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Volumn 69, Issue 2, 2006, Pages 267-275

Electrochemical characterization of biosensor based on nitrite reductase and methyl viologen co-immobilized glassy carbon electrode

Author keywords

Biosensor; Co immobilization; Methyl viologen; Nitrite reductase; PAH

Indexed keywords

CO-IMMOBILIZATION; ELECTRON TRANSFER; GLASSY CARBON ELECTRODE; METHYL VIOLOGEN; NITRITE REDUCTASE;

EID: 33750008215     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2006.03.030     Document Type: Article
Times cited : (30)

References (34)
  • 2
    • 0035927760 scopus 로고    scopus 로고
    • Detection and determination of nitrate and nitrite: a review
    • Moorcroft M.J., Davis J., and Compton R.G. Detection and determination of nitrate and nitrite: a review. Talanta 54 (2001) 785-803
    • (2001) Talanta , vol.54 , pp. 785-803
    • Moorcroft, M.J.1    Davis, J.2    Compton, R.G.3
  • 5
    • 0016828220 scopus 로고
    • A novel enzyme electrode methode for the determination of nitrite based on nitrite reductase
    • Kiang C.H., Kuan S.S., and Guilbault G.G. A novel enzyme electrode methode for the determination of nitrite based on nitrite reductase. Anal. Chim. Acta 80 (1975) 209-214
    • (1975) Anal. Chim. Acta , vol.80 , pp. 209-214
    • Kiang, C.H.1    Kuan, S.S.2    Guilbault, G.G.3
  • 7
    • 0000747021 scopus 로고    scopus 로고
    • A nitrite sensor based on a highly sensitive nitrite reductase mediator-coupled amperometric detection
    • Strehlitz B., Gründig B., Schumacher W., Kronack P.M.H., Vorlop K.-D., and Kotte H. A nitrite sensor based on a highly sensitive nitrite reductase mediator-coupled amperometric detection. Anal. Chem. 68 (1996) 807-816
    • (1996) Anal. Chem. , vol.68 , pp. 807-816
    • Strehlitz, B.1    Gründig, B.2    Schumacher, W.3    Kronack, P.M.H.4    Vorlop, K.-D.5    Kotte, H.6
  • 8
    • 0031302870 scopus 로고    scopus 로고
    • A nitrite biosensor based on a maltose binding protein nitrite reductase fusion immobilized on an electropolymerized film of a pyrrole-derived bipyridinium
    • Wu Q., Storrier G.D., Pariente F., Yang Y., Shapleigh J.P., and Abruňa H.D. A nitrite biosensor based on a maltose binding protein nitrite reductase fusion immobilized on an electropolymerized film of a pyrrole-derived bipyridinium. Anal. Chem. 69 (1997) 4856-4863
    • (1997) Anal. Chem. , vol.69 , pp. 4856-4863
    • Wu, Q.1    Storrier, G.D.2    Pariente, F.3    Yang, Y.4    Shapleigh, J.P.5    Abruňa, H.D.6
  • 10
    • 0036134830 scopus 로고    scopus 로고
    • Optical biosensor based on nitrite reductase immobilized in controlled pore glass
    • Rosa C.C., Cruz H.J., Vidal M., and Oliva A.G. Optical biosensor based on nitrite reductase immobilized in controlled pore glass. Biosens. Bioelectron. 17 (2002) 45-52
    • (2002) Biosens. Bioelectron. , vol.17 , pp. 45-52
    • Rosa, C.C.1    Cruz, H.J.2    Vidal, M.3    Oliva, A.G.4
  • 11
    • 1642359212 scopus 로고    scopus 로고
    • An efficient poly(pyrrole-viologen)-nitrite reductase biosensor for the mediated detection of nitrite
    • Silva S.D., Cosnier S., Almeida M.G., and Moura J.J.G. An efficient poly(pyrrole-viologen)-nitrite reductase biosensor for the mediated detection of nitrite. Electrochem. Commun. 6 (2004) 404-408
    • (2004) Electrochem. Commun. , vol.6 , pp. 404-408
    • Silva, S.D.1    Cosnier, S.2    Almeida, M.G.3    Moura, J.J.G.4
  • 12
    • 0001076517 scopus 로고    scopus 로고
    • Dissimilatory nitrite and nitric oxide reductase
    • Averill B.A. Dissimilatory nitrite and nitric oxide reductase. Chem. Rev. 96 (1996) 2951-2964
    • (1996) Chem. Rev. , vol.96 , pp. 2951-2964
    • Averill, B.A.1
  • 13
    • 0033788756 scopus 로고    scopus 로고
    • Metal coordination and mechanism of multicopper nitrite reductase
