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Volumn 704, Issue , 2013, Pages 67-74

Direct electrochemistry and environmental sensing of rice hemoglobin immobilized at graphite electrodes

Author keywords

Bioelectrocatalysis; Electron transfer; Heme proteins; Ligand sensing: oxygen, hydrogen peroxide, cyanide and superoxide; Rice hemoglobin

Indexed keywords

CYANIDES; ELECTRON TRANSITIONS; GRAPHITE ELECTRODES; HEMOGLOBIN; HYDROGEN PEROXIDE; PEROXIDES; PORPHYRINS; RATE CONSTANTS; REDOX REACTIONS; REDUCTION;

EID: 84880367432     PISSN: 15726657     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jelechem.2013.06.015     Document Type: Article
Times cited : (13)

References (63)
  • 1
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • DOI 10.1016/j.jinorgbio.2004.11.006, PII S0162013404003502, Heme-Diatomic Interactions, Part 1
    • M.-A. Gilles-Gonzalez, and G. Gonzalez Heme-based sensors:defining characteristics, recent developments, and regulatory hypotheses J. Inorg. Biochem. 99 2005 1 22 (Pubitemid 39642968)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 1-22
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 2
    • 0004152433 scopus 로고    scopus 로고
    • A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt, John Wiley & Sons, Ltd. Chichester
    • M. Paoli, and K. Nagai Hemoglobin A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt, Handbook of Metalloproteins 2001 John Wiley & Sons, Ltd. Chichester pp. 16-30
    • (2001) Handbook of Metalloproteins , pp. 16-30
    • Paoli, M.1    Nagai Hemoglobin, K.2
  • 3
    • 0038101540 scopus 로고    scopus 로고
    • Direct measurement of equilibrium constants for high-affinity hemoglobins
    • S. Kundu, S.A. Premer, J.A. Hoy, J.T. Trent III, and M.S. Hargrove Direct measurement of equilibrium constants for high affinity hemoglobins Biophys. J. 84 2003 3931 3940 (Pubitemid 36637888)
    • (2003) Biophysical Journal , vol.84 , Issue.6 , pp. 3931-3940
    • Kundu, S.1    Premer, S.A.2    Hoy, J.A.3    Trent III, J.T.4    Hargrove, M.S.5
  • 4
    • 0035001778 scopus 로고    scopus 로고
    • Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications
    • A.I. Alayash, P.P. Rakesh, and R.E. Cashon Redox reactions of hemoglobin and myoglobin: biological and toxicological implications Antioxid. Redox Signal. 3 2001 313 327 (Pubitemid 32473345)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.2 , pp. 313-327
    • Alayash, A.I.1    Patel, R.P.2    Cashon, R.E.3
  • 5
    • 0021989717 scopus 로고
    • Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites
    • S. Yoshikawa, D.H. O'Keeffe, and W.S. Caughey Investigations of cyanide as infrared probe of hemeprotein ligand binding sites J. Biol. Chem. 260 1985 3518 3528 (Pubitemid 15114352)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.6 , pp. 3518-3528
    • Yoshikawa, S.1    O'Keeffe, D.H.2    Caughey, W.S.3
  • 7
    • 0025201423 scopus 로고
    • A novel antioxidant role for hemoglobin
    • C. Giulivi, and K.J.A. Davies A novel antioxidant role for hemoglobin J. Biol. Chem. 265 1990 19453 19460
    • (1990) J. Biol. Chem. , vol.265 , pp. 19453-19460
    • Giulivi, C.1    Davies, K.J.A.2
  • 11
    • 79952492056 scopus 로고    scopus 로고
    • Unmediated enzyme electrodes
    • C.A. Grimes, E.C. Dickey, M.V. Pishko, American Scientific Publishers Stevenson Ranch, California, USA
    • E.E. Ferapontova Unmediated enzyme electrodes C.A. Grimes, E.C. Dickey, M.V. Pishko, Encyclopedia of Sensors vol. 10 2006 American Scientific Publishers Stevenson Ranch, California, USA 391 422
