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Volumn 20, Issue 2, 2004, Pages 294-304

Direct electrochemistry and electrocatalysis of heme-proteins entrapped in agarose hydrogel films

Author keywords

Agarose; Electrocatalysis; Electrochemistry; Hemoglobin; Horseradish peroxidase; Myoglobin

Indexed keywords

CATALYSIS; CYCLIC VOLTAMMETRY; ELECTROCHEMISTRY; ELECTRON TRANSITIONS; ENZYME IMMOBILIZATION; HYDROGELS; PH EFFECTS; PROTEINS; RATE CONSTANTS;

EID: 4043077652     PISSN: 09565663     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bios.2004.01.015     Document Type: Article
Times cited : (180)

References (62)
  • 2
    • 0001549184 scopus 로고    scopus 로고
    • Recent development in Faradaic bioelectrochemistry
    • Armstrong F.A., Wilson G.S. Recent development in Faradaic bioelectrochemistry. Electrochim. Acta. 45:2000;2623-2645
    • (2000) Electrochim. Acta , vol.45 , pp. 2623-2645
    • Armstrong, F.A.1    Wilson, G.S.2
  • 4
    • 0034927281 scopus 로고    scopus 로고
    • Influence of thermal history on the structural and mechanical proterties of agarose gels
    • Aymard P., Martin D.R., Plucknett K., Foster T.J., Clark A.H., Norton I.T. Influence of thermal history on the structural and mechanical proterties of agarose gels. Biopolymers. 59:2001;131-144
    • (2001) Biopolymers , vol.59 , pp. 131-144
    • Aymard, P.1    Martin, D.R.2    Plucknett, K.3    Foster, T.J.4    Clark, A.H.5    Norton, I.T.6
  • 8
    • 0033549045 scopus 로고    scopus 로고
    • Electron transfer and adsorption of myoglobin on self-assembled surfactant films: An electrochemical tapping-mode AFM study
    • Boussaad S., Tao N.J. Electron transfer and adsorption of myoglobin on self-assembled surfactant films: an electrochemical tapping-mode AFM study. J. Am. Chem. Soc. 121:1999;4510-4515
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4510-4515
    • Boussaad, S.1    Tao, N.J.2
  • 9
    • 0034734278 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin
    • Brunori M. Structural dynamics of myoglobin. Biophys. Chem. 86:2000;221-230
    • (2000) Biophys. Chem. , vol.86 , pp. 221-230
    • Brunori, M.1
  • 11
    • 0035179722 scopus 로고    scopus 로고
    • Direct electrochemistry of heme-proteins: Effect of electrode surface modification by neutral surfactant
    • Chattopadhyay K., Mazumdar S. Direct electrochemistry of heme-proteins: effect of electrode surface modification by neutral surfactant. Bioelectrochemistry. 53:2000;17-24
    • (2000) Bioelectrochemistry , vol.53 , pp. 17-24
    • Chattopadhyay, K.1    Mazumdar, S.2
  • 12
    • 0032646986 scopus 로고    scopus 로고
    • Ordered electrochemistry active films of hemoglobin, didodecyldimethylammonium ions, and clay
    • Chen X., Hu N., Zeng Y., Rusling J.F., Yang J. Ordered electrochemistry active films of hemoglobin, didodecyldimethylammonium ions, and clay. Langmuir. 15:1999;7022-7030
    • (1999) Langmuir , vol.15 , pp. 7022-7030
    • Chen, X.1    Hu, N.2    Zeng, Y.3    Rusling, J.F.4    Yang, J.5
  • 13
    • 0032477947 scopus 로고    scopus 로고
    • UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse myoglobin
    • Chi Z., Asher S.A. UV resonance Raman determination of protein acid denaturation: selective unfolding of helical segments of horse myoglobin. Biochemistry. 37:1998;2865-2872
    • (1998) Biochemistry , vol.37 , pp. 2865-2872
    • Chi, Z.1    Asher, S.A.2
  • 14
    • 0028099794 scopus 로고
    • The protein moiety modulates the redox potential in cytochrome c
    • Dolla A., Blanchard L., Guerlesquin F., Bruschi M. The protein moiety modulates the redox potential in cytochrome c. Biochimie. 76:1994;471-479
    • (1994) Biochimie , vol.76 , pp. 471-479
    • Dolla, A.1    Blanchard, L.2    Guerlesquin, F.3    Bruschi, M.4
  • 15
