov, P.3
  • 12
    • 77953293555 scopus 로고    scopus 로고
    • 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 hirsutalaccase
    • Ackermann Y., Guschin D.A., Eckhard K., Shleev S., Schuhmann W. 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 hirsutalaccase. Electrochem. Commun. 2010, 12:640-643.
    • (2010) Electrochem. Commun. , vol.12 , pp. 640-643
    • Ackermann, Y.1    Guschin, D.A.2    Eckhard, K.3    Shleev, S.4    Schuhmann, W.5
  • 13
    • 55049095938 scopus 로고    scopus 로고
    • Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase laccase directly attached to chemically modified carbons
    • Blanford C.F., Foster C.E., Heath R.S., Armstrong F.A. Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase laccase directly attached to chemically modified carbons. Faraday Discuss. 2009, 140:319-335.
    • (2009) Faraday Discuss. , vol.140 , pp. 319-335
    • Blanford, C.F.1    Foster, C.E.2    Heath, R.S.3    Armstrong, F.A.4
  • 16
    • 84865005899 scopus 로고    scopus 로고
    • Combined ATR-SEIRAS and EC-STM study of the immobilization of laccase on chemically modified Au electrodes
    • Vaz-Domínguez C., Pita M., De Lacey A.L., Shleev S., Cuesta A. Combined ATR-SEIRAS and EC-STM study of the immobilization of laccase on chemically modified Au electrodes. J. Phys. Chem. C 2012, 116:16532-16540.
    • (2012) J. Phys. Chem. C , vol.116 , pp. 16532-16540
    • Vaz-Domínguez, C.1    Pita, M.2    De Lacey, A.L.3    Shleev, S.4    Cuesta, A.5
  • 18
    • 79953902587 scopus 로고    scopus 로고
    • Self-regulating enzyme-nanotube ensemble films and their application as flexible electrodes for biofuel cells
    • Miyake T., Yoshino S., Yamada T., Hata K., Nishizawa M. Self-regulating enzyme-nanotube ensemble films and their application as flexible electrodes for biofuel cells. J. Am. Chem. Soc. 2011, 133:5129-5134.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5129-5134
    • Miyake, T.1    Yoshino, S.2    Yamada, T.3    Hata, K.4    Nishizawa, M.5
  • 19
    • 82955194837 scopus 로고    scopus 로고
    • Anthracene-modified multi-walled carbon nanotubes as direct electron transfer scaffolds for enzymatic oxygen reduction
    • Meredith M.T., Minson M., Hickey D., Artyushkova K., Glatzhofer D.T., Minteer S.D. Anthracene-modified multi-walled carbon nanotubes as direct electron transfer scaffolds for enzymatic oxygen reduction. ACS Catal. 2011, 1:1683-1690.
    • (2011) ACS Catal. , vol.1 , pp. 1683-1690
    • Meredith, M.T.1    Minson, M.2    Hickey, D.3    Artyushkova, K.4    Glatzhofer, D.T.5    Minteer, S.D.6
  • 21
    • 84866366891 scopus 로고    scopus 로고
    • Enhanced direct electron transfer between laccase and hierarchical carbon microfibers/carbon nanotubes composite electrodes. Comparison of three enzyme immobilization methods
    • Gutiérrez-Sánchez C., Jia W., Beyl Y., Pita M., Schuhmann W., De Lacey A.L., Stoica L. Enhanced direct electron transfer between laccase and hierarchical carbon microfibers/carbon nanotubes composite electrodes. Comparison of three enzyme immobilization methods. Electrochim. Acta 2012, 82:218-223.
    • (2012) Electrochim. Acta , vol.82 , pp. 218-223
    • Gutiérrez-Sánchez, C.1    Jia, W.2    Beyl, Y.3    Pita, M.4    Schuhmann, W.5    De Lacey, A.L.6    Stoica, L.7
  • 22
    • 84865109292 scopus 로고    scopus 로고
    • Mass transport controlled oxygen reduction at anthraquinone modified 3D-CNT electrodes with immobilized Trametes hirsuta laccase
    • Sosna M., Stoica L., Wright E., Kilburn J., Schuhmann W., Bartlett P.N. Mass transport controlled oxygen reduction at anthraquinone modified 3D-CNT electrodes with immobilized Trametes hirsuta laccase. Phys. Chem. Chem. Phys. 2012, 14:11882-11885.
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 11882-11885
    • Sosna, M.1    Stoica, L.2    Wright, E.3    Kilburn, J.4    Schuhmann, W.5    Bartlett, P.N.6
  • 24
    • 0020813840 scopus 로고
    • Electrochemical study of gold electrodes with anodic oxide films. 1. Formation and reduction behaviour of anodic oxides on gold
    • Oesch U., Janata J. Electrochemical study of gold electrodes with anodic oxide films. 1. Formation and reduction behaviour of anodic oxides on gold. Electrochim. Acta 1983, 28:1237-1246.
