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Volumn 78, Issue 2, 2010, Pages 124-129

Carbon nanotube-hydroxyapatite-hemoglobin nanocomposites with high bioelectrocatalytic activity

Author keywords

Bioelectrochemistry; Direct electron transfer; Electrocatalysis; Hemoglobin; MWCNTs HA

Indexed keywords

AMPEROMETRIC RESPONSE; BIOELECTROCATALYTIC ACTIVITY; BIOELECTROCHEMISTRY; CATALYTIC REACTIVITY; DETECTION LIMITS; DIRECT ELECTRON TRANSFER; ELECTROCHEMICAL REDUCTIONS; FTIR SPECTROSCOPY; HETEROGENEOUS ELECTRON TRANSFER RATE CONSTANT; NATIVE CONFORMATION; SELF-ASSEMBLING; SEM; SURFACE COVERAGES; TRICHLOROACETIC ACID;

EID: 77949571253     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2009.08.009     Document Type: Article
Times cited : (34)

References (38)
  • 1
    • 0023440175 scopus 로고
    • Direct electron transfer reactions of cytochrome c at silver electrodes
    • Reed D.E., and Hawkridge F.M. Direct electron transfer reactions of cytochrome c at silver electrodes. Anal. Chem. 59 (1987) 2334-2339
    • (1987) Anal. Chem. , vol.59 , pp. 2334-2339
    • Reed, D.E.1    Hawkridge, F.M.2
  • 2
    • 0024289078 scopus 로고
    • Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue
    • Ye J., and Baldwin R.P. Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue. Anal. Chem. 60 (1988) 2263-2268
    • (1988) Anal. Chem. , vol.60 , pp. 2263-2268
    • Ye, J.1    Baldwin, R.P.2
  • 3
    • 0000929629 scopus 로고    scopus 로고
    • Enzyme bioelectrochemistry in cast biomembrane-like films
    • Rusling J.F. Enzyme bioelectrochemistry in cast biomembrane-like films. Acc. Chem. Res. 31 (1998) 363-369
    • (1998) Acc. Chem. Res. , vol.31 , pp. 363-369
    • Rusling, J.F.1
  • 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., and Gazaryan I. Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors. Anal. Chim. Acta 400 (1999) 91-108
    • (1999) Anal. Chim. Acta , vol.400 , pp. 91-108
    • Gorton, L.1    Lindgren, A.2    Larsson, T.3    Munteanu, F.D.4    Ruzgas, T.5    Gazaryan, I.6
  • 5
    • 33846828295 scopus 로고    scopus 로고
    • Direct electrochemical response of myoglobin using a room temperature ionic liquid, 1-(2-hydroxyethyl)-3-methyl imidazolium tetrafluoroborate, as supporting electrolyte
    • Ding S., Xu M., Zhao G., and Wei X. Direct electrochemical response of myoglobin using a room temperature ionic liquid, 1-(2-hydroxyethyl)-3-methyl imidazolium tetrafluoroborate, as supporting electrolyte. Electrochem. Commun. 9 (2007) 216-220
    • (2007) Electrochem. Commun. , vol.9 , pp. 216-220
    • Ding, S.1    Xu, M.2    Zhao, G.3    Wei, X.4
  • 7
    • 62649086047 scopus 로고    scopus 로고
    • Bioelectrochemistry of hemoglobin immobilized on a sodium alginate-multi wall carbon nanotubes composite film
    • Zhao H.Y., Zheng W., Meng Z.X., Zhou H.M., Xu X.X., Li Z., and Zheng Y.F. Bioelectrochemistry of hemoglobin immobilized on a sodium alginate-multi wall carbon nanotubes composite film. Biosens. Bioelectron. 24 (2009) 2352-2357
    • (2009) Biosens. Bioelectron. , vol.24 , pp. 2352-2357
    • Zhao, H.Y.1    Zheng, W.2    Meng, Z.X.3    Zhou, H.M.4    Xu, X.X.5    Li, Z.6    Zheng, Y.F.7
  • 8
    • 0000234036 scopus 로고
    • Direct electron transfer of horse heart myoglobin at an indium oxide electrode
    • Taniguchi I., Watanabe K., Tominaga M., and Hawkridge F.M. Direct electron transfer of horse heart myoglobin at an indium oxide electrode. J. Electroanal. Chem. 333 (1992) 331-338
    • (1992) J. Electroanal. Chem. , vol.333 , pp. 331-338
    • Taniguchi, I.1    Watanabe, K.2    Tominaga, M.3    Hawkridge, F.M.4
  • 9
    • 26444547158 scopus 로고    scopus 로고
    • Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids
    • Wang S.F., Chen T., Zhang Z.L., Shen X.C., Lu Z.X., Pang D.W., and Wong K.Y. Direct electrochemistry and electrocatalysis of heme proteins entrapped in agarose hydrogel films in room-temperature ionic liquids. Langmuir 21 (2005) 9260-9266
    • (2005) Langmuir , vol.21 , pp. 9260-9266
    • Wang, S.F.1    Chen, T.2    Zhang, Z.L.3    Shen, X.C.4    Lu, Z.X.5    Pang, D.W.6    Wong, K.Y.7
  • 10
    • 33846391922 scopus 로고    scopus 로고
    • Hemoglobin niobate composite based biosensor for efficient determination of hydrogen peroxide in a broad pH range
    • Gao L., and Gao Q. Hemoglobin niobate composite based biosensor for efficient determination of hydrogen peroxide in a broad pH range. Biosens. Bioelectron. 22 (2007) 1454-1460
    • (2007) Biosens. Bioelectron. , vol.22 , pp. 1454-1460
    • Gao, L.1    Gao, Q.2
  • 11
    • 34250174469 scopus 로고    scopus 로고
    • Gelatin-functionalized carbon nanotubes for the bioelectrochemistry of hemoglobin
    • Zheng W., and Zheng Y.F. Gelatin-functionalized carbon nanotubes for the bioelectrochemistry of hemoglobin. Electrochem. Commun. 9 (2007) 1619-1623
    • (2007) Electrochem. Commun. , vol.9 , pp. 1619-1623
    • Zheng, W.1    Zheng, Y.F.2
  • 12
    • 41549143208 scopus 로고    scopus 로고
    • An amperometic biosensor based on hemoglobin immobilized in poly(ε-caprolactone) film and its application
    • Zheng W., Li J., and Zheng Y.F. An amperometic biosensor based on hemoglobin immobilized in poly(ε-caprolactone) film and its application. Biosens. Bioelectron. 23 (2008) 1562-1566
    • (2008) Biosens. Bioelectron. , vol.23 , pp. 1562-1566
    • Zheng, W.1    Li, J.2    Zheng, Y.F.3
  • 13
    • 22444443916 scopus 로고    scopus 로고
    • Bioelectrochemically functional nanohybrids through co-assembling of proteins and surfactants onto carbon nanotubes: facilitated electron transfer of assembled proteins with enhanced faradic response
    • Yan Y., Zheng W., Zhang M., Wang L., Su L., and Mao L. Bioelectrochemically functional nanohybrids through co-assembling of proteins and surfactants onto carbon nanotubes: facilitated electron transfer of assembled proteins with enhanced faradic response. Langmuir 21 (2005) 6560-6566
    • (2005) Langmuir , vol.21 , pp. 6560-6566
    • Yan, Y.1    Zheng, W.2    Zhang, M.3    Wang, L.4    Su, L.5    Mao, L.6
  • 14
    • 26444597028 scopus 로고    scopus 로고
    • Molecular films of water-miscible ionic liquids formed onto glassy carbon electrode: characterization and electrochemical applications
    • Yu P., Lin Y., Xiang L., Su L., Zhang J., and Mao L. Molecular films of water-miscible ionic liquids formed onto glassy carbon electrode: characterization and electrochemical applications. Langmuir 21 (2005) 9000-9006
    • (2005) Langmuir , vol.21 , pp. 9000-9006
    • Yu, P.1    Lin, Y.2    Xiang, L.3    Su, L.4    Zhang, J.5    Mao, L.6
  • 15
    • 0242469044 scopus 로고    scopus 로고
    • Direct electrochemistry of horseradish peroxidase bonded on a conducting polymer modified glassy carbon electrode
    • Kong Y., Boopathi M., and Shim Y. Direct electrochemistry of horseradish peroxidase bonded on a conducting polymer modified glassy carbon electrode. Biosens. Bioelectron. 19 (2003) 227-232
    • (2003) Biosens. Bioelectron. , vol.19 , pp. 227-232
    • Kong, Y.1    Boopathi, M.2    Shim, Y.3
  • 16
    • 0025366526 scopus 로고
    • Cross-linked redox gels containing glucose oxidase for amperometric biosensor applications
    • Gregg B.A., and Heller A. Cross-linked redox gels containing glucose oxidase for amperometric biosensor applications. Anal. Chem. 62 (1990) 258-263
    • (1990) Anal. Chem. , vol.62 , pp. 258-263
    • Gregg, B.A.1    Heller, A.2
  • 17
    • 39749123171 scopus 로고    scopus 로고
    • Self-assembly of electroactive layer-by-layer films of heme proteins with anionic surfactant dihexadecyl phosphate