    • Suzuki S., Kataoka K., and Yamaguchi K. Metal coordination and mechanism of multicopper nitrite reductase. Acc. Chem. Res. 33 (2000) 728-735
    • (2000) Acc. Chem. Res. , vol.33 , pp. 728-735
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3
  • 14
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • Godden J.W., Turley S., Teller D.C., Adman E.T., Liu M.Y., Payne W.J., and JeGall J. The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. Science 253 (1991) 438-442
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Payne, W.J.6    JeGall, J.7
  • 15
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction
    • Kukimoto M., Nishiyama M., Murphy M.E.P., Turley S., Adman E.T., Horinouchi S., and Beppu T. X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction. Biochemistry 33 (1994) 5246-5252
    • (1994) Biochemistry , vol.33 , pp. 5246-5252
    • Kukimoto, M.1    Nishiyama, M.2    Murphy, M.E.P.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 17
    • 0021989793 scopus 로고
    • Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaeroides forma sp. denitrificans
    • Michalski W.P., and Nicholas D.J.D. Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaeroides forma sp. denitrificans. BBA 828 (1985) 130-137
    • (1985) BBA , vol.828 , pp. 130-137
    • Michalski, W.P.1    Nicholas, D.J.D.2
  • 18
    • 0030658026 scopus 로고    scopus 로고
    • Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis
    • Murphy M.E.P., Turley S., and Adman E.T. Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. J. Biol. Chem. 272 45 (1997) 28455-28460
    • (1997) J. Biol. Chem. , vol.272 , Issue.45 , pp. 28455-28460
    • Murphy, M.E.P.1    Turley, S.2    Adman, E.T.3
  • 19
    • 0037466312 scopus 로고    scopus 로고
    • Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu
    • Ellis M.J., Dodd F.E., Sawers G., Eady R.R., and Hasnain S.S. Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu. J. Mol. Biol. 328 (2003) 429-438
    • (2003) J. Mol. Biol. , vol.328 , pp. 429-438
    • Ellis, M.J.1    Dodd, F.E.2    Sawers, G.3    Eady, R.R.4    Hasnain, S.S.5
  • 20
    • 0032923887 scopus 로고    scopus 로고
    • Bacterial nitric oxide synthesis
    • Cutruzzolá F. Bacterial nitric oxide synthesis. BBA 1411 (1999) 231-249
    • (1999) BBA , vol.1411 , pp. 231-249
    • Cutruzzolá, F.1
  • 21
    • 84978427829 scopus 로고
    • Direct electrochemistry of nitrite reductase from Achromobacter cycloclastes IAM 1013
    • Kohzuma T., Shidara S., and Suzuki S. Direct electrochemistry of nitrite reductase from Achromobacter cycloclastes IAM 1013. Bull. Chem. Soc. Jpn. 67 1 (1994) 138-143
    • (1994) Bull. Chem. Soc. Jpn. , vol.67 , Issue.1 , pp. 138-143
    • Kohzuma, T.1    Shidara, S.2    Suzuki, S.3
  • 22
    • 0032574836 scopus 로고    scopus 로고
    • Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3
    • Olesen K., Veselov A., Zhao Y., Wang Y., Danner B., Scholes C.P., and Shapleigh J.P. Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3. Biochemistry 37 (1998) 6086-6094
    • (1998) Biochemistry , vol.37 , pp. 6086-6094
    • Olesen, K.1    Veselov, A.2    Zhao, Y.3    Wang, Y.4    Danner, B.5    Scholes, C.P.6    Shapleigh, J.P.7
  • 23
    • 33750006957 scopus 로고    scopus 로고
    • G. Decher, J. B. Schlenoff (Ed.), Multilayer thin films - sequential assembly of nanocomposite materials, WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim, 2003.
  • 24
    • 0023949893 scopus 로고
    • Electron transfer between the hydrogenase from Desulfovibrio vulgaris (Hildenborough) and viologens
    • Hoogvliet J.C., Lievense L.C., van DIJK C., and Veeger C. Electron transfer between the hydrogenase from Desulfovibrio vulgaris (Hildenborough) and viologens. Eur. J. Biochem. 174 (1988) 281-285
