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Volumn 28, Issue 29, 2012, Pages 10925-10933

Direct electrochemistry of phanerochaete chrysosporium cellobiose dehydrogenase covalently attached onto gold nanoparticle modified solid gold electrodes

Author keywords

[No Author keywords available]

Indexed keywords

4-AMINOTHIOPHENOL; 4-MERCAPTOBENZOIC ACIDS; 4-MERCAPTOPHENOL; BIOELECTROCATALYSIS; BIOELECTROCHEMISTRY; CELLOBIOSE DEHYDROGENASE; COVALENT IMMOBILIZATION; COVALENT LINKAGE; CROSSLINKER; DIRECT ELECTROCHEMISTRY; DIRECT ELECTRON TRANSFER; ELECTROCHEMICAL RESPONSE; ELECTRODE MATERIAL; ELECTRONIC APPLICATION; EXTRACELLULAR; FAST ELECTRON TRANSFER; FLAVOCYTOCHROME; FLEXIBLE LINKERS; FORMAL POTENTIAL; GLUTARALDEHYDES; GOLD ELECTRODES; GOLD NANOPARTICLE; GOLD NANOPARTICLES; LACTOSE OXIDATION; MIXED SAM; MIXED SELF ASSEMBLED MONOLAYERS; MODIFIED ELECTRODES; PHANEROCHAETE CHRYSOSPORIUM; POLYCRYSTALLINE GOLD; REDOX ENZYME; SURFACE COVERAGES; TWO DOMAINS;

EID: 84864369357     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la3018858     Document Type: Article
Times cited : (52)

References (43)
  • 1
    • 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 (7) 2379-2438
    • (2008) Chem. Rev. , vol.108 , Issue.7 , pp. 2379-2438
    • Leger, C.1    Bertrand, P.2
  • 2
    • 77956752465 scopus 로고
    • Direct electrochemistry of proteins and enzymes
    • Guo, L.-H.; Hill, H. A. O. Direct electrochemistry of proteins and enzymes Adv. Inorg. Chem. 1991, 36, 341-375
    • (1991) Adv. Inorg. Chem. , vol.36 , pp. 341-375
    • Guo, L.-H.1    Hill, H.A.O.2
  • 3
    • 0001555718 scopus 로고    scopus 로고
    • Enzyme-catalyzed direct electron transfer. Fundamentals and analytical applications
    • Ghindilis, A. L.; Atanasov, P.; Wilkins, E. Enzyme-catalyzed direct electron transfer. Fundamentals and analytical applications Electroanalysis 1997, 9 (9) 661-674
    • (1997) Electroanalysis , vol.9 , Issue.9 , pp. 661-674
    • Ghindilis, A.L.1    Atanasov, P.2    Wilkins, E.3
  • 4
    • 0032717605 scopus 로고    scopus 로고
    • Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors
    • Gorton, L.; Lindgren, A.; Larsson, T.; Munteanu, F. D.; Ruzgas, T.; Gazaryan, I. Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors Anal. Chim. Acta 1999, 400 (1-3) 91-108
    • (1999) Anal. Chim. Acta , vol.400 , Issue.1-3 , pp. 91-108
    • Gorton, L.1    Lindgren, A.2    Larsson, T.3    Munteanu, F.D.4    Ruzgas, T.5    Gazaryan, I.6
  • 6
    • 49049118534 scopus 로고    scopus 로고
    • Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis
    • Cracknell, J. A.; Vincent, K. A.; Armstrong, F. A. Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis Chem. Rev. 2008, 108 (7) 2439-2461
    • (2008) Chem. Rev. , vol.108 , Issue.7 , pp. 2439-2461
    • Cracknell, J.A.1    Vincent, K.A.2    Armstrong, F.A.3
  • 7
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • Langston, J. A.; Shaghasi, T.; Abbate, E.; Xu, F.; Vlasenko, E.; Sweeney, M. D. Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61 Appl. Environ. Microbiol. 2011, 77, 7007-7015
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6
  • 8
    • 84855912007 scopus 로고    scopus 로고
    • Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases
    • Beeson, W. T.; Phillips, C. M.; Cate, J. H. D.; Marletta, M. A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases J. Am. Chem. Soc. 2012, 134, 890-892