    • 0034306442 scopus 로고    scopus 로고
    • Direct electrochemical characterization of the interaction between haemoglobin and nitric oxide
    • Fan C., Chen X., Li G., Zhu J., Zhu D., Scheer H. Direct electrochemical characterization of the interaction between haemoglobin and nitric oxide. Phys. Chem. Chem. Phys. 2:2000;4409-4413
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4409-4413
    • Fan, C.1    Chen, X.2    Li, G.3    Zhu, J.4    Zhu, D.5    Scheer, H.6
  • 16
    • 0035387644 scopus 로고    scopus 로고
    • Electron-transfer reactivity and enzymatic activity of hemoglobin in a SP sephadex membrane
    • Fan C., Wang H., Sun S., Zhu D., Wagner G., Li G. Electron-transfer reactivity and enzymatic activity of hemoglobin in a SP sephadex membrane. Anal. Chem. 73:2001;2850-2854
    • (2001) Anal. Chem. , vol.73 , pp. 2850-2854
    • Fan, C.1    Wang, H.2    Sun, S.3    Zhu, D.4    Wagner, G.5    Li, G.6
  • 17
    • 0029063668 scopus 로고
    • A specttroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins
    • Faulkner K.M., Bonaventura C., Crumbliss A.L. A specttroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins. J. Biol. Chem. 270:1995;13604-13612
    • (1995) J. Biol. Chem. , vol.270 , pp. 13604-13612
    • Faulkner, K.M.1    Bonaventura, C.2    Crumbliss, A.L.3
  • 18
    • 0033694734 scopus 로고    scopus 로고
    • Redox reactions of heme-containing metalloproteins: Dynamic effects of self-assembled monolayers on thermodynamics and kinetics of cytochrome c electron-transfer reaction
    • Fedurco M. Redox reactions of heme-containing metalloproteins: dynamic effects of self-assembled monolayers on thermodynamics and kinetics of cytochrome c electron-transfer reaction. Coord. Chem. Rev. 209:2000;263-331
    • (2000) Coord. Chem. Rev. , vol.209 , pp. 263-331
    • Fedurco, M.1
  • 21
    • 0001555718 scopus 로고    scopus 로고
    • Enzyme-catalyzed direct electron transfer: Fundamentals and analytical application
    • Ghindilis A.L., Atanasov P., Wilkins E. Enzyme-catalyzed direct electron transfer: fundamentals and analytical application. Electroanalysis. 9:1997;661-674
    • (1997) Electroanalysis , vol.9 , pp. 661-674
    • Ghindilis, A.L.1    Atanasov, P.2    Wilkins, E.3
  • 22
    • 0035425177 scopus 로고    scopus 로고
    • Engineering and design in the bioelectrochemistry of metalloproteins
    • Gilardi G., Fantuzzi A., Sadeghi S.J. Engineering and design in the bioelectrochemistry of metalloproteins. Curr. Opin. Struct. Biol. 11:2001;491-499
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 491-499
    • Gilardi, G.1    Fantuzzi, A.2    Sadeghi, S.J.3
  • 23
    • 0032717605 scopus 로고    scopus 로고
    • Direct electron transfer between heme-contaning 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-contaning 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
  • 24
    • 0000390845 scopus 로고    scopus 로고
    • Organic phase enzyme electrodes based on organohydrogel
    • Guo Y., Dong S. Organic phase enzyme electrodes based on organohydrogel. Anal. Chem. 69:1997;1904-1908
    • (1997) Anal. Chem. , vol.69 , pp. 1904-1908
    • Guo, Y.1    Dong, S.2
  • 25
    • 0032771755 scopus 로고    scopus 로고
    • Immobilization of P450 monooxygenase and chloroplast for use in light-driven bioreactors
    • Hara M., Iazvovskaia S., Ohkawa H., Asada Y., Miyake J. Immobilization of P450 monooxygenase and chloroplast for use in light-driven bioreactors. J. Biosci. Bioeng. 87:1999;793-797
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 793-797
    • Hara, M.1    Iazvovskaia, S.2    Ohkawa, H.3    Asada, Y.4    Miyake, J.5
  • 26
    • 0001233062 scopus 로고
    • Oxidation-reduction potentials of horseradish preoxidase
    • Harbury H.A. Oxidation-reduction potentials of horseradish preoxidase. J. Biol. Chem. 225:1957;1009-1024