    • (2006) Encyclopedia of Sensors , vol.10 , pp. 391-422
    • Ferapontova, E.E.1
  • 12
    • 0037039595 scopus 로고    scopus 로고
    • Heme protein-clay films: Direct electrochemistry and electrochemical catalysis
    • DOI 10.1021/la010834a
    • Y. Zhou, N. Hu, Y. Zeng, and J.F. Rusling Heme protein-clay films: direct electrochemistry and electrochemical catalysis Langmuir 18 2002 211 219 (Pubitemid 35382297)
    • (2002) Langmuir , vol.18 , Issue.1 , pp. 211-219
    • Zhou, Y.1    Hu, N.2    Zeng, Y.3    Rusling, J.F.4
  • 13
    • 23744448903 scopus 로고    scopus 로고
    • Core-shell nanocluster films of hemoglobin and clay nanoparticle: Direct electrochemistry and electrocatalysis
    • DOI 10.1016/j.bpc.2005.04.010, PII S030146220500075X
    • Y. Liu, and N. Hu Core-shell nanocluster films of hemoglobin and clay nanoparticle: direct electrochemistry and electrocatalysis Biophys. Chem. 117 2005 27 37 (Pubitemid 41121979)
    • (2005) Biophysical Chemistry , vol.117 , Issue.1 , pp. 27-37
    • Liu, Y.1    Liu, H.2    Hu, N.3
  • 15
    • 4544300944 scopus 로고    scopus 로고
    • Highly sensitive voltammetric biosensor for nitric oxide based on its high affinity with hemoglobin
    • DOI 10.1016/j.aca.2004.07.038, PII S0003267004008803
    • C. Fan, X. Liu, J. Pang, G. Li, and H. Scheer Highly sensitive voltammetric biosensor for nitric oxide based on its affinity with hemoglobin Anal. Chim. Acta 523 2004 225 228 (Pubitemid 39221444)
    • (2004) Analytica Chimica Acta , vol.523 , Issue.2 , pp. 225-228
    • Fan, C.1    Liu, X.2    Pang, J.3    Li, G.4    Scheer, H.5
  • 16
    • 0030042975 scopus 로고    scopus 로고
    • Electron transfer between electrodes and heme proteins in protein-DNA films
    • DOI 10.1021/ja960065v
    • A.-E.F. Nassar, and J.F. Rusling Electron transfer between electrodes and heme proteins in protein-DNA films J. Am. Chem. Soc. 118 1996 3043 3044 (Pubitemid 3044282)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.12 , pp. 3043-3044
    • Nassar, A.E.1    Rusling, J.F.2    Nakashima, N.3
  • 17
    • 0000786392 scopus 로고    scopus 로고
    • Composite films of surfactants, nafion, and proteins with electrochemical and enzyme activity
    • Q. Huang, Z. Lu, and J.F. Rusling Composite films of surfactants nafion, and proteins with electrochemical and enzyme activity Langmuir 12 1996 5472 5480 (Pubitemid 126562251)
    • (1996) Langmuir , vol.12 , Issue.22 , pp. 5472-5480
    • Huang, Q.1    Lu, Z.2    Rusling, J.F.3
  • 18
    • 0033525321 scopus 로고    scopus 로고
    • Enhanced electron transfer fro hemoglobin in poly(ester sulfonic acid) films on pyrolytic graphite electrodes
    • J. Yang, N. Hu, and J.F. Rusling Enhanced electron transfer fro hemoglobin in poly(ester sulfonic acid) films on pyrolytic graphite electrodes J. Electroanal. Chem. 463 1999 53 62
    • (1999) J. Electroanal. Chem. , vol.463 , pp. 53-62
    • Yang, J.1    Hu, N.2    Rusling, J.F.3
  • 19
    • 35548968035 scopus 로고    scopus 로고
    • Self-assembled films of hemoglobin/laponite/chitosan: Application for the direct electrochemistry and catalysis to hydrogen peroxide
    • DOI 10.1021/bm070329d
    • D. Shan, E. Han, H. Xue, and S. Cosnier Self-assembled films of hemoglobin/laponite/chitosan: application forthe direct electrochemistry and catalysis to hydrogen peroxide Biomacromolecules 8 2007 3041 3046 (Pubitemid 350011623)
    • (2007) Biomacromolecules , vol.8 , Issue.10 , pp. 3041-3046
    • Shan, D.1    Han, E.2    Xue, H.3    Cosnier, S.4
  • 23
    • 2042456719 scopus 로고    scopus 로고
    • Recombinant horseradish peroxidase- and cytochrome c-based two-electrode system for detection of superoxide radicals
