메뉴 건너뛰기




Volumn 76, Issue 1 I, 1999, Pages 443-450

Apohorseradish peroxidase unfolding and refolding: Intrinsic tryptophan fluorescence studies

Author keywords

[No Author keywords available]

Indexed keywords

GUANIDINE; HORSERADISH PEROXIDASE; TRYPTOPHAN;

EID: 0032952722     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77211-5     Document Type: Article
Times cited : (31)

References (42)
  • 1
    • 0022129680 scopus 로고
    • Multifrequency phase fluorometry using the harmonic content of a mode-locked laser
    • Alcala, J. R., E. Gratton, and D. M. Jameson. 1985. Multifrequency phase fluorometry using the harmonic content of a mode-locked laser. Anal. Instrum. 14:225-250.
    • (1985) Anal. Instrum. , vol.14 , pp. 225-250
    • Alcala, J.R.1    Gratton, E.2    Jameson, D.M.3
  • 2
    • 0023320102 scopus 로고
    • Resolvability of fluorescence lifetime distributions
    • Alcala, J. R., E. Gratton, and F. J. Prendergast. 1987a. Resolvability of fluorescence lifetime distributions. Biophys. J. 51:587-596.
    • (1987) Biophys. J. , vol.51 , pp. 587-596
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.J.3
  • 3
    • 0023317270 scopus 로고
    • Fluorescence lifetime distributions in proteins
    • Alcala, J. R., E. Gratton, and F. J. Prendergast. 1987b. Fluorescence lifetime distributions in proteins. Biophys. J. 51:597-604.
    • (1987) Biophys. J. , vol.51 , pp. 597-604
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.J.3
  • 4
    • 0023357309 scopus 로고
    • Interpretation of fluorescence decay in proteins using continuous lifetime distributions
    • Alcala, J. R., E. Gratton, and F. J. Prendergast. 1987c. Interpretation of fluorescence decay in proteins using continuous lifetime distributions. Biophys. J. 51:925-936.
    • (1987) Biophys. J. , vol.51 , pp. 925-936
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.J.3
  • 5
    • 0028500077 scopus 로고
    • Expression of a neutral horseradish peroxidase in Escherichia coli
    • Bartonek-Roxå, E., and H. Eriksson. 1994. Expression of a neutral horseradish peroxidase in Escherichia coli. J. Biotechnol. 37:133-142.
    • (1994) J. Biotechnol. , vol.37 , pp. 133-142
    • Bartonek-Roxå, E.1    Eriksson, H.2
  • 7
    • 0024294305 scopus 로고
    • Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin
    • Bismuto. E., E. Gratton, and G. Irace. 1988. Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin. Biochemistry. 27:2132-2136.
    • (1988) Biochemistry , vol.27 , pp. 2132-2136
    • Bismuto, E.1    Gratton, E.2    Irace, G.3
  • 8
    • 0020804264 scopus 로고
    • Intramolecular tryptophan heme energy transfer in horseradish peroxidase
    • Brunet, J. E., G. A. Gonzalez, and C. P. Sotomayor. 1983. Intramolecular tryptophan heme energy transfer in horseradish peroxidase. Photochem. Photobiol. 38:253-254.
    • (1983) Photochem. Photobiol. , vol.38 , pp. 253-254
    • Brunet, J.E.1    Gonzalez, G.A.2    Sotomayor, C.P.3
  • 9
    • 0027519596 scopus 로고
    • Dynamics of protoporphyrin IX in the heme pocket of horseradish peroxidase
    • Brunet, J. E., and M. Pulgar. 1993. Dynamics of protoporphyrin IX in the heme pocket of horseradish peroxidase. Biochim. Biophys. Acta. 1203: 171-174.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 171-174
    • Brunet, J.E.1    Pulgar, M.2
  • 10
    • 0028012732 scopus 로고
    • Hydrodynamics of horseradish peroxidase revealed by global analysis of multiple fluorescence probes
    • Brunet, J. E., V. Vargas, E. Gratton, and D. M. Jameson. 1994. Hydrodynamics of horseradish peroxidase revealed by global analysis of multiple fluorescence probes. Biophys. J. 66:446-453.
    • (1994) Biophys. J. , vol.66 , pp. 446-453
    • Brunet, J.E.1    Vargas, V.2    Gratton, E.3    Jameson, D.M.4
  • 11
    • 0017251905 scopus 로고
    • The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzymes C
    • Clarke, J., and L. M. Shannon. 1976. The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzymes C. Biochim. Biophys. Acta. 421:428-442.