    • (1957) J. Biol. Chem. , vol.225 , pp. 1009-1024
    • Harbury, H.A.1
  • 27
    • 0030536477 scopus 로고    scopus 로고
    • The development of bioelectrochemistry
    • Hill H.A.O. The development of bioelectrochemistry. Coord. Chem. Rev. 151:1996;115-123
    • (1996) Coord. Chem. Rev. , vol.151 , pp. 115-123
    • Hill, H.A.O.1
  • 28
    • 0022469080 scopus 로고
    • Unfolding pathway of myoglobin: Molecular properties of intermediate forms
    • Irace G., Bismuto E., Savy F., Colonna G. Unfolding pathway of myoglobin: molecular properties of intermediate forms. Arch. Biochem. Biophys. 244:1986;459-459
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 459-459
    • Irace, G.1    Bismuto, E.2    Savy, F.3    Colonna, G.4
  • 30
    • 0000064115 scopus 로고
    • Electrochemical studies of cyanometmyoglobin and metmyoglobin: Implications for long-range electron transfer in proteins
    • King B.C., Hawkridge F.M., Hoffman B.M. Electrochemical studies of cyanometmyoglobin and metmyoglobin: implications for long-range electron transfer in proteins. J. Am. Chem. Soc. 114:1992;10603-10608
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10603-10608
    • King, B.C.1    Hawkridge, F.M.2    Hoffman, B.M.3
  • 31
    • 58149362952 scopus 로고
    • Selective and sensitive electrochemical measurement of nitric oxide in aqueous solution: Discussion and new results
    • Lantoine F., Trévin S., Bedioui F., Devynck J. Selective and sensitive electrochemical measurement of nitric oxide in aqueous solution: discussion and new results. J. Electroanal. Chem. 392:1995;85-89
    • (1995) J. Electroanal. Chem. , vol.392 , pp. 85-89
    • Lantoine, F.1    Trévin, S.2    Bedioui, F.3    Devynck, J.4
  • 33
    • 0021759421 scopus 로고
    • Structural basis for the variation of pH-dependent redox potentials of pseudomonas cytochromes c-551
    • Leitch F.A., Moore G.R., Pettigrew G.W. Structural basis for the variation of pH-dependent redox potentials of pseudomonas cytochromes c-551. Biochemistry. 23:1984;1831-1838
    • (1984) Biochemistry , vol.23 , pp. 1831-1838
    • Leitch, F.A.1    Moore, G.R.2    Pettigrew, G.W.3
  • 34
  • 35
    • 0038179881 scopus 로고    scopus 로고
    • Chen, X, Direct electrochemistry of horseradish peroxidase in surfactant films
    • (in Chinese)
    • Liu H., Li J., Hill H.A.O. Chen, X, Direct electrochemistry of horseradish peroxidase in surfactant films. Chin. J. Anal. Chem. 29:2001;511-515. (in Chinese)
    • (2001) Chin. J. Anal. Chem. , vol.29 , pp. 511-515
    • Liu, H.1    Li, J.2    Hill, H.A.O.3
  • 37
    • 0034895677 scopus 로고    scopus 로고
    • Electrocatalysis of nitric oxide reduction by hemoglobin entrapped in surfactant films
    • Mimica D., Zagal J.H., Bedioui F. Electrocatalysis of nitric oxide reduction by hemoglobin entrapped in surfactant films. Electrochem. Commun. 3:2001;435-438
    • (2001) Electrochem. Commun. , vol.3 , pp. 435-438
    • Mimica, D.1    Zagal, J.H.2    Bedioui, F.3
  • 38
    • 0036525946 scopus 로고    scopus 로고
    • Nitric oxide and myoglobins
    • Møller J.K.S., Skibsted L.H. Nitric oxide and myoglobins. Chem. Rev. 102:2002;1167-1178
    • (2002) Chem. Rev. , vol.102 , pp. 1167-1178
    • Møller, J.K.S.1    Skibsted, L.H.2
  • 39
    • 0000610156 scopus 로고
    • Structure of hemoglobin: Three-dimensional fourier synthesis of reduced human hemoglobin at 5.5-A resolution
    • Muirhead H., Perutz M.F. Structure of hemoglobin: three-dimensional fourier synthesis of reduced human hemoglobin at 5.5-A resolution. Nature. 199:1963;633-638
    • (1963) Nature , vol.199 , pp. 633-638
    • Muirhead, H.1    Perutz, M.F.2
  • 40
    • 0000866442 scopus 로고    scopus 로고
    • Proton-coupled electron transfer from electrodes to myoglobin in ordered biomembrane-like films