    • DOI 10.1016/j.bioelechem.2003.09.026, PII S1567539404000490
    • S. Shipovskov, E.E. Ferapontova, I. Gazaryan, and T. Ruzgas Recombinant horseradish peroxidase- and cytochrome c-based two-electrode system for detection of superoxide radicals Bioelectrochem. 63 2004 277 280 (Pubitemid 38534234)
    • (2004) Bioelectrochemistry , vol.63 , Issue.1-2 , pp. 277-280
    • Shipovskov, S.1    Ferapontova, E.E.2    Gazaryan, I.3    Ruzgas, T.4
  • 24
    • 33847103553 scopus 로고    scopus 로고
    • Direct electron transfer kinetics in horseradish peroxidase electrocatalysis
    • DOI 10.1021/jp064277i
    • R. Andrue, E.E. Ferapontova, L. Gorton, and J.J. Calvente Direct electron transfer kinetics in horseradish peroxidase electrocatalysis J. Phys. Chem. B 111 2007 469 477 (Pubitemid 46278978)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.2 , pp. 469-477
    • Andreu, R.1    Ferapontova, E.E.2    Gorton, L.3    Calvente, J.J.4
  • 26
    • 0036148207 scopus 로고    scopus 로고
    • Adsorption of differently charged forms of horseradish peroxidase on metal electrodes of different nature: Effect of surface charges
    • DOI 10.1016/S1567-5394(01)00155-4, PII S1567539401001554
    • E. Ferapontova, and E. Dominguez Adsorption of differently charged forms of horseradish peroxidase on metal electrodes of different nature: effect of surface charges Bioelectrochem. 55 2002 127 130 (Pubitemid 34084766)
    • (2002) Bioelectrochemistry , vol.55 , Issue.1-2 , pp. 127-130
    • Ferapontova, E.1    Dominguez, E.2
  • 27
    • 0037997920 scopus 로고    scopus 로고
    • 2 with different forms of horseradish peroxidase directly adsorbed at polycrystalline silver and gold
    • 2 with different forms of horseradish peroxidase directly adsorbed at polycrystalline silver and gold Electroanalysis 15 2003 484 491
    • (2003) Electroanalysis , vol.15 , pp. 484-491
    • Ferapontova, E.1    Gorton, L.2
  • 29
    • 84880349344 scopus 로고
    • A redetermination of the oxidation potential of the hemoglobin- methemoglobin system
    • J.B. Conant, and A.M. Pappenheimer A redetermination of the oxidation potential of the hemoglobin-methemoglobin system J. Biol. Chem. 98 1932 57 62
    • (1932) J. Biol. Chem. , vol.98 , pp. 57-62
    • Conant, J.B.1    Pappenheimer, A.M.2
  • 30
    • 0000287214 scopus 로고
    • Oxidation-reduction potentials of the methemoglobin-hemoglobin system
    • J.F. Taylor, and A.B. Hastings Oxidation-reduction potentials of the methemoglobin-hemoglobin system J. Biol. Chem. 131 1939 649 662
    • (1939) J. Biol. Chem. , vol.131 , pp. 649-662
    • Taylor, J.F.1    Hastings, A.B.2
  • 31
    • 0017840540 scopus 로고
    • Oxidation-reduction reactions of hemoglobin A, hemoglobin M Iwate, and hemoglobin M Hyde Park
    • T. Yamada, C.P. Marini, and J.C. Cassatt Oxidation-reduction reactions of hemoglobin A, hemoglobin M Iwate and hemoglobine M hyde park Biochem. 17 1978 231 236 (Pubitemid 8270206)
    • (1978) Biochemistry , vol.17 , Issue.2 , pp. 231-236
    • Yamada, T.1    Marini, C.P.2    Cassatt, J.C.3
  • 32
    • 0141482219 scopus 로고    scopus 로고
    • Direct electron transfer of heme- and molybdopterin cofactor-containing chicken liver sulfite oxidase on alkanethiol-modified gold electrodes
    • DOI 10.1021/ac0341923
    • E.E. Ferapontova, T. Ruzgas, and L. Gorton Direct electron transfer of heme- and molybdopterin cofactor-containing chicken liver sulfite oxidase on alkanethiol-modified gold electrodes Anal. Chem. 75 2003 4841 4850 (Pubitemid 37139786)
