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Volumn 19, Issue 4, 2003, Pages 1238-1243

Oxidation of ABTS by silicate-immobilized cytochrome c in nonaqueous solutions

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROMES;

EID: 0041508717     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp0340537     Document Type: Article
Times cited : (29)

References (40)
  • 1
    • 0033022775 scopus 로고    scopus 로고
    • Measurements of the kinetic constants of protein adsorption onto silica particles
    • Docoslis, A.; Wu, W.; Giese, R. F.; Van Oss, C. J. Measurements of the kinetic constants of protein adsorption onto silica particles. Colloids Surf., B 1999, 13, 83.
    • (1999) Colloids Surf., B , vol.13 , pp. 83
    • Docoslis, A.1    Wu, W.2    Giese, R.F.3    Van Oss, C.J.4
  • 2
    • 0000024503 scopus 로고
    • Ellipsometry studies of protein layers adsorbed at hydrophobic surfaces
    • Malmsten, M. Ellipsometry studies of protein layers adsorbed at hydrophobic surfaces. J. Colloid Interface Sci. 1994, 166, 333.
    • (1994) J. Colloid Interface Sci. , vol.166 , pp. 333
    • Malmsten, M.1
  • 4
    • 0027619202 scopus 로고
    • Preparation of immobilised proteins covalently coupled through silane coupling agents to inorganic supports
    • Weetall, H. H. Preparation of immobilised proteins covalently coupled through silane coupling agents to inorganic supports. Appl. Biochem. Biotechnol. 1993, 41, 157.
    • (1993) Appl. Biochem. Biotechnol. , vol.41 , pp. 157
    • Weetall, H.H.1
  • 5
    • 0017267831 scopus 로고
    • Covalent coupling methods for inorganic support materials
    • Weetall, H. H. Covalent coupling methods for inorganic support materials. Methods Enzymol. 1976, 44, 134.
    • (1976) Methods Enzymol. , vol.44 , pp. 134
    • Weetall, H.H.1
  • 7
    • 0037067114 scopus 로고    scopus 로고
    • Review: Properties and applications of proteins encapsulated within sol-gel derived materials
    • Jin, W.; Brennan, J. D. Review. Properties and applications of proteins encapsulated within sol-gel derived materials. Anal. Chim. Acta 2002, 461, 1.
    • (2002) Anal. Chim. Acta , vol.461 , pp. 1
    • Jin, W.1    Brennan, J.D.2
  • 10
    • 0031801728 scopus 로고    scopus 로고
    • Nonionic triblock and star diblock copolymer and oligomeric surfactant syntheses of highly ordered, hydrothermally stable, meoporous silica structures
    • Zhao, D.; Huo, Q.; Feng, J.; Chmelka, B. F.; Stucky, G. D. Nonionic triblock and star diblock copolymer and oligomeric surfactant syntheses of highly ordered, hydrothermally stable, meoporous silica structures. J. Am. Chem. Soc. 1998, 120, 6024.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6024
    • Zhao, D.1    Huo, Q.2    Feng, J.3    Chmelka, B.F.4    Stucky, G.D.5
  • 11
    • 0033610438 scopus 로고    scopus 로고
    • Mesoporous silicate sequestration and release of proteins
    • Han, Y.-J.; Stucky, G. D.; Butler, A. Mesoporous silicate sequestration and release of proteins. J. Am. Chem. Soc. 1999, 121, 9897.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9897
    • Han, Y.-J.1    Stucky, G.D.2    Butler, A.3
  • 12
    • 0037174353 scopus 로고    scopus 로고
    • Entrapping enzyme in a functionalized nanoporous support
    • Lei, C.; Shin, Y.; Liu, J.; Ackerman, E. J. Entrapping enzyme in a functionalized nanoporous support. J. Am. Chem. Soc. 2002, 127, 11242.
    • (2002) J. Am. Chem. Soc. , vol.127 , pp. 11242
    • Lei, C.1    Shin, Y.2    Liu, J.3    Ackerman, E.J.4
  • 13
    • 0034736430 scopus 로고    scopus 로고
    • A new support for the immobilization of penicillin acylase
    • He, J.; Li, X.; Evans, D. G.; Duan, X.; Li., C. A new support for the immobilization of penicillin acylase. J. Mol. Catal. B 2000, 11, 45.
    • (2000) J. Mol. Catal. B , vol.11 , pp. 45
    • He, J.1    Li, X.2    Evans, D.G.3    Duan, X.4    Li, C.5
  • 14
    • 0030569494 scopus 로고    scopus 로고
    • Enzyme immobilization in MCM-41 molecular sieve
    • Díaz, J. F.; Balkus, K. J. Enzyme immobilization in MCM-41 molecular sieve. J. Mol. Catal. B 1996, 2, 115.
    • (1996) J. Mol. Catal. B , vol.2 , pp. 115
    • Díaz, J.F.1    Balkus, K.J.2
  • 15
    • 0034597441 scopus 로고    scopus 로고
    • Cytochrome c immobilization into meoporous molecular sieves