    • Nassar A.E.F., Zhang Z., Hu N., Rusling J.F., Kumosinski T.F. Proton-coupled electron transfer from electrodes to myoglobin in ordered biomembrane-like films. J. Phys. Chem. B. 101:1997;2224-2231
    • (1997) J. Phys. Chem. B , vol.101 , pp. 2224-2231
    • Nassar, A.E.F.1    Zhang, Z.2    Hu, N.3    Rusling, J.F.4    Kumosinski, T.F.5
  • 41
    • 0000163656 scopus 로고
    • IR reflectance studies of electron transfer promotes for cytochrome c on a gold electrode
    • Niwa K., Furukawa M., Niki K. IR reflectance studies of electron transfer promotes for cytochrome c on a gold electrode. J. Electroanal. Chem. 245:1988;275-285
    • (1988) J. Electroanal. Chem. , vol.245 , pp. 275-285
    • Niwa, K.1    Furukawa, M.2    Niki, K.3
  • 42
    • 0345651843 scopus 로고
    • Characterization of quasi-reversible surface processes by square-wave voltammetry
    • O'Dea J.J., Osteryoung J.G. Characterization of quasi-reversible surface processes by square-wave voltammetry. Anal. Chem. 65:1993;3090-3097
    • (1993) Anal. Chem. , vol.65 , pp. 3090-3097
    • O'Dea, J.J.1    Osteryoung, J.G.2
  • 43
    • 0343081403 scopus 로고    scopus 로고
    • The electrocatalytic reduction of organohalides by myoglobin and hemoglobin in a biomembrane-like film and its application to the electrochemical detection of pollutants: New trends and discussion
    • Ordaz A.A., Bedioui F. The electrocatalytic reduction of organohalides by myoglobin and hemoglobin in a biomembrane-like film and its application to the electrochemical detection of pollutants: new trends and discussion. Sens. Actuators B. 59:1999;128-133
    • (1999) Sens. Actuators B , vol.59 , pp. 128-133
    • Ordaz, A.A.1    Bedioui, F.2
  • 44
    • 0034773546 scopus 로고    scopus 로고
    • Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin
    • Ozaki S., Roach M.P., Matsui T., Watanabe Y. Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin. Acc. Chem. Res. 34:2001;818-825
    • (2001) Acc. Chem. Res. , vol.34 , pp. 818-825
    • Ozaki, S.1    Roach, M.P.2    Matsui, T.3    Watanabe, Y.4
  • 45
    • 0027940427 scopus 로고
    • Acid-induced transformation of myoglobin. Characterization of a new equilibrium heme-pocket intermediate
    • Palaniappan V., Bocian D.F. Acid-induced transformation of myoglobin. Characterization of a new equilibrium heme-pocket intermediate. Biochemistry. 33:1994;14264-14274
    • (1994) Biochemistry , vol.33 , pp. 14264-14274
    • Palaniappan, V.1    Bocian, D.F.2
  • 46
    • 0037164046 scopus 로고    scopus 로고
    • Ultrathin layered myoglobin-polyion films functional and stable at acidic pH values
    • Panchangnula V., Kumar C.V., Rusling J.F. Ultrathin layered myoglobin-polyion films functional and stable at acidic pH values. J. Am. Chem. Soc. 124:2002;12515-12521
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12515-12521
    • Panchangnula, V.1    Kumar, C.V.2    Rusling, J.F.3
  • 47
    • 0037066257 scopus 로고    scopus 로고
    • Myoglobin, a paradigm in the study of protein dynamics
    • Parak F.G., Nienhaus G.U. Myoglobin, a paradigm in the study of protein dynamics. Chem. Phys. Chem. 3:2002;249-254
    • (2002) Chem. Phys. Chem. , vol.3 , pp. 249-254
    • Parak, F.G.1    Nienhaus, G.U.2
  • 48
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • Pascher T., Chesick J.P., Winkler J.R., Gray H.B. Protein folding triggered by electron transfer. Science. 271:1996;1558-1560
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 49
    • 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
  • 50
    • 0000739645 scopus 로고
    • Enhanced electron transfer for myoglobin in surfactant films on electrodes
    • Rusling J.F., Nassar A.E.F. Enhanced electron transfer for myoglobin in surfactant films on electrodes. J. Am. Chem. Soc. 115:1993;11891-11897
