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Volumn 41, Issue 2, 1996, Pages 217-220

The effect of oxygen on the electrochemical behavior of myoglobin

Author keywords

Myoglobin; Oxygen; Synchronous fluorescence spectroscopy

Indexed keywords

CHARGE TRANSFER; COMPOSITION EFFECTS; CYCLIC VOLTAMMETRY; ELECTROCHEMICAL ELECTRODES; ELECTROCHEMISTRY; ELECTROLYTIC REDUCTION; LIVING SYSTEMS STUDIES; OXIDATION; OXYGEN; REACTION KINETICS; SPECTROSCOPY;

EID: 0030450824     PISSN: 03024598     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0302-4598(96)05119-7     Document Type: Article
Times cited : (7)

References (26)
  • 3
    • 0018129356 scopus 로고
    • Haem exposure as the determinate of oxidation-reduction potential of haem proteins
    • [3] E. Stellwagen, Haem exposure as the determinate of oxidation-reduction potential of haem proteins, Nature, 275 (1978) 73.
    • (1978) Nature , vol.275 , pp. 73
    • Stellwagen, E.1
  • 4
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 å resolution: I crystallographic refinement of metmyoglobin from sperm whale
    • [4] T. Takano, Structure of myoglobin refined at 2.0 Å resolution: I Crystallographic refinement of metmyoglobin from sperm whale, J. Mol. Biol., 110 (1977) 537.
    • (1977) J. Mol. Biol. , vol.110 , pp. 537
    • Takano, T.1
  • 7
    • 0017978714 scopus 로고
    • Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode
    • [7] J.F. Stargardt, F.M. Hawkridge and H. L. Landrum, Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode, Anal. Chem., 50 (1978) 930.
    • (1978) Anal. Chem. , vol.50 , pp. 930
    • Stargardt, J.F.1    Hawkridge, F.M.2    Landrum, H.L.3
  • 8
    • 33847086411 scopus 로고
    • Surface-enhanced resonance Raman scattering from cytochrome c adsorbed on a silver electrode
    • [8] T.M. Cotton, S.G. Schultz and R.P. Van Duyne, surface-enhanced resonance Raman scattering from cytochrome c adsorbed on a silver electrode, J. Am. Chem. Soc., 102 (1980) 7960.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7960
    • Cotton, T.M.1    Schultz, S.G.2    Van Duyne, R.P.3
  • 9
    • 0000577655 scopus 로고
    • 343-heterogeneous electron transfer kinetics of sperm whale myoglobin
    • [9] E.F. Bowden, F.M. Hawkridge and H.N. Blount, 343-Heterogeneous electron transfer kinetics of sperm whale myoglobin, Bioelectrochem. Bioenerg., 7 (1980) 447.
    • (1980) Bioelectrochem. Bioenerg. , vol.7 , pp. 447
    • Bowden, E.F.1    Hawkridge, F.M.2    Blount, H.N.3
  • 10
    • 0026787992 scopus 로고
    • Redox-induced conformational changes in myoglobin and hemoglobin: Electrochemistry and ultraviolet-visible and Fourier transform infrared difference spectroscopy at surface-modified gold electrode in an ultra-thin-layer spectroelectrochemical cell
    • [10] D.D. Schlereth and W. Mantele, Redox-induced conformational changes in myoglobin and hemoglobin: electrochemistry and ultraviolet-visible and Fourier transform infrared difference spectroscopy at surface-modified gold electrode in an ultra-thin-layer spectroelectrochemical cell, Biochemstry, 31 (1992) 7494.
    • (1992) Biochemstry , vol.31 , pp. 7494
    • Schlereth, D.D.1    Mantele, W.2
  • 11
    • 0022758474 scopus 로고
    • A novel mediator for the investigation of the electrochemistry of metalloproteins
    • [11] S. Kwee, A novel mediator for the investigation of the electrochemistry of metalloproteins, Bioelectrochem. Bioenerg., 16 (1986) 99.
    • (1986) Bioelectrochem. Bioenerg. , vol.16 , pp. 99
    • Kwee, S.1
  • 12
    • 84984351217 scopus 로고
    • Study on electrode process of myoglobin at a polymerized toluidine blue film electrode
    • [12] S. Dong and Q. Chu, Study on electrode process of myoglobin at a polymerized toluidine blue film electrode, Chin. J. Chem., 11 (1993) 12.
    • (1993) Chin. J. Chem. , vol.11 , pp. 12
    • Dong, S.1    Chu, Q.2
  • 13
    • 0024289078 scopus 로고
    • Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue
    • [13] J. Ye and R.P. Baldwin, Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue, Anal. Chem., 60 (1988) 2263.
    • (1988) Anal. Chem. , vol.60 , pp. 2263
    • Ye, J.1    Baldwin, R.P.2
  • 14
    • 0344787415 scopus 로고
    • A study of the electron transfer and oxygen binding reactions of myoglobin
    • [14] B.C. King and F.M. Hawkridge, A study of the electron transfer and oxygen binding reactions of myoglobin, J. Electroanal. Chem., 237 (1987) 81.
    • (1987) J. Electroanal. Chem. , vol.237 , pp. 81
    • King, B.C.1    Hawkridge, F.M.2
  • 15
    • 0000234036 scopus 로고