    • Washmon-Kriel, L.; Jimenez, V. L. ; Balkus, K. J. Cytochrome c immobilization into meoporous molecular sieves. J. Mol. Catal. B 2000, 10, 453.
    • (2000) J. Mol. Catal. B , vol.10 , pp. 453
    • Washmon-Kriel, L.1    Jimenez, V.L.2    Balkus, K.J.3
  • 16
    • 0035359821 scopus 로고    scopus 로고
    • Enzyme immobilisation using siliceous mesoporous molecular sieves
    • Yiu, H. H. P.; Wright, P. A.; Botting, N. P. Enzyme immobilisation using siliceous mesoporous molecular sieves. Microprous Mesoporous Mat. 2001, 44-45, 763.
    • (2001) Microprous Mesoporous Mat. , vol.44-45 , pp. 763
    • Yiu, H.H.P.1    Wright, P.A.2    Botting, N.P.3
  • 17
    • 0035820045 scopus 로고    scopus 로고
    • Adsorption and activity of cytochrome c on mesoporous silicates
    • Deere, J.; Magner, E.; Wall, J. G.; Hodnett, B. K. Adsorption and activity of cytochrome c on mesoporous silicates. Chem. Commun. 2001, 465.
    • (2001) Chem. Commun. , pp. 465
    • Deere, J.1    Magner, E.2    Wall, J.G.3    Hodnett, B.K.4
  • 18
    • 0037173849 scopus 로고    scopus 로고
    • The mechanistic and structural features of protein adsorption onto mesoporous silicates
    • Deere, J.; Magner, E.; Wall, J. G.; Hodnett, B. K. The mechanistic and structural features of protein adsorption onto mesoporous silicates. J. Phys. Chem. B 2002, 106, 7340.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 7340
    • Deere, J.1    Magner, E.2    Wall, J.G.3    Hodnett, B.K.4
  • 19
    • 0027703820 scopus 로고
    • Effect of water-miscible organic solvents on the catalytic activity of cytochrome c
    • Vazquez-Duhalt, R.; Westlake, D. W. S.; Fedorak, P. M. Effect of water-miscible organic solvents on the catalytic activity of cytochrome c. Enzyme Microb. Technol. 1993, 15, 936-943.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 936-943
    • Vazquez-Duhalt, R.1    Westlake, D.W.S.2    Fedorak, P.M.3
  • 20
    • 0027194319 scopus 로고
    • Cytochrome P450-like substrate oxidation catalysed by cytochrome c and immobilized cytochrome c
    • Akasaka, R.; Mushino, T.; Hirobe, M. Cytochrome P450-like substrate oxidation catalysed by cytochrome c and immobilized cytochrome c. Arch. Biochem. Biophys. 1993, 301, 355-360.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 355-360
    • Akasaka, R.1    Mushino, T.2    Hirobe, M.3
  • 21
    • 21844470225 scopus 로고    scopus 로고
    • Practical route to high activity enzyme preparations for synthesis in organic media
    • Partridge, J.; Halling, P. J.; Moore, B. D. Practical route to high activity enzyme preparations for synthesis in organic media. Chem. Commun. 1998, 841-842.
    • (1998) Chem. Commun. , pp. 841-842
    • Partridge, J.1    Halling, P.J.2    Moore, B.D.3
  • 22
    • 0000597110 scopus 로고
    • Cytochrome c from vertebrate and invertebrate sources
    • Margoliash, E.; Walasek O. F. Cytochrome c from vertebrate and invertebrate sources. Methods Enzymol. 1967, 10, 339.
    • (1967) Methods Enzymol. , vol.10 , pp. 339
    • Margoliash, E.1    Walasek, O.F.2
  • 25
    • 12444345676 scopus 로고    scopus 로고
    • note
    • No increase in specific activity was observed at higher concentrations of hydrogen peroxide.
  • 27
    • 0025101781 scopus 로고
    • Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: A Resonance Raman study
    • Hildebrandt, P.; Heimburg, T.; Marsh, D.; Powell G. L. Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: A Resonance Raman study. Biochemistry 1990, 29, 1661.
    • (1990) Biochemistry , vol.29 , pp. 1661
    • Hildebrandt, P.1    Heimburg, T.2    Marsh, D.3    Powell, G.L.4
  • 30
    • 0000203470 scopus 로고
    • Surface enhanced Raman spectroscopic evidence that adsorption on silver particles can denature heme proteins
    • Smulevich, G.; Spiro, T. G. Surface enhanced Raman spectroscopic evidence that adsorption on silver particles can denature heme proteins. J. Phys. Chem. 1985, 89, 5168.
    • (1985) J. Phys. Chem. , vol.89 , pp. 5168
    • Smulevich, G.1    Spiro, T.G.2
  • 31
    • 33845183059 scopus 로고
    • Consistent porphyrin force field. 3. Out-of-plane modes in the Resonance Raman spectra of planar and ruffled nickel-octaethylporphyrin
    • Li, X.-Y.; Czernuszewicz, R. S.; Kincaid, J. R.; Spiro, T. G. Consistent porphyrin force field. 3. Out-of-plane modes in the Resonance Raman spectra of planar and ruffled nickel-octaethylporphyrin. J. Am. Chem. Soc. 1989, 111, 7012.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7012