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 890-892
    • Beeson, W.T.1    Phillips, C.M.2    Cate, J.H.D.3    Marletta, M.A.4
  • 9
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • Phillips, C. M.; Beeson, W. T. I. V.; Cate, J. H.; Marletta, M. A. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa ACS Chem. Biol. 2011, 6, 1399-1406
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.I.V.2    Cate, J.H.3    Marletta, M.A.4
  • 10
    • 77956791837 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase: A versatile catalyst for electrochemical applications
    • Ludwig, R.; Harreither, W.; Tasca, F.; Gorton, L. Cellobiose dehydrogenase: A versatile catalyst for electrochemical applications ChemPhysChem 2010, 11, 2674-2697
    • (2010) ChemPhysChem , vol.11 , pp. 2674-2697
    • Ludwig, R.1    Harreither, W.2    Tasca, F.3    Gorton, L.4
  • 11
    • 46049096923 scopus 로고    scopus 로고
    • Role of carbon nanotubes in electroanalytical chemistry: A review
    • AgüíÂ, L.; YáńÂez- SedeńÂo, P.; PingarróÂn, J. M. Role of carbon nanotubes in electroanalytical chemistry: A review Anal. Chim. Acta 2008, 622 (1-2) 11-47
    • (2008) Anal. Chim. Acta , vol.622 , Issue.1-2 , pp. 11-47
    • Agüíâ, L.1    Yáńâez- Sedeńâo, P.2    Pingarróân, J.M.3
  • 14
    • 84867862483 scopus 로고    scopus 로고
    • Mediatorless high-power glucose biofuel cells based on compressed carbon nanotube-enzyme electrodes
    • 1365/1-1365/6
    • Zebda, A.; Gondran, C.; Le, G. A.; Holzinger, M.; Cinquin, P.; Cosnier, S. Mediatorless high-power glucose biofuel cells based on compressed carbon nanotube-enzyme electrodes Nat. Commun. 2011, 2 (1365/1-1365/6) S1365/1-S1365/3
    • (2011) Nat. Commun. , vol.2
    • Zebda, A.1    Gondran, C.2    Le, G.A.3    Holzinger, M.4    Cinquin, P.5    Cosnier, S.6
  • 16
    • 4544315692 scopus 로고    scopus 로고
    • Long-range electrical contacting of redox enzymes by SWCNT connectors
    • Patolsky, F.; Weizmann, Y.; Willner, I. Long-range electrical contacting of redox enzymes by SWCNT connectors Angew. Chem., Int. Ed. 2004, 43 (16) 2113-2117
    • (2004) Angew. Chem., Int. Ed. , vol.43 , Issue.16 , pp. 2113-2117
    • Patolsky, F.1    Weizmann, Y.2    Willner, I.3
  • 17
    • 84859374980 scopus 로고    scopus 로고
    • Characteristics of third-generation glucose biosensors based on Corynascus thermophilus cellobiose dehydrogenase immobilized on commercially available screen-printed electrodes working under physiological conditions
    • Zafar, M. N.; Safina, G.; Ludwig, R.; Gorton, L. Characteristics of third-generation glucose biosensors based on Corynascus thermophilus cellobiose dehydrogenase immobilized on commercially available screen-printed electrodes working under physiological conditions Anal. Biochem. 2012, 425 (1) 36-42
    • (2012) Anal. Biochem. , vol.425 , Issue.1 , pp. 36-42
    • Zafar, M.N.1    Safina, G.2    Ludwig, R.3    Gorton, L.4
  • 18
    • 48249108041 scopus 로고    scopus 로고
    • Direct electron transfer at cellobiose dehydrogenase modified anodes for biofuel cells
    • Tasca, F.; Gorton, L.; Harreither, W.; Haltrich, D.; Ludwig, R.; Nöll, G. Direct electron transfer at cellobiose dehydrogenase modified anodes for biofuel cells J. Phys. Chem. C 2008, 112 (26) 9956-9961