    • Direct electron transfer of horse heart myoglobin at an indium oxide electrode
    • [15] I. Taniguchi, K. Watanabe, M. Tominaga and F.M. Hawkridge, Direct electron transfer of horse heart myoglobin at an indium oxide electrode, J. Electroanal. Chem., 333 (1992) 331.
    • (1992) J. Electroanal. Chem. , vol.333 , pp. 331
    • Taniguchi, I.1    Watanabe, K.2    Tominaga, M.3    Hawkridge, F.M.4
  • 16
    • 0029645136 scopus 로고
    • Electron transfer from electrodes to myoglobin: Facilitated in surfactant films and blocked by adsorbed biomacromolecules
    • [16] A.F. Nassar, W.S. Willis and J.F. Rusling, Electron transfer from electrodes to myoglobin: facilitated in surfactant films and blocked by adsorbed biomacromolecules, Anal. Chem., 67 (1995) 2386.
    • (1995) Anal. Chem. , vol.67 , pp. 2386
    • Nassar, A.F.1    Willis, W.S.2    Rusling, J.F.3
  • 17
    • 0000739645 scopus 로고
    • Enhanced electron transfer for myoglobin in surfactant films on electrodes
    • [17] J.F. Rusling and A.F. Nassar, Enhanced electron transfer for myoglobin in surfactant films on electrodes, J. Am. Chem. Soc., 115 (1993) 11891.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11891
    • Rusling, J.F.1    Nassar, A.F.2
  • 18
    • 0018626364 scopus 로고
    • 310-optically transparent thin layer electrode techniques for the study of biological redox systems
    • [18] W.R. Heineman, M.L. Meckstoth, B.J. Norris and C. Su, 310-Optically transparent thin layer electrode techniques for the study of biological redox systems, Bioelectrochem. Bioenerg., 6 (1979) 577.
    • (1979) Bioelectrochem. Bioenerg. , vol.6 , pp. 577
    • Heineman, W.R.1    Meckstoth, M.L.2    Norris, B.J.3    Su, C.4
  • 19
    • 33947483336 scopus 로고
    • Theory and application of cyclic voltammetry for measurement of electrode reaction kinetics
    • [19] R.S. Nicholson, Theory and application of cyclic voltammetry for measurement of electrode reaction kinetics, Anal. Chem., 35 (1965) 1351.
    • (1965) Anal. Chem. , vol.35 , pp. 1351
    • Nicholson, R.S.1
  • 20
    • 4243947039 scopus 로고    scopus 로고
    • The study of synchronous fluorescence spectroscopy of horse heart myoglobin
    • submitted to
    • [20] J. Chou and T. Lu, The study of synchronous fluorescence spectroscopy of horse heart myoglobin, submitted to Spectrochim. Acta.
    • Spectrochim. Acta.
    • Chou, J.1    Lu, T.2
  • 21
    • 0000043876 scopus 로고
    • Evidence for the role of myoglobin in facilitating oxygen transport
    • [21] B.C. King and F.M. Hawkridge, Evidence for the role of myoglobin in facilitating oxygen transport, Talanta, 36 (1989) 331.
    • (1989) Talanta , vol.36 , pp. 331
    • King, B.C.1    Hawkridge, F.M.2
  • 23
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9Å
    • [23] R.F. Tilton, I.D. Kuntz, Jr., and G.A. Petsko, Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9Å, Biochemistry, 23 (1984) 2849.
    • (1984) Biochemistry , vol.23 , pp. 2849
    • Tilton, R.F.1    Kuntz I.D., Jr.2    Petsko, G.A.3
  • 24
    • 0001271667 scopus 로고
    • Preliminary spectrofluoroelectrochemical studies indicate a possible conformational change in horse heart cytochrome c upon reduction
    • [24] M.J. Simone, W.R. Heineman and G.P. Kreishman, Preliminary spectrofluoroelectrochemical studies indicate a possible conformational change in horse heart cytochrome c upon reduction, J. Colloid Interface Sci., 86 (1982) 295.
    • (1982) J. Colloid Interface Sci. , vol.86 , pp. 295
    • Simone, M.J.1    Heineman, W.R.2    Kreishman, G.P.3
  • 25
    • 0002954253 scopus 로고
    • Determination of unimolecular electron transfer rate constants for strongly adsorbed cytochrome c on tin dioxide electrodes
    • [25] J. Willit and E.F. Bowden, Determination of unimolecular electron transfer rate constants for strongly adsorbed cytochrome c on tin dioxide electrodes, J. Electroanal. Chem., 221 (1987) 265.
    • (1987) J. Electroanal. Chem. , vol.221 , pp. 265
    • Willit, J.1    Bowden, E.F.2
  • 26
    • 0000064115 scopus 로고
    • Electrochemical studies of cyanometmyoglobin and metmyoglobin: Implications for long-range electron transfer in proteins
    • [26] B.C. King, F.M. Hawkridge and B.M. Hoffman, Electrochemical studies of cyanometmyoglobin and metmyoglobin: implications for long-range electron transfer in proteins, J. Am. Chem. Soc., 114 (1992) 10603.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10603
    • King, B.C.1    Hawkridge, F.M.2    Hoffman, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.