    • (1983) Electrochim. Acta , vol.28 , pp. 1237-1246
    • Oesch, U.1    Janata, J.2
  • 26
    • 84878993114 scopus 로고    scopus 로고
    • Bilirubin oxidase-based nanobiocathode working in serum-mimic buffer for implantable biofuel cell
    • Gutiérrez-Sánchez C., Pita M., Toscano M.D., De Lacey A.L. Bilirubin oxidase-based nanobiocathode working in serum-mimic buffer for implantable biofuel cell. Electroanalysis 2013, 25:1359-1362.
    • (2013) Electroanalysis , vol.25 , pp. 1359-1362
    • Gutiérrez-Sánchez, C.1    Pita, M.2    Toscano, M.D.3    De Lacey, A.L.4
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 84862872328 scopus 로고    scopus 로고
    • Synthesis and optical properties of small Au nanorods using a seedless growth technique
    • Ali M.R.K., Snyder B., El-Sayed M.A. Synthesis and optical properties of small Au nanorods using a seedless growth technique. Langmuir 2012, 28:9807-9815.
    • (2012) Langmuir , vol.28 , pp. 9807-9815
    • Ali, M.R.K.1    Snyder, B.2    El-Sayed, M.A.3
  • 30
    • 0027663721 scopus 로고
    • A new hydrosol of gold clusters. 1. Formation and particle size variation
    • Duff D., Baiker A., Edwards P.P. A new hydrosol of gold clusters. 1. Formation and particle size variation. Langmuir 1993, 9:2301-2309.
    • (1993) Langmuir , vol.9 , pp. 2301-2309
    • Duff, D.1    Baiker, A.2    Edwards, P.P.3
  • 31
    • 0037137649 scopus 로고    scopus 로고
    • Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes
    • Leger C., Jones A.K., Albracht S.P.J., Armstrong F.A. Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes. J. Phys. Chem. B 2002, 106:13058-13063.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 13058-13063
    • Leger, C.1    Jones, A.K.2    Albracht, S.P.J.3    Armstrong, F.A.4
  • 32
    • 72149128516 scopus 로고    scopus 로고
    • Direct electrochemistry of bilirubin oxidase on three-dimensional gold nanoparticle electrodes and its application in a biofuel cell
    • Murata K., Kajiya K., Nakamura N., Ohno H. Direct electrochemistry of bilirubin oxidase on three-dimensional gold nanoparticle electrodes and its application in a biofuel cell. Energy Environ. Sci. 2009, 2:1280-1285.
    • (2009) Energy Environ. Sci. , vol.2 , pp. 1280-1285
    • Murata, K.1    Kajiya, K.2    Nakamura, N.3    Ohno, H.4
  • 34
    • 77956570124 scopus 로고    scopus 로고
    • Electrocatalytic oxygen reduction on functionalized gold nanoparticles incorporated in a hydrophobic environment
    • Mirkhalaf F., Schiffrin D.J. Electrocatalytic oxygen reduction on functionalized gold nanoparticles incorporated in a hydrophobic environment. Langmuir 2010, 26:14995-15001.
    • (2010) Langmuir , vol.26 , pp. 14995-15001
    • Mirkhalaf, F.1    Schiffrin, D.J.2
  • 36
    • 4544231693 scopus 로고    scopus 로고
    • Bioelectrocatalysis of oxygen reduction reaction by laccase on gold electrodes
    • Gupta G., Rajendran V., Atanassov P. Bioelectrocatalysis of oxygen reduction reaction by laccase on gold electrodes. Electroanalysis 2004, 16:1182-1185.
    • (2004) Electroanalysis , vol.16 , pp. 1182-1185
    • Gupta, G.1    Rajendran, V.2    Atanassov, P.3
  • 37
    • 15844415813 scopus 로고
    • Mechanism of the inhibition of laccase activity from polyporus versicolor by halide-ions
    • Naki A., Varfolomeev S.D. Mechanism of the inhibition of laccase activity from polyporus versicolor by halide-ions. Biochem. Mosc. 1981, 46:1344-1350.
    • (1981) Biochem. Mosc. , vol.46 , pp. 1344-1350
    • Naki, A.1    Varfolomeev, S.D.2
  • 39
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • Leger C., Bertrand P. Direct electrochemistry of redox enzymes as a tool for mechanistic studies. Chem. Rev. 2008, 108:2379-2438.
    • (2008) Chem. Rev. , vol.108 , pp. 2379-2438
    • Leger, C.1    Bertrand, P.2
  • 41
    • 77954574396 scopus 로고    scopus 로고
    • Kinetics of electrocatalytic reduction of oxygen and hydrogen peroxide on dispersed gold nanoparticles
    • Jirkovsky J.S., Halasa M., Schiffrin D.J. Kinetics of electrocatalytic reduction of oxygen and hydrogen peroxide on dispersed gold nanoparticles. Phys. Chem. Chem. Phys. 2010, 12:8042-8052.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 8042-8052
    • Jirkovsky, J.S.1    Halasa, M.2    Schiffrin, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.