    • (1976) Biochim. Biophys. Acta , vol.421 , pp. 428-442
    • Clarke, J.1    Shannon, L.M.2
  • 12
    • 0028796185 scopus 로고
    • pH-induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes
    • Das, T. K., and S. Mazumdar. 1995. pH-Induced conformational perturbation in horseradish peroxidase. Picosecond tryptophan fluorescence studies on native and cyanide-modified enzymes. Eur. J. Biochem. 227:823-828.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 823-828
    • Das, T.K.1    Mazumdar, S.2
  • 13
    • 0014952478 scopus 로고
    • Thin-layer isoelectric focusing on Sephadex layers of horseradish peroxidase
    • Delincee, H., and J. B. Radolla. 1970. Thin-layer isoelectric focusing on Sephadex layers of horseradish peroxidase. Biochim. Biophys. Acta. 200:3607-3617.
    • (1970) Biochim. Biophys. Acta , vol.200 , pp. 3607-3617
    • Delincee, H.1    Radolla, J.B.2
  • 14
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:482-501.
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 15
    • 0021411487 scopus 로고
    • A multifrequency cross-correlation phase fluorometer using synchrotron radiation
    • Gratton, E., D. M. Jameson, N. Rosato, and G. Weber. 1984. A multifrequency cross-correlation phase fluorometer using synchrotron radiation. Rev. Sci. Instrum. 55:486-494.
    • (1984) Rev. Sci. Instrum. , vol.55 , pp. 486-494
    • Gratton, E.1    Jameson, D.M.2    Rosato, N.3    Weber, G.4
  • 17
    • 0026760509 scopus 로고
    • Baculovirus expression and characterization of catalytically active horseradish peroxidase
    • Hartman, C., and P. R. Ortiz de Montellano. 1992. Baculovirus expression and characterization of catalytically active horseradish peroxidase. Arch. Biochem. Biophys. 297:61-72.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 61-72
    • Hartman, C.1    Ortiz De Montellano, P.R.2
  • 18
    • 0026490427 scopus 로고
    • Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer
    • James, E. P. G., W. Wu, L. Stites, and L. Brand. 1992. Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer. Biochemistry. 31:10217-10225.
    • (1992) Biochemistry , vol.31 , pp. 10217-10225
    • James, E.P.G.1    Wu, W.2    Stites, L.3    Brand, L.4
  • 19
    • 0002061188 scopus 로고
    • Fluorescence: Principles, methodologies, and applications
    • E. Voss, Jr., editor. Uniscience Series. CRC Press, Boca Raton, FL
    • Jameson, D. M. 1984. Fluorescence: principles, methodologies, and applications. In Fluorescein Hapten: An Immunological Probe. E. Voss, Jr., editor. Uniscience Series. CRC Press, Boca Raton, FL. 23-48.
    • (1984) Fluorescein Hapten: An Immunological Probe , pp. 23-48
    • Jameson, D.M.1
  • 20
    • 0003053080 scopus 로고
    • The measurement and analysis of heterogeneous emission by multifrequency phase and modulation fluorometry
    • Jameson, D. M., E. Gratton, and R. D. Hall. 1984. The measurement and analysis of heterogeneous emission by multifrequency phase and modulation fluorometry. Appl. Spectrosc. Rev. 20:55-105.
    • (1984) Appl. Spectrosc. Rev. , vol.20 , pp. 55-105
    • Jameson, D.M.1    Gratton, E.2    Hall, R.D.3
  • 22
    • 0029436215 scopus 로고
    • Application of fluorescence spectroscopy for determining the structure and function of proteins
    • J. N. Herron, W. Jiskoot, and D. J. A. Crommelin, editors. Plenum Press, New York
    • Jiskoot, W., V. Hlady, J. J. Naleway, and J. N. Herron. 1995. Application of fluorescence spectroscopy for determining the structure and function of proteins. In Physical Methods to Characterize Pharmaceutical Proteins. J. N. Herron, W. Jiskoot, and D. J. A. Crommelin, editors. Plenum Press, New York. 1-63.
    • (1995) Physical Methods to Characterize Pharmaceutical Proteins , pp. 1-63
    • Jiskoot, W.1    Hlady, V.2    Naleway, J.J.3    Herron, J.N.4
  • 23
    • 0024421393 scopus 로고
    • Time-resolved fluorescence studies on