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Spiro, T.G.4
  • 32
    • 0011079003 scopus 로고
    • Consistent porphyrin force field. 1. Normal-mode analysis for nickel porphine and nickel tetraphenylporphine from Resonance Raman and infrared spectra and isotope shifts
    • Li, X.-Y.; Czernuszewicz, R. S.; Kincaid, J. R.; Su, Y. O.; Spiro, T. G. Consistent porphyrin force field. 1. Normal-mode analysis for nickel porphine and nickel tetraphenylporphine from Resonance Raman and infrared spectra and isotope shifts. J. Phys. Chem. 1990, 94, 31.
    • (1990) J. Phys. Chem. , vol.94 , pp. 31
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Su, Y.O.4    Spiro, T.G.5
  • 33
    • 33845183744 scopus 로고
    • Nickel octaethylporphyrin ruffling dynamics from Resonance Raman spectroscopy
    • Czernuszewicz, R. S.; Li, X.-Y.; Spiro, T. G. Nickel octaethylporphyrin ruffling dynamics from Resonance Raman spectroscopy. J. Am. Chem. Soc. 1989, 111, 7024.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7024
    • Czernuszewicz, R.S.1    Li, X.-Y.2    Spiro, T.G.3
  • 34
    • 0022539256 scopus 로고
    • Interaction of ferricytochrome c with cardiolipin multilayers: A Resonance Raman study
    • Vincent, J. S.; Levin, I. W. Interaction of ferricytochrome c with cardiolipin multilayers: A Resonance Raman study. J. Am. Chem. Soc. 1986, 108, 3551.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 3551
    • Vincent, J.S.1    Levin, I.W.2
  • 35
    • 33847086411 scopus 로고
    • Surface-enhanced Resonance Raman scattering from cytochrome c and myoglobin adsorbed on a silver electrode
    • Cotton, T. M.; Schultz, S. G.; Van Duyne, R. P. Surface-enhanced Resonance Raman scattering from cytochrome c and myoglobin adsorbed on a silver electrode. J. Am. Chem. Soc. 1980, 102, 7960.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7960
    • Cotton, T.M.1    Schultz, S.G.2    Van Duyne, R.P.3
  • 36
    • 0001173024 scopus 로고
    • Resonance Raman and electronic spectra of heme a complexes and cytochrome oxidase
    • Choi, S.; Lee, J. J.; Wei Y. H.; Spiro, T. G. Resonance Raman and electronic spectra of heme a complexes and cytochrome oxidase. J. Am. Chem. Soc. 1983, 105, 3692.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3692
    • Choi, S.1    Lee, J.J.2    Wei, Y.H.3    Spiro, T.G.4
  • 37
    • 0000161385 scopus 로고
    • Surface-enhanced Resonance Raman spectroscopy of cytochrome c at room and low temperatures
    • Hildebrandt, P.; Stockburger, M. Surface-enhanced Resonance Raman spectroscopy of cytochrome c at room and low temperatures. J. Phys. Chem. 1986, 90, 6017.
    • (1986) J. Phys. Chem. , vol.90 , pp. 6017
    • Hildebrandt, P.1    Stockburger, M.2
  • 38
    • 0027194319 scopus 로고
    • Cytochrome P450-like substrate oxidation catalysed by cytochrome c and immobilized cytochrome c
    • Akasaka, R.; Mushino, T.; Hirobe, M. Cytochrome P450-like substrate oxidation catalysed by cytochrome c and immobilized cytochrome c. Arch. Biochem. Biophys. 1993, 301, 355.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 355
    • Akasaka, R.1    Mushino, T.2    Hirobe, M.3
  • 39
    • 0021106640 scopus 로고
    • A 1H-NMR-logitudinal relaxation study of the interaction between cytochrome c and cytochrome c oxidase
    • Falk, K.-E.; Ångström, J. A 1H-NMR-logitudinal relaxation study of the interaction between cytochrome c and cytochrome c oxidase. Biochim. Biophys. Acta 1983, 722, 291.
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 291
    • Falk, K.-E.1    Ångström, J.2
  • 40
    • 0023658734 scopus 로고
    • A proton NMR-study of the non-covalent complex of horse cytochrome c and yeast cytochrome c peroxidase and its comparison with other interacting protein complexes
    • Satterlee, J.; Moench, S. J.; Erman, J. E. A proton NMR-study of the non-covalent complex of horse cytochrome c and yeast cytochrome c peroxidase and its comparison with other interacting protein complexes. Biochim. Biophys. Acta 1987, 912, 87.
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 87
    • Satterlee, J.1    Moench, S.J.2    Erman, J.E.3


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