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11891-11897
    • Rusling, J.F.1    Nassar, A.E.F.2
  • 51
    • 0036646074 scopus 로고    scopus 로고
    • Mechanistic and molecular investigations on stabilization of horseradish peroxidase c
    • Schmidt A., Schumacher J.T., Reichelt J., Hecht H.J., Bilitewski U. Mechanistic and molecular investigations on stabilization of horseradish peroxidase c. Anal. Chem. 74:2002;3037-3045
    • (2002) Anal. Chem. , vol.74 , pp. 3037-3045
    • Schmidt, A.1    Schumacher, J.T.2    Reichelt, J.3    Hecht, H.J.4    Bilitewski, U.5
  • 52
    • 0034610349 scopus 로고    scopus 로고
    • Heme redox potential control in de novo designed four-α-helix bundle
    • Shifman J.M., Gibney B.R., Sharp R.E., Dutton P.L. Heme redox potential control in de novo designed four-α-helix bundle. Biochemistry. 39:2000;14813-14821
    • (2000) Biochemistry , vol.39 , pp. 14813-14821
    • Shifman, J.M.1    Gibney, B.R.2    Sharp, R.E.3    Dutton, P.L.4
  • 53
    • 0034582188 scopus 로고    scopus 로고
    • Effects of pH on the kinetic reaction mechanism of myoglobin unfolding
    • Sogbein O.O., Simmons D.A., Konermann L. Effects of pH on the kinetic reaction mechanism of myoglobin unfolding. J. Am. Soc. Mass Spectrosc. 11:2000;312-319
    • (2000) J. Am. Soc. Mass Spectrosc. , vol.11 , pp. 312-319
    • Sogbein, O.O.1    Simmons, D.A.2    Konermann, L.3
  • 54
    • 0016400375 scopus 로고
    • Resonance Raman spectra of heme-proteins. Effect of oxidation and spin state
    • Spiro T.G., Strekas T.C. Resonance Raman spectra of heme-proteins. Effect of oxidation and spin state. J. Am. Chem. Soc. 96:1974;338-345
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 338-345
    • Spiro, T.G.1    Strekas, T.C.2
  • 55
    • 0034234621 scopus 로고    scopus 로고
    • Electron transfer from diamond electrodes to heme peptide and peroxidase
    • Tatsuma T., Mori H., Fulishima A. Electron transfer from diamond electrodes to heme peptide and peroxidase. Anal. Chem. 72:2000;2919-2924
    • (2000) Anal. Chem. , vol.72 , pp. 2919-2924
    • Tatsuma, T.1    Mori, H.2    Fulishima, A.3
  • 56
    • 0029867916 scopus 로고    scopus 로고
    • Control of myoglobin electron-transfer rate by the distal (nonbound) histidine residue
    • Van Dyke B.R., Saltman P., Armstrong F.A. Control of myoglobin electron-transfer rate by the distal (nonbound) histidine residue. J. Am. Chem. Soc. 118:1996;3490-3492
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3490-3492
    • Van Dyke, B.R.1    Saltman, P.2    Armstrong, F.A.3
  • 57
    • 0034791070 scopus 로고    scopus 로고
    • Factors that determine the unusually low reduction potential of cytochrome c (550) in cyanobacterial photosystem II
    • Vrettos J.S., Reifler M.J., Laksshmi K.V., de Paula J.C. Factors that determine the unusually low reduction potential of cytochrome c (550) in cyanobacterial photosystem II. J. Biol. Inorg. Chem. 6:2001;708-716
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 708-716
    • Vrettos, J.S.1    Reifler, M.J.2    Laksshmi, K.V.3    De Paula, J.C.4
  • 60
    • 0014280659 scopus 로고
    • Regulation in macromolecules, as illustrated by hemoglobin
    • Wyman J. Regulation in macromolecules, as illustrated by hemoglobin. Q. Rev. Biophys. 1:1968;35-80
    • (1968) Q. Rev. Biophys. , vol.1 , pp. 35-80
    • Wyman, J.1
  • 62
    • 0034670331 scopus 로고    scopus 로고
    • Direct electron transfer of ferritin adsorbed at bare gold electrodes
    • Zapien D.C., Johnson M.A. Direct electron transfer of ferritin adsorbed at bare gold electrodes. J. Electranal. Chem. 494:2000;114-120
    • (2000) J. Electranal. Chem. , vol.494 , pp. 114-120
    • Zapien, D.C.1    Johnson, M.A.2


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