    • (2008) J. Phys. Chem. C , vol.112 , Issue.26 , pp. 9956-9961
    • Tasca, F.1    Gorton, L.2    Harreither, W.3    Haltrich, D.4    Ludwig, R.5    Nöll, G.6
  • 19
    • 52649106024 scopus 로고    scopus 로고
    • Highly efficient and versatile anodes for biofuel cells based on cellobiose dehydrogenase from Myriococcum thermophilum
    • Tasca, F.; Gorton, L.; Harreither, W.; Haltrich, D.; Ludwig, R.; Nöll, G. Highly efficient and versatile anodes for biofuel cells based on cellobiose dehydrogenase from Myriococcum thermophilum J. Phys. Chem. C 2008, 112 (35) 13668-13673
    • (2008) J. Phys. Chem. C , vol.112 , Issue.35 , pp. 13668-13673
    • Tasca, F.1    Gorton, L.2    Harreither, W.3    Haltrich, D.4    Ludwig, R.5    Nöll, G.6
  • 20
    • 77956806866 scopus 로고    scopus 로고
    • A simple and sensitive method for lactose detection based on direct electron transfer between immobilised cellobiose dehydrogenase and screen-printed carbon electrodes
    • Safina, G.; Ludwig, R.; Gorton, L. A simple and sensitive method for lactose detection based on direct electron transfer between immobilised cellobiose dehydrogenase and screen-printed carbon electrodes Electrochim. Acta 2010, 55, 7690-7695
    • (2010) Electrochim. Acta , vol.55 , pp. 7690-7695
    • Safina, G.1    Ludwig, R.2    Gorton, L.3
  • 21
    • 0034670332 scopus 로고    scopus 로고
    • Direct electron transfer between the heme of cellobiose dehydrogenase and thiol modified gold electrodes
    • Lindgren, A.; Larsson, T.; Ruzgas, T.; Gorton, L. Direct electron transfer between the heme of cellobiose dehydrogenase and thiol modified gold electrodes J. Electroanal. Chem. 2000, 494 (2) 105-113
    • (2000) J. Electroanal. Chem. , vol.494 , Issue.2 , pp. 105-113
    • Lindgren, A.1    Larsson, T.2    Ruzgas, T.3    Gorton, L.4
  • 22
    • 0035910243 scopus 로고    scopus 로고
    • Direct electron transfer of cellobiose dehydrogenase from various biological origins at gold and graphite electrodes
    • Lindgren, A.; Gorton, L.; Ruzgas, T.; Baminger, U.; Haltrich, D.; Schülein, M. Direct electron transfer of cellobiose dehydrogenase from various biological origins at gold and graphite electrodes J. Electroanal. Chem. 2001, 496 (1-2) 76-81
    • (2001) J. Electroanal. Chem. , vol.496 , Issue.1-2 , pp. 76-81
    • Lindgren, A.1    Gorton, L.2    Ruzgas, T.3    Baminger, U.4    Haltrich, D.5    Schülein, M.6
  • 23
    • 14644411719 scopus 로고    scopus 로고
    • Electrochemical investigation of cellobiose dehydrogenase from new fungal sources on Au electrodes
    • Stoica, L.; Dimcheva, N.; Haltrich, D.; Ruzgas, T.; Gorton, L. Electrochemical investigation of cellobiose dehydrogenase from new fungal sources on Au electrodes Biosens. Bioelectron. 2005, 20 (10) 2010-2018
    • (2005) Biosens. Bioelectron. , vol.20 , Issue.10 , pp. 2010-2018
    • Stoica, L.1    Dimcheva, N.2    Haltrich, D.3    Ruzgas, T.4    Gorton, L.5
  • 24
    • 39649094088 scopus 로고    scopus 로고
    • Investigation of electron transfer between cellobiose dehydrogenase from Myriococcum thermophilum and gold electrodes
    • Coman, V.; Harreither, W.; Ludwig, R.; Haltrich, D.; Gorton, L. Investigation of electron transfer between cellobiose dehydrogenase from Myriococcum thermophilum and gold electrodes Chem. Anal. (Warsaw) 2007, 52 (6) 945-960
    • (2007) Chem. Anal. (Warsaw) , vol.52 , Issue.6 , pp. 945-960