    • Shan W., Liu H., Shi J., Yang L., and Hu N. Self-assembly of electroactive layer-by-layer films of heme proteins with anionic surfactant dihexadecyl phosphate. Biophys. Chem. 134 (2008) 101-109
    • (2008) Biophys. Chem. , vol.134 , pp. 101-109
    • Shan, W.1    Liu, H.2    Shi, J.3    Yang, L.4    Hu, N.5
  • 18
    • 34547538271 scopus 로고    scopus 로고
    • Assembly of layer-by-layer films of electroactive hemoglobin and surfactant didodecyldimethylammonium bromide
    • Hu Y., Sun H., and Hu N. Assembly of layer-by-layer films of electroactive hemoglobin and surfactant didodecyldimethylammonium bromide. J. Colloid Interface Sci. 314 (2007) 131-140
    • (2007) J. Colloid Interface Sci. , vol.314 , pp. 131-140
    • Hu, Y.1    Sun, H.2    Hu, N.3
  • 19
    • 29144446184 scopus 로고    scopus 로고
    • Electrochemistry and electroanalytical applications of carbon nanotubes: a review
    • Gong K., Yan Y., Zhang M., Xiong S., and Mao L. Electrochemistry and electroanalytical applications of carbon nanotubes: a review. Anal. Sci. 21 (2005) 1383-1393
    • (2005) Anal. Sci. , vol.21 , pp. 1383-1393
    • Gong, K.1    Yan, Y.2    Zhang, M.3    Xiong, S.4    Mao, L.5
  • 21
    • 0037419878 scopus 로고    scopus 로고
    • Solvent-free functionalization of carbon nanotubes
    • Dyke C.A., and Tour J.M. Solvent-free functionalization of carbon nanotubes. J. Am. Chem. Soc. 125 (2003) 1156-1157
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1156-1157
    • Dyke, C.A.1    Tour, J.M.2
  • 22
    • 0141516670 scopus 로고    scopus 로고
    • Sidewall amino-fuctionalization of single-walled carbon nanotubes through fluorination and subsequent reactions with terminal diamines
    • Stevens J.L., Huang A.Y., Peng H., Chian I.W., Khabashesku V.N., and Margrave J.L. Sidewall amino-fuctionalization of single-walled carbon nanotubes through fluorination and subsequent reactions with terminal diamines. Nano Lett. 3 (2003) 331-336
    • (2003) Nano Lett. , vol.3 , pp. 331-336
    • Stevens, J.L.1    Huang, A.Y.2    Peng, H.3    Chian, I.W.4    Khabashesku, V.N.5    Margrave, J.L.6
  • 24
    • 38049035804 scopus 로고    scopus 로고
    • Improved biological characteristics of poly(L-lactic acid) electrospun membrane by incorporation of multiwalled carbon nanotubes/hydroxyapatite nanoparticles
    • Mei F., Zhong J., Yang X., Quyang X., Zhang S., Hu X., Ma Q., Lu J., Ryu S., and Deng X. Improved biological characteristics of poly(L-lactic acid) electrospun membrane by incorporation of multiwalled carbon nanotubes/hydroxyapatite nanoparticles. Biomacromolecules 8 (2007) 3729-3735
    • (2007) Biomacromolecules , vol.8 , pp. 3729-3735
    • Mei, F.1    Zhong, J.2    Yang, X.3    Quyang, X.4    Zhang, S.5    Hu, X.6    Ma, Q.7    Lu, J.8    Ryu, S.9    Deng, X.10
  • 25
    • 34548539020 scopus 로고    scopus 로고
    • Tribological behavior of plasma-sprayed carbon nanotube-reinforced hydroxyapatite coating in physiological solution
    • Balani K., Chen Y., Harimkar S.P., Dahotre N.B., and Agarwal A. Tribological behavior of plasma-sprayed carbon nanotube-reinforced hydroxyapatite coating in physiological solution. Acta Biomater. 3 (2007) 944-951
    • (2007) Acta Biomater. , vol.3 , pp. 944-951
    • Balani, K.1    Chen, Y.2    Harimkar, S.P.3    Dahotre, N.B.4    Agarwal, A.5
  • 27
    • 0043238138 scopus 로고    scopus 로고
    • Functionalization of carbon nanotubes with amphiphilic molecules and their Langmuir-Blodgett films
    • Feng L., Li H., Li F., Shi Z., and Gu Z. Functionalization of carbon nanotubes with amphiphilic molecules and their Langmuir-Blodgett films. Carbon 41 (2003) 2385-2391
    • (2003) Carbon , vol.41 , pp. 2385-2391
    • Feng, L.1    Li, H.2    Li, F.3    Shi, Z.4    Gu, Z.5
  • 28
    • 40949158467 scopus 로고    scopus 로고
    • Exfoliated single-walled carbon nanotube-based hydrogen sensor