    • (2003) Analytical Chemistry , vol.75 , Issue.18 , pp. 4841-4850
    • Ferapontova, E.E.1    Ruzgas, T.2    Gorton, L.3
  • 34
    • 0036832946 scopus 로고    scopus 로고
    • Effect of pH on direct electron transfer between graphite and horseradish peroxidase
    • DOI 10.1016/S0022-0728(01)00692-1, PII S0022072801006921
    • E. Ferapontova, and E. Puganova Effect of pH on direct electron transfer between graphite and horseradish peroxidase J. Electroanal. Chem. 518 2002 20 26 (Pubitemid 33142221)
    • (2002) Journal of Electroanalytical Chemistry , vol.518 , Issue.1 , pp. 20-26
    • Ferapontova, E.1    Puganova, E.2
  • 35
    • 0000311733 scopus 로고
    • Electrochemical stability of catechols with a pyrene side chain strongly adsorbed on graphite electrodes for catalytic oxidation of dihydronicotinamide adenine dinucleotide
    • H. Jaegfeldt, T. Kuwana, and G. Johansson Electrochemical stability of catechols with a pyrene side chain strongly adsorbed on graphite electrodes for catalytic oxidation of dihydronicotinamide adenine dinucleotide J. Am. Chem. Soc. 105 1983 1805 1814
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 1805-1814
    • Jaegfeldt, H.1    Kuwana, T.2    Johansson, G.3
  • 37
    • 0028969560 scopus 로고
    • Kinetic measurements of a surface confined redox reaction
    • S. Komorsky-Lovric, and M. Lovric Kinetic measurements of a surface confined redox reaction Anal. Chim. Acta 305 1995 248 255
    • (1995) Anal. Chim. Acta , vol.305 , pp. 248-255
    • Komorsky-Lovric, S.1    Lovric, M.2
  • 39
    • 84880346429 scopus 로고    scopus 로고
    • 2 reduction by Streptomyces coelicolor laccase orientated at promoter-modified graphite electrodes
    • 10.1002/cphc.201300069
    • 2 reduction by Streptomyces coelicolor laccase orientated at promoter-modified graphite electrodes ChemPhysChem 2013 10.1002/cphc.201300069
    • (2013) ChemPhysChem
    • Lörcher, S.1    Lopes, P.2    Kartashov, A.3    Ferapontova, E.E.4
  • 40
    • 4544231695 scopus 로고    scopus 로고
    • Direct peroxidase bioelectrocatalysis on a variety of electrode materials
    • E.E. Ferapontova Direct peroxidase bioelectrocatalysis on a variety of electrode materials Electroanalysis 16 2004 1101 1112
    • (2004) Electroanalysis , vol.16 , pp. 1101-1112
    • Ferapontova, E.E.1
  • 42
    • 17144423192 scopus 로고    scopus 로고
    • Autoxidation studies of extracellular hemoglobin of Glossoscolex paulistus at pH 9: Cyanide and hydroxyl effect
    • DOI 10.1016/j.bpc.2004.12.041
    • A.L. Poli, L.M. Moreira, and H.A. Imasato Autooxidation studies of extracellular hemoglobin of Glossoscolex paulistus at pH 9: cyanide and hydroxyl effect Biophys. Chem. 114 2005 253 260 (Pubitemid 40521523)
    • (2005) Biophysical Chemistry , vol.114 , Issue.2-3 , pp. 253-260
    • Poli, A.L.1    Moreira, L.M.2    Hidalgo, A.A.3    Imasato, H.4
  • 43
    • 79960126950 scopus 로고    scopus 로고
    • Amperometric flow-biosensor for cyanide based on an inhibitory effect upon bioelectrocatalytic reduction of oxygen by peroxidase-modified carbon-felt
    • Y. Wang, and Y. Hasebe Amperometric flow-biosensor for cyanide based on an inhibitory effect upon bioelectrocatalytic reduction of oxygen by peroxidase-modified carbon-felt Electroanalysis 23 2011 1631 1637
    • (2011) Electroanalysis , vol.23 , pp. 1631-1637
    • Wang, Y.1    Hasebe, Y.2
  • 44
    • 0000190062 scopus 로고    scopus 로고
    • Development of a Sol-Gel Enzyme Inhibition-Based Amperometric Biosensor for Cyanide
    • T.M. Park, E.I. Iwuoha, and M.R. Smyth Development of a sol-gel enzyme inhibition-based amperometric biosensor for cyanide Electroanalysis 9 1997 1120 1123 (Pubitemid 127441373)
    • (1997) Electroanalysis , vol.9 , Issue.14 , pp. 1120-1123
    • Park, T.-M.1    Iwuoha, E.I.2    Smyth, M.R.3
  • 45
    • 0030250377 scopus 로고    scopus 로고
    • Mediator-free amperometric determination of toxic substances based on their inhibition of immobilized horseradish peroxidase
    • DOI 10.1021/bp960056q
    • J. Zhao, R.W. Henkens, and A.L. Crumbliss Mediator-free amperometric determination of toxic substances based on their inhibition of immobilized horseradish peroxidase Biotechnol. Prog. 12 1996 703 708 (Pubitemid 26368074)
    • (1996) Biotechnology Progress , vol.12 , Issue.5 , pp. 703-708
    • Zhao, J.1    Henkens, R.W.2    Crumbliss, A.L.3
  • 46
    • 0025708773 scopus 로고
    • Cyanide detection using a substrate-regenerating peroxidase-based biosensor
    • M.H. Smit, and A.E.G. Cass Cyanide detection using a substrate- regenerating peroxidase-based biosensor Anal. Chem. 62 1990 2429 2436
    • (1990) Anal. Chem. , vol.62 , pp. 2429-2436
    • Smit, M.H.1    Cass, A.E.G.2
  • 47
    • 0001436026 scopus 로고    scopus 로고
    • 2-generating peroxidase electrodes as reagentless cyanide sensors
    • 2-generating peroxidase electrodes as reagentless cyanide sensors Anal. Chem. 68 1996 1612 1615
    • (1996) Anal. Chem. , vol.68 , pp. 1612-1615
    • Tatsuma, T.1    Oyama, N.2
  • 48
    • 0001185725 scopus 로고
    • Determination of cyanide using a tyrosinase amperometric biosensor with catechol as substrate
    • X.Y. Hu, and Z.Z. Leng Determination of cyanide using a tyrosinase amperometric biosensor with catechol as substrate Analyst 120 1995 1555 1557
    • (1995) Analyst , vol.120 , pp. 1555-1557
    • Hu, X.Y.1    Leng, Z.Z.2
  • 49
    • 0027916875 scopus 로고
    • Toxin detection using a tyrosinase-coupled oxygen electrode
    • M.H. Smit, and G.A. Rechnitz Toxin detection using a tyrosinase-coupled oxygen electrode Anal. Chem. 65 1993 380 385
    • (1993) Anal. Chem. , vol.65 , pp. 380-385
    • Smit, M.H.1    Rechnitz, G.A.2
  • 50
    • 0029079947 scopus 로고
    • A biosensor as warning device for the detection of cyanide, chlorophenols, atrazine and carbamate pesticides
    • J.-L. Besombes, S. Cosnier, P. Labbac, and G. Reverdy A biosensor as warning device for the detection of cyanide, chlorophenols, atrazine and carbamate pesticides Anal. Chim. Acta 311 1995 255 263
    • (1995) Anal. Chim. Acta , vol.311 , pp. 255-263
    • Besombes, J.-L.1    Cosnier, S.2    Labbac, P.3    Reverdy, G.4
  • 51
    • 0000586315 scopus 로고    scopus 로고
    • Renewable-reagent enzyme inhibition sensor for remote monitoring of cyanide
    • J. Wang, B. Tian, J. Lu, D. MacDonald, J. Wang, and D. Luo Renewable-reagent enzyme inhibition sensor for remote monitoring of cyanide Electroanalysis 10 1998 1034 1037 (Pubitemid 128441167)
    • (1998) Electroanalysis , vol.10 , Issue.15 , pp. 1034-1037
    • Wang, J.1    Tian, B.2    Lu, J.3    MacDonald, D.4    Wang, J.5    Luo, D.6
  • 52
    • 0347361592 scopus 로고    scopus 로고
    • Subnanomolar cyanide detection at polyphenol oxidase/clay biosensors
    • DOI 10.1021/ac034713m
    • D. Shan, C. Mousty, and S. Cosnier Subnanomolar cyanide detection at polyphenol oxidase/clay biosensors Anal. Chem. 76 2004 178 183 (Pubitemid 38040648)
    • (2004) Analytical Chemistry , vol.76 , Issue.1 , pp. 178-183
    • Shan, D.1    Mousty, C.2    Cosnier, S.3
  • 53
    • 0035918528 scopus 로고    scopus 로고
    • A model for ligand binding to hexacoordinate hemoglobins
    • DOI 10.1021/bi0100790
    • J.T. Trent, A.N. Hvitved, and M.S. Hargrove A model for ligand binding to hexacoordinate hemoglobins Biochemistry 40 2001 6155 6163 (Pubitemid 32466320)
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6155-6163
    • Trent III, J.T.1    Hvitved, A.N.2    Hargrove, M.S.3
  • 55
    • 33748392625 scopus 로고
    • Free radical produced in the reaction of metmyoglobin with hydrogen peroxide
    • J.F. Gibson, D.J.E. Ingram, and P. Nicholls Free radical produced in the reaction of metmyoglobin with hydrogen peroxide Nature 181 1958 1398 1399
    • (1958) Nature , vol.181 , pp. 1398-1399
    • Gibson, J.F.1    Ingram, D.J.E.2    Nicholls, P.3
  • 56
    • 0000952295 scopus 로고
    • The mechanism of methmyoglobin oxidation
    • N. Kelso King, and M.E. Winfieled The mechanism of methmyoglobin oxidation J. Biol. Chem. 238 1963 1520 1528
    • (1963) J. Biol. Chem. , vol.238 , pp. 1520-1528
    • Kelso King, N.1    Winfieled, M.E.2
  • 57
    • 72149101608 scopus 로고    scopus 로고
    • Analysis of peroxidase activity of rice (Oryza sativa) recombinant hemoglobin 1: Implications for in vivo function of hexacoordinate non-symbiotic hemoglobins in plants
    • F. Violante-Mota, E. Tellechea, J.F. Moran, G. Sarath, and R. Arredondo-Peter Analysis of peroxidase activity of rice (Oryza sativa) recombinant hemoglobin 1: implications for in vivo function of hexacoordinate non-symbiotic hemoglobins in plants Phytochemistry 71 2010 21 26
    • (2010) Phytochemistry , vol.71 , pp. 21-26
    • Violante-Mota, F.1    Tellechea, E.2    Moran, J.F.3    Sarath, G.4    Arredondo-Peter, R.5
  • 59
    • 0034564686 scopus 로고    scopus 로고
    • Analysis of individual biochemical events based on artificial synapses using ultramicroelectrodes: Cellular oxidative burst
    • C. Amatore, S. Arbault, D. Bruce, P. de Oliveira, M. Erard, and M. Vuillaume Analysis of individual biochemical events based on artificial synapses using ultramicroelectrodes: cellular oxidative burst Faraday Discuss. 116 2000 319 333
    • (2000) Faraday Discuss. , vol.116 , pp. 319-333
    • Amatore, C.1    Arbault, S.2    Bruce, D.3    De Oliveira, P.4    Erard, M.5    Vuillaume, M.6
  • 60
    • 0001721490 scopus 로고
    • Electrochemical generation and reactivity of the superoxide ion in aqueous solutions
    • J. Divisek, and B. Kastening Electrochemical generation and reactivity of the superoxide ion in aqueous solutions J. Electroanal. Chem. 65 1975 603 621
    • (1975) J. Electroanal. Chem. , vol.65 , pp. 603-621
    • Divisek, J.1    Kastening, B.2
  • 61
    • 0033119689 scopus 로고    scopus 로고
    • Superoxide dismutase activity measurement using cytochrome c-modified electrode
    • DOI 10.1021/ac980961k
    • F. Lisdat, B. Ge, E. Ehrentreich-Förster, R. Reszka, and F.W. Scheller Superoxide dismutase activity measurement using cytochrome c-modified electrode Anal. Chem. 71 1999 1359 1365 (Pubitemid 29177294)
    • (1999) Analytical Chemistry , vol.71 , Issue.7 , pp. 1359-1365
    • Lisdat, F.1    Ge, B.2    Ehrentreich-Forster, E.3    Reszka, R.4    Scheller, F.W.5
  • 63
    • 0037017693 scopus 로고    scopus 로고
    • Superoxide sensor based on cytochrome c immobilized on mixed-thiol SAM with a new calibration method
    • DOI 10.1016/S0003-2670(01)01545-8, PII S0003267001015458
    • B. Ge, and F. Lisdat Superoxide sensor based on cytochrome c immobilized on mixed-thiol SAM with a new calibration method Anal. Chim. Acta 454 2002 53 64 (Pubitemid 34159194)
    • (2002) Analytica Chimica Acta , vol.454 , Issue.1 , pp. 53-64
    • Ge, B.1    Lisdat, F.2


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