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Volumn 76, Issue 1-2, 2009, Pages 34-41

Direct electron transfer reactions between human ceruloplasmin and electrodes

Author keywords

Ceruloplasmin; Direct electron transfer reactions; T1, T2, and T3 copper sites; T2 T3 copper cluster

Indexed keywords

CERULOPLASMIN; CERULOPLASMINS; COMPLEX MECHANISMS; COPPER SITES; DIRECT ELECTRON TRANSFER; DIRECT ELECTRON TRANSFER REACTIONS; ELECTRODE SURFACES; EXTENDED RANGE; FARADAIC PROCESS; GOLD ELECTRODES; GOLD NANOPARTICLES; INTRA-MOLECULAR ELECTRON TRANSFER; KINETIC TRAPPING; MIDPOINT POTENTIALS; MULTI-FUNCTIONAL; REDOX ENZYME; REDOX TRANSFORMATIONS; REDUCTION OF OXYGEN; T1, T2, AND T3 COPPER SITES; T2/T3 COPPER CLUSTER;

EID: 68549118693     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2009.05.012     Document Type: Article
Times cited : (21)

References (51)
  • 3
    • 33846678076 scopus 로고    scopus 로고
    • Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites
    • Bento I., Peixoto C., Zaitsev V.N., and Lindley P.F. Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites. Acta Crystallogr. D63 (2007) 240-248
    • (2007) Acta Crystallogr. , vol.D63 , pp. 240-248
    • Bento, I.1    Peixoto, C.2    Zaitsev, V.N.3    Lindley, P.F.4
  • 5
    • 0028934992 scopus 로고
    • Structure, oxidant activity, and cardiovascular mechanisms of human ceruloplasmin
    • Fox P.L., Mukhopadhyay C., and Ehrenwald E. Structure, oxidant activity, and cardiovascular mechanisms of human ceruloplasmin. Life Sci. 56 (1995) 1749-1758
    • (1995) Life Sci. , vol.56 , pp. 1749-1758
    • Fox, P.L.1    Mukhopadhyay, C.2    Ehrenwald, E.3
  • 6
    • 0016841056 scopus 로고
    • Evidence for ceruloplasmin as a copper transport protein
    • Hsieh H.S., and Frieden E. Evidence for ceruloplasmin as a copper transport protein. Biochem. Biophys. Res. Commun. 67 (1975) 1326-1331
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 1326-1331
    • Hsieh, H.S.1    Frieden, E.2
  • 7
    • 68549096400 scopus 로고    scopus 로고
    • Uppsala Universitet, Uppsala 72 pp.
    • Rosengren A. Cell-Protein-Material Interactions on Bioceramics and Model Surfaces. General Biochemistry (2004), Uppsala Universitet, Uppsala 72 pp.