    • (1988) Eur. J. Biochem. , vol.174 , pp. 281-285
    • Hoogvliet, J.C.1    Lievense, L.C.2    van DIJK, C.3    Veeger, C.4
  • 25
    • 0026816759 scopus 로고
    • Reduction of nitrate and nitrite in water by immobilized enzymes
    • Mellor R.B., Ronnenberg J., Campbell W.H., and Diekmann S. Reduction of nitrate and nitrite in water by immobilized enzymes. Nature 355 (1992) 717-719
    • (1992) Nature , vol.355 , pp. 717-719
    • Mellor, R.B.1    Ronnenberg, J.2    Campbell, W.H.3    Diekmann, S.4
  • 26
    • 0033705280 scopus 로고    scopus 로고
    • Electroreduction of methylviologen in the presence of nitrite. Its influence on enzymatic electrodes
    • Ferreyra N.F., Dassie S.A., and Solis V.M. Electroreduction of methylviologen in the presence of nitrite. Its influence on enzymatic electrodes. J. Electroanal. Chem. 486 (2000) 126-132
    • (2000) J. Electroanal. Chem. , vol.486 , pp. 126-132
    • Ferreyra, N.F.1    Dassie, S.A.2    Solis, V.M.3
  • 28
    • 0018361387 scopus 로고
    • The chronoamperometric determination of homogeneous small molecule-redox protein reaction rates
    • Ryan M.D., Wei J.F., Feinberg B.A., and Lau Y.K. The chronoamperometric determination of homogeneous small molecule-redox protein reaction rates. Anal. Biochem. 96 (1979) 326-333
    • (1979) Anal. Biochem. , vol.96 , pp. 326-333
    • Ryan, M.D.1    Wei, J.F.2    Feinberg, B.A.3    Lau, Y.K.4
  • 29
    • 0037420696 scopus 로고    scopus 로고
    • Electrochemical study of the intermolecular electron transfer to Pseudomonas aeruginosa cytochrome cd1 nitrite reductase
    • Lojou E., Cutruzzola F., Tegoni M., and Bianco P. Electrochemical study of the intermolecular electron transfer to Pseudomonas aeruginosa cytochrome cd1 nitrite reductase. Electrochim. Acta 48 (2003) 1055-1064
    • (2003) Electrochim. Acta , vol.48 , pp. 1055-1064
    • Lojou, E.1    Cutruzzola, F.2    Tegoni, M.3    Bianco, P.4
  • 30
    • 0000014215 scopus 로고
    • Bard A.J. (Ed), Marcel Dekker, Inc., New York
    • Murray R.W. In: Bard A.J. (Ed). Chemically Modified Electrodes vol. 13 (1984), Marcel Dekker, Inc., New York 191-368
    • (1984) Chemically Modified Electrodes , vol.13 , pp. 191-368
    • Murray, R.W.1
  • 32
    • 0037062623 scopus 로고    scopus 로고
    • Catalytic function and local proton structure at the type 2 copper of nitrite reductase: the correlation of enzymatic pH dependence, conserved residues, and proton hyperfine structure
    • Zhao Y., Lukoyanov D.A., Toropov Y.V., Wu K., Shapleigh J.P., and Scholes C.P. Catalytic function and local proton structure at the type 2 copper of nitrite reductase: the correlation of enzymatic pH dependence, conserved residues, and proton hyperfine structure. Biochemistry 41 (2002) 7464-7474
    • (2002) Biochemistry , vol.41 , pp. 7464-7474
    • Zhao, Y.1    Lukoyanov, D.A.2    Toropov, Y.V.3    Wu, K.4    Shapleigh, J.P.5    Scholes, C.P.6
  • 33
    • 27544509539 scopus 로고    scopus 로고
    • Electrochemical determination of nitrate with nitrate reductase-immobilized electrodes under ambient air
    • Quan D., Shim J.H., Kim J.D., Park H.S., Cha G.S., and Nam H. Electrochemical determination of nitrate with nitrate reductase-immobilized electrodes under ambient air. Anal. Chem. 77 14 (2005) 4467-4473
    • (2005) Anal. Chem. , vol.77 , Issue.14 , pp. 4467-4473
    • Quan, D.1    Shim, J.H.2    Kim, J.D.3    Park, H.S.4    Cha, G.S.5    Nam, H.6
  • 34
    • 0003113502 scopus 로고
    • Eldman P.G., and Wang J. (Eds), ACS, Washington, D.C. Chap. 5
    • Gibson T.D., and Woodward J.R. In: Eldman P.G., and Wang J. (Eds). Biosensors and Chemical Sensors (1992), ACS, Washington, D.C. 40-55 Chap. 5
    • (1992) Biosensors and Chemical Sensors , pp. 40-55
    • Gibson, T.D.1    Woodward, J.R.2


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