    • Coman, V.1    Harreither, W.2    Ludwig, R.3    Haltrich, D.4    Gorton, L.5
  • 26
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg, B. M.; Henriksson, G.; Pettersson, G.; Divne, C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase J. Mol. Biol. 2002, 315 (3) 421-434
    • (2002) J. Mol. Biol. , vol.315 , Issue.3 , pp. 421-434
    • Hallberg, B.M.1    Henriksson, G.2    Pettersson, G.3    Divne, C.4
  • 27
    • 0034650750 scopus 로고    scopus 로고
    • A new scaffold for binding heme in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg, B. M.; Bergfors, T.; Backbro, K.; Pettersson, G.; Henriksson, G.; Divne, C. A new scaffold for binding heme in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase Structure 2000, 8 (1) 79-88
    • (2000) Structure , vol.8 , Issue.1 , pp. 79-88
    • Hallberg, B.M.1    Bergfors, T.2    Backbro, K.3    Pettersson, G.4    Henriksson, G.5    Divne, C.6
  • 28
    • 0035465380 scopus 로고    scopus 로고
    • Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris
    • Yoshida, M.; Ohira, T.; Igarashi, K.; Nagasawa, H.; Aida, K.; Hallberg, B. M.; Divne, C.; Nishino, T.; Samejima, M. Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris Biosci. Biotechnol. Biochem. 2001, 65, 2050-2057
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2050-2057
    • Yoshida, M.1    Ohira, T.2    Igarashi, K.3    Nagasawa, H.4    Aida, K.5    Hallberg, B.M.6    Divne, C.7    Nishino, T.8    Samejima, M.9
  • 29
    • 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 (1-2) 248-254
    • (1976) Anal. Biochem. , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0003051583 scopus 로고
    • Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions
    • Frens, G. Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions Nature 1973, 241 (105) 20-22
    • (1973) Nature , vol.241 , Issue.105 , pp. 20-22
    • Frens, G.1
  • 31
    • 34250156343 scopus 로고    scopus 로고
    • Determination of size and concentration of gold nanoparticles from UV-Vis spectra
    • Haiss, W.; Thanh, N. T. K.; Aveyard, J.; Fernig, D. G. Determination of size and concentration of gold nanoparticles from UV-Vis spectra Anal. Chem. 2007, 79, 4215-4221
    • (2007) Anal. Chem. , vol.79 , pp. 4215-4221
    • Haiss, W.1    Thanh, N.T.K.2    Aveyard, J.3    Fernig, D.G.4
  • 32
    • 0021479748 scopus 로고
    • A cyclic voltammetric study of the gold-oxygen system
    • Hoare, J. P. A cyclic voltammetric study of the gold-oxygen system J. Electrochem. Soc. 1984, 131 (8) 1808-1815
    • (1984) J. Electrochem. Soc. , vol.131 , Issue.8 , pp. 1808-1815
    • Hoare, J.P.1
  • 34
    • 0346034536 scopus 로고    scopus 로고
    • Kinetics of the inter-domain electron transfer in flavocytochrome cellobiose dehydrogenase from the white-rot fungus Phanerochaete chrysosporium
    • Igarashi, K.; Momohara, I.; Nishino, T.; Samejima, M. Kinetics of the inter-domain electron transfer in flavocytochrome cellobiose dehydrogenase from the white-rot fungus Phanerochaete chrysosporium Biochem. J. 2002, 365, 521-526
    • (2002) Biochem. J. , vol.365 , pp. 521-526
    • Igarashi, K.1    Momohara, I.2    Nishino, T.3    Samejima, M.4
  • 36
    • 0037006029 scopus 로고    scopus 로고
    • STM of mixed alkylthiol self-assembled monolayers on Au(111)