    • (2004) General Biochemistry
    • Rosengren, A.1
  • 9
    • 0000852301 scopus 로고
    • Deficiency of ceruloplasmin in patients with hepatolenticular degeneration. I
    • Scheinberg H., and Gitlin D. Deficiency of ceruloplasmin in patients with hepatolenticular degeneration. I. Science 116 (1952) 484-485
    • (1952) Science , vol.116 , pp. 484-485
    • Scheinberg, H.1    Gitlin, D.2
  • 10
    • 7544227821 scopus 로고    scopus 로고
    • Enzymatic biofuel cells for implantable and microscale devices
    • Barton S.C., Gallaway J., and Atanassov P. Enzymatic biofuel cells for implantable and microscale devices. Chem. Rev. 104 (2004) 4867-4886
    • (2004) Chem. Rev. , vol.104 , pp. 4867-4886
    • Barton, S.C.1    Gallaway, J.2    Atanassov, P.3
  • 11
    • 0742304946 scopus 로고    scopus 로고
    • Miniature biofuel cells
    • Heller A. Miniature biofuel cells. Phys. Chem. Chem. Phys. 6 (2004) 209-216
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 209-216
    • Heller, A.1
  • 12
    • 18144414044 scopus 로고    scopus 로고
    • The three-dimensional structure of human ceruloplasmin at 3.0 Å resolution
    • Zaitsev V., Zaitseva I., Card G., Bax B., Ralph A., and Lindley P. The three-dimensional structure of human ceruloplasmin at 3.0 Å resolution. Fold. Des. 1 (1996) S71
    • (1996) Fold. Des. , vol.1
    • Zaitsev, V.1    Zaitseva, I.2    Card, G.3    Bax, B.4    Ralph, A.5    Lindley, P.6
  • 14
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trametes versicolor at 1.90 Å resolution containing a full complement of coppers
    • Piontek K., Antorini M., and Choinowski T. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90 Å resolution containing a full complement of coppers. J. Biol. Chem. 277 (2002) 37663-37669
    • (2002) J. Biol. Chem. , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 15
    • 0034694708 scopus 로고    scopus 로고
    • The thermodynamics, kinetics, and molecular mechanism of intramolecular electron transfer in human ceruloplasmin
    • Machonkin T.E., and Solomon E.I. The thermodynamics, kinetics, and molecular mechanism of intramolecular electron transfer in human ceruloplasmin. J. Am. Chem. Soc. 122 (2000) 12547-12560
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12547-12560
    • Machonkin, T.E.1    Solomon, E.I.2
  • 16
    • 0032581039 scopus 로고    scopus 로고
    • Spectroscopic and magnetic studies of human ceruloplasmin: identification of a redox-inactive reduced type 1 copper site
    • Machonkin T.E., Zhang H.H., Hedman B., Hodgson K.O., and Solomon E.I. Spectroscopic and magnetic studies of human ceruloplasmin: identification of a redox-inactive reduced type 1 copper site. Biochemistry 37 (1998) 9570-9578
    • (1998) Biochemistry , vol.37 , pp. 9570-9578
    • Machonkin, T.E.1    Zhang, H.H.2    Hedman, B.3    Hodgson, K.O.4    Solomon, E.I.5
  • 17
    • 0015789453 scopus 로고
    • The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin
    • Deinum J., and Vänngård T. The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin. Biochim. Biophys. Acta 310 (1973) 321-330
    • (1973) Biochim. Biophys. Acta , vol.310 , pp. 321-330
    • Deinum, J.1    Vänngård, T.2
  • 19
    • 0344037839 scopus 로고
    • Electrochemical conversion of lactoperoxidase, ceruloplasmin and alkaline phosphatase on mercury electrodes
    • Razumas V., Vidugiris G., Zapalskyte A., Gudavicius A., and Kulys J. Electrochemical conversion of lactoperoxidase, ceruloplasmin and alkaline phosphatase on mercury electrodes. Bioelectrochem. Bioenerg. 15 (1986) 407-415