    • Kumar M.K., Reddy A.L.M., and Ramaprabhu S. Exfoliated single-walled carbon nanotube-based hydrogen sensor. Sens. Actuators, B, Chem. 130 (2008) 653-660
    • (2008) Sens. Actuators, B, Chem. , vol.130 , pp. 653-660
    • Kumar, M.K.1    Reddy, A.L.M.2    Ramaprabhu, S.3
  • 29
    • 34548201028 scopus 로고
    • X-ray and infrared studies of lead apatites
    • Bhatnagar V.M. X-ray and infrared studies of lead apatites. Can. J. Chem. 49 (1971) 662-663
    • (1971) Can. J. Chem. , vol.49 , pp. 662-663
    • Bhatnagar, V.M.1
  • 31
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: a method for resolving intrinsically overlapped bands
    • Kauppinen J.K., Moffate D.J., Mantsch H.H., and Lameron D.G. Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Appl. Spectrosc. 35 (1981) 271-276
    • (1981) Appl. Spectrosc. , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffate, D.J.2    Mantsch, H.H.3    Lameron, D.G.4
  • 32
    • 0000668320 scopus 로고
    • Spectrophotometric, magnetic and titrimetrie studies on the heme-linked groups in myoglobin
    • Theorell H., and Ehrenberg A. Spectrophotometric, magnetic and titrimetrie studies on the heme-linked groups in myoglobin. Acta Chem. Scand. 5 (1951) 823-848
    • (1951) Acta Chem. Scand. , vol.5 , pp. 823-848
    • Theorell, H.1    Ehrenberg, A.2
  • 33
    • 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. 61 (1979) 19-28
    • (1979) J. Electroanal. Chem. , vol.61 , pp. 19-28
    • Laviron, E.1
  • 34
    • 42649129343 scopus 로고    scopus 로고
    • Direct electrochemistry and enzymatic activity of hemoglobin immobilized in ordered mesoporous titanium oxide matrix
    • Jia N., Wen Y., Yang G., Lian Q., Xu C., and Shen H. Direct electrochemistry and enzymatic activity of hemoglobin immobilized in ordered mesoporous titanium oxide matrix. Electrochem. Commun. 10 (2008) 774-777
    • (2008) Electrochem. Commun. , vol.10 , pp. 774-777
    • Jia, N.1    Wen, Y.2    Yang, G.3    Lian, Q.4    Xu, C.5    Shen, H.6
  • 35
    • 35748935084 scopus 로고    scopus 로고
    • Accelerated direct electrochemistry of hemoglobin based on hemoglobin-carbon nanotube (Hb-CNT) assembly
    • Zhang R., Wang X., and Shiu K. Accelerated direct electrochemistry of hemoglobin based on hemoglobin-carbon nanotube (Hb-CNT) assembly. J. Colloid Interface Sci. 316 (2007) 517-522
    • (2007) J. Colloid Interface Sci. , vol.316 , pp. 517-522
    • Zhang, R.1    Wang, X.2    Shiu, K.3
  • 36
    • 0042890314 scopus 로고    scopus 로고
    • Direct electrochemisty and nitric oxide interaction of heme proteins adsorbed on nanocrystalline tin oxide electrodes
    • Topoglidis E., Astuti Y., Duriaux F., Gratzel M., and Durrant J.R. Direct electrochemisty and nitric oxide interaction of heme proteins adsorbed on nanocrystalline tin oxide electrodes. Langmuir 19 (2003) 6894-6900
    • (2003) Langmuir , vol.19 , pp. 6894-6900
    • Topoglidis, E.1    Astuti, Y.2    Duriaux, F.3    Gratzel, M.4    Durrant, J.R.5
  • 37
    • 0019035135 scopus 로고
    • Rotating ring-disk enzyme electrode for biocatalysis kinetic studies and characterization of the immobilized enzyme layer
    • Kamin R.A., and Wilson G.S. Rotating ring-disk enzyme electrode for biocatalysis kinetic studies and characterization of the immobilized enzyme layer. Anal. Chem. 52 (1980) 1198-1205
    • (1980) Anal. Chem. , vol.52 , pp. 1198-1205
    • Kamin, R.A.1    Wilson, G.S.2
  • 38
    • 49749103143 scopus 로고    scopus 로고
    • Preparation of poly(L-lactide) and its application in bioelectrochemistry
    • Zheng W., Li J., and Zheng Y.F. Preparation of poly(L-lactide) and its application in bioelectrochemistry. J. Electroanal. Chem. 621 (2008) 69-74
    • (2008) J. Electroanal. Chem. , vol.621 , pp. 69-74
    • Zheng, W.1    Li, J.2    Zheng, Y.F.3


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