    • Klein, H.; Battaglini, N.; Bellini, B.; Dumas, P. STM of mixed alkylthiol self-assembled monolayers on Au(111) Mater. Sci. Eng. C 2002, 19 (1-2) 279-283
    • (2002) Mater. Sci. Eng. C , vol.19 , Issue.1-2 , pp. 279-283
    • Klein, H.1    Battaglini, N.2    Bellini, B.3    Dumas, P.4
  • 37
    • 33845280242 scopus 로고
    • Formation of two-component surfaces by the spontaneous assembly of monolayers on gold from solutions containing mixtures of organic thiols
    • Bain, C. D.; Whitesides, G. M. Formation of two-component surfaces by the spontaneous assembly of monolayers on gold from solutions containing mixtures of organic thiols J. Am. Chem. Soc. 1988, 110 (19) 6560-6561
    • (1988) J. Am. Chem. Soc. , vol.110 , Issue.19 , pp. 6560-6561
    • Bain, C.D.1    Whitesides, G.M.2
  • 39
    • 33748804918 scopus 로고    scopus 로고
    • Binary mixtures of self-assembled monolayers of 1,8-octanedithiol and 1-octanethiol for a controlled growth of gold nanoparticles
    • Aliganga, A. K. A.; Duwez, A.-S.; Mittler, S. Binary mixtures of self-assembled monolayers of 1,8-octanedithiol and 1-octanethiol for a controlled growth of gold nanoparticles Org. Electron. 2006, 7 (5) 337-350
    • (2006) Org. Electron. , vol.7 , Issue.5 , pp. 337-350
    • Aliganga, A.K.A.1    Duwez, A.-S.2    Mittler, S.3
  • 40
    • 74249098880 scopus 로고    scopus 로고
    • A simple fabrication method for three-dimensional gold nanoparticle electrodes and their application to the study of the direct electrochemistry of cytochrome
    • Murata, K.; Kajiya, K.; Nukaga, M.; Suga, Y.; Watanabe, T.; Nakamura, N.; Ohno, H. A simple fabrication method for three-dimensional gold nanoparticle electrodes and their application to the study of the direct electrochemistry of cytochrome c. Electroanalysis 2010, 22, 185-190
    • (2010) C. Electroanalysis , vol.22 , pp. 185-190
    • Murata, K.1    Kajiya, K.2    Nukaga, M.3    Suga, Y.4    Watanabe, T.5    Nakamura, N.6    Ohno, H.7
  • 41
    • 49249148639 scopus 로고
    • General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems
    • Laviron, E. General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems J. Electroanal. Chem. Interfacial Electrochem. 1979, 101, 19-28
    • (1979) J. Electroanal. Chem. Interfacial Electrochem. , vol.101 , pp. 19-28
    • Laviron, E.1
  • 42
    • 18044398972 scopus 로고    scopus 로고
    • Self-assembled monolayers of thiolates on metals as a form of nanotechnology
    • Love, J. C.; Estroff, L. A.; Kriebel, J. K.; Nuzzo, R. G.; Whitesides, G. M. Self-assembled monolayers of thiolates on metals as a form of nanotechnology Chem. Rev. 2005, 105 (4) 1103-1170
    • (2005) Chem. Rev. , vol.105 , Issue.4 , pp. 1103-1170
    • Love, J.C.1    Estroff, L.A.2    Kriebel, J.K.3    Nuzzo, R.G.4    Whitesides, G.M.5
  • 43
    • 84860197665 scopus 로고    scopus 로고
    • Investigation of the pH-dependent electron transfer mechanism of ascomycetous class II cellobiose dehydrogenases on electrodes
    • Harreither, W.; Nicholls, P.; Sygmund, C.; Gorton, L.; Ludwig, R. Investigation of the pH-dependent electron transfer mechanism of ascomycetous class II cellobiose dehydrogenases on electrodes Langmuir 2012, 28 (16) 6714-6723
    • (2012) Langmuir , vol.28 , Issue.16 , pp. 6714-6723
    • Harreither, W.1    Nicholls, P.2    Sygmund, C.3    Gorton, L.4    Ludwig, R.5


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