    • (1986) Bioelectrochem. Bioenerg. , vol.15 , pp. 407-415
    • Razumas, V.1    Vidugiris, G.2    Zapalskyte, A.3    Gudavicius, A.4    Kulys, J.5
  • 20
    • 0025804819 scopus 로고
    • The electrochemical behavior of copper proteins using differential pulse polarography
    • Studnickova M., Pitrincova J., and Kovar J. The electrochemical behavior of copper proteins using differential pulse polarography. Bioelectrochem. Bioenerg. 25 (1991) 109-120
    • (1991) Bioelectrochem. Bioenerg. , vol.25 , pp. 109-120
    • Studnickova, M.1    Pitrincova, J.2    Kovar, J.3
  • 25
    • 52949143475 scopus 로고    scopus 로고
    • Direct electron transfer from graphite and functionalized gold electrodes to T1 and T2/T3 copper centers of bilirubin oxidase
    • Ramirez P., Mano N., Andreu R., Ruzgas T., Heller A., Gorton L., and Shleev S. Direct electron transfer from graphite and functionalized gold electrodes to T1 and T2/T3 copper centers of bilirubin oxidase. Biochim. Biophys. Acta 1777 (2008) 1364-1369
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1364-1369
    • Ramirez, P.1    Mano, N.2    Andreu, R.3    Ruzgas, T.4    Heller, A.5    Gorton, L.6    Shleev, S.7
  • 26
    • 4143122049 scopus 로고    scopus 로고
    • Direct heterogeneous electron transfer reactions of bilirubin oxidase at a spectrographic graphite electrode
    • Shleev S., El Kasmi A., Ruzgas T., and Gorton L. Direct heterogeneous electron transfer reactions of bilirubin oxidase at a spectrographic graphite electrode. Electrochem. Commun. 6 (2004) 934-939
    • (2004) Electrochem. Commun. , vol.6 , pp. 934-939
    • Shleev, S.1    El Kasmi, A.2    Ruzgas, T.3    Gorton, L.4
  • 27
    • 4544310436 scopus 로고    scopus 로고
    • Biomolecule-functionalized carbon nanotubes: applications in nanobioelectronics
    • Katz E., and Willner I. Biomolecule-functionalized carbon nanotubes: applications in nanobioelectronics. ChemPhysChem 5 (2004) 1084-1104
    • (2004) ChemPhysChem , vol.5 , pp. 1084-1104
    • Katz, E.1    Willner, I.2
  • 28
    • 1042278755 scopus 로고    scopus 로고
    • Electroanalytical and bioelectroanalytical systems based on metal and semiconductor nanoparticles
    • Katz E., Willner I., and Wang J. Electroanalytical and bioelectroanalytical systems based on metal and semiconductor nanoparticles. Electroanalysis 16 (2004) 19-44
    • (2004) Electroanalysis , vol.16 , pp. 19-44
    • Katz, E.1    Willner, I.2    Wang, J.3
  • 29
    • 0141994637 scopus 로고    scopus 로고
    • Electrochemistry at carbon nanotube electrodes
    • Li N., Wang J., and Li M. Electrochemistry at carbon nanotube electrodes. Rev. Anal. Chem. 22 (2003) 19-33
    • (2003) Rev. Anal. Chem. , vol.22 , pp. 19-33
    • Li, N.1    Wang, J.2    Li, M.3
  • 30
    • 0015813630 scopus 로고
    • Spectrophotometric determination of protein concentration in cell extracts containing tRNA and rRNA
    • Ehresmann B., Imbault P., and Weil J.H. Spectrophotometric determination of protein concentration in cell extracts containing tRNA and rRNA. Anal. Biochem. 54 (1973) 454-463
    • (1973) Anal. Biochem. , vol.54 , pp. 454-463
    • Ehresmann, B.1    Imbault, P.2    Weil, J.H.3
  • 31
    • 0141704212 scopus 로고    scopus 로고
    • Nanoparticulated gold: syntheses, structures, electronics, and reactivities
    • Schmid G., and Corain B. Nanoparticulated gold: syntheses, structures, electronics, and reactivities. Eur. J. Inorg. Chem. (2003) 3081-3098
    • (2003) Eur. J. Inorg. Chem. , pp. 3081-3098
    • Schmid, G.1    Corain, B.2
  • 32
    • 0000311733 scopus 로고
    • Electrochemical stability of catechols with a pyrene side chain strongly adsorbed on graphite electrodes for catalytic oxidation of dihydronicotinamide adenine dinucleotide
    • Jaegfeldt H., Kuwana T., and Johansson G. 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
  • 33
    • 84918552880 scopus 로고
    • Real surface area measurements in electrochemistry
    • Trasatti S., and Petrii O.A. Real surface area measurements in electrochemistry. Pure Appl. Chem. 63 (1991) 711-734
    • (1991) Pure Appl. Chem. , vol.63 , pp. 711-734
    • Trasatti, S.1    Petrii, O.A.2
  • 34
    • 33947712341 scopus 로고    scopus 로고
    • Direct electrochemical conversion of bilirubin oxidase at carbon nanotube-modified glassy carbon electrodes
    • Weigel M.C., Tritscher E., and Lisdat F. Direct electrochemical conversion of bilirubin oxidase at carbon nanotube-modified glassy carbon electrodes. Electrochem. Commun. 9 (2007) 689-693
    • (2007) Electrochem. Commun. , vol.9 , pp. 689-693
    • Weigel, M.C.1    Tritscher, E.2    Lisdat, F.3
  • 35
    • 0017858702 scopus 로고
    • Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface
    • De Feijter J.A., Benjamins J., and Veer F.A. Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface. Biopolymers 17 (1978) 1759-1772
    • (1978) Biopolymers , vol.17 , pp. 1759-1772
    • De Feijter, J.A.1    Benjamins, J.2    Veer, F.A.3
  • 36
    • 0001329209 scopus 로고    scopus 로고
    • Cyclic voltammetry and electrocatalysis of the blue copper oxidase Polyporus versicolor laccase
    • Thuesen M.H., Farver O., Reinhammar B., and Ulstrup J. Cyclic voltammetry and electrocatalysis of the blue copper oxidase Polyporus versicolor laccase. Acta Chem. Scand. 52 (1998) 555-562
    • (1998) Acta Chem. Scand. , vol.52 , pp. 555-562
    • Thuesen, M.H.1    Farver, O.2    Reinhammar, B.3    Ulstrup, J.4
  • 37
    • 19344375607 scopus 로고    scopus 로고
    • Attachment of organic layers to conductive or semiconductive surfaces by reduction of diazonium salts
    • Pinson J., and Podvorica F. Attachment of organic layers to conductive or semiconductive surfaces by reduction of diazonium salts. Chem. Soc. Rev. 34 (2005) 429-439
    • (2005) Chem. Soc. Rev. , vol.34 , pp. 429-439
    • Pinson, J.1    Podvorica, F.2
  • 38
    • 68549110603 scopus 로고
    • Role of enzyme mechanism in the manifestation of its electrocatalytic properties
    • Gindilis A.L., Yaropolov A.I., and Berezin I.V. Role of enzyme mechanism in the manifestation of its electrocatalytic properties. Dokl. Akad. Nauk SSSR 293 (1987) 383-386
    • (1987) Dokl. Akad. Nauk SSSR , vol.293 , pp. 383-386
    • Gindilis, A.L.1    Yaropolov, A.I.2    Berezin, I.V.3
  • 41
    • 0032526258 scopus 로고    scopus 로고
    • Unmediated heterogeneous electron transfer reaction of ascorbate oxidase and laccase at a gold electrode
    • Santucci R., Ferri T., Morpurgo L., Savini I., and Avigliano L. Unmediated heterogeneous electron transfer reaction of ascorbate oxidase and laccase at a gold electrode. Biochem. J. 332 (1998) 611-615
    • (1998) Biochem. J. , vol.332 , pp. 611-615
    • Santucci, R.1    Ferri, T.2    Morpurgo, L.3    Savini, I.4    Avigliano, L.5
  • 42
    • 0345356950 scopus 로고    scopus 로고
    • Catalytic monolayer voltammetry and in situ scanning tunneling microscopy of copper nitrite reductase on cysteamine-modified Au(111) electrodes
    • Zhang J., Welinder A.C., Hansen A.G., Christensen H.E.M., and Ulstrup J. Catalytic monolayer voltammetry and in situ scanning tunneling microscopy of copper nitrite reductase on cysteamine-modified Au(111) electrodes. J. Phys. Chem. B 107 (2003) 12480-12484
    • (2003) J. Phys. Chem. B , vol.107 , pp. 12480-12484
    • Zhang, J.1    Welinder, A.C.2    Hansen, A.G.3    Christensen, H.E.M.4    Ulstrup, J.5
  • 43
    • 0017900041 scopus 로고
    • Steady-state kinetics of laccase from Rhus vernicifera
    • Petersen L.C., and Degn H. Steady-state kinetics of laccase from Rhus vernicifera. Biochim. Biophys. Acta 526 (1978) 85-92
    • (1978) Biochim. Biophys. Acta , vol.526 , pp. 85-92
    • Petersen, L.C.1    Degn, H.2
  • 45
    • 24744467360 scopus 로고    scopus 로고
    • Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism
    • Antonyuk S.V., Strange R.W., Sawers G., Eady R.R., and Hasnain S.S. Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 12041-12046
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12041-12046
    • Antonyuk, S.V.1    Strange, R.W.2    Sawers, G.3    Eady, R.R.4    Hasnain, S.S.5
  • 46
    • 35648965701 scopus 로고    scopus 로고
    • Structure and function of type 1 copper in multicopper oxidases
    • Sakurai T., and Kataoka K. Structure and function of type 1 copper in multicopper oxidases. Cell. Mol. Life Sci. 64 (2007) 2642-2656
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2642-2656
    • Sakurai, T.1    Kataoka, K.2
  • 48
    • 53249127484 scopus 로고    scopus 로고
    • Transistor-like behavior of a fungal laccase
    • Shleev S., and Ruzgas T. Transistor-like behavior of a fungal laccase. Angew. Chem., Int. Ed. 47 (2008) 7270-7274
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 7270-7274
    • Shleev, S.1    Ruzgas, T.2
  • 49
    • 33646190025 scopus 로고    scopus 로고
    • Direct heterogeneous electron transfer reactions of fungal laccases at bare and thiol-modified gold electrodes
    • Pita M., Shleev S., Ruzgas T., Fernandez V.M., Yaropolov A.I., and Gorton L. Direct heterogeneous electron transfer reactions of fungal laccases at bare and thiol-modified gold electrodes. Electrochem. Commun. 8 (2006) 747-753
    • (2006) Electrochem. Commun. , vol.8 , pp. 747-753
    • Pita, M.1    Shleev, S.2    Ruzgas, T.3    Fernandez, V.M.4    Yaropolov, A.I.5    Gorton, L.6
  • 50
    • 33750470362 scopus 로고    scopus 로고
    • Direct heterogeneous electron transfer reactions of Trametes hirsuta laccase at bare and thiol-modified gold electrodes
    • Shleev S., Pita M., Yaropolov A.I., Ruzgas T., and Gorton L. Direct heterogeneous electron transfer reactions of Trametes hirsuta laccase at bare and thiol-modified gold electrodes. Electroanalysis 18 (2006) 1901-1908
    • (2006) Electroanalysis , vol.18 , pp. 1901-1908
    • Shleev, S.1    Pita, M.2    Yaropolov, A.I.3    Ruzgas, T.4    Gorton, L.5
  • 51
    • 0033600576 scopus 로고    scopus 로고
    • Investigation of the anomalous spectroscopic features of the copper sites in chicken ceruloplasmin: comparison to human ceruloplasmin
    • Machonkin T.E., Musci G., Zhang H.H., Patti M.C.B.D., Calabrese L., Hedman B., Hodgson K.O., and Solomon E.I. Investigation of the anomalous spectroscopic features of the copper sites in chicken ceruloplasmin: comparison to human ceruloplasmin. Biochemistry 38 (1999) 11093-11102
    • (1999) Biochemistry , vol.38 , pp. 11093-11102
    • Machonkin, T.E.1    Musci, G.2    Zhang, H.H.3    Patti, M.C.B.D.4    Calabrese, L.5    Hedman, B.6    Hodgson, K.O.7    Solomon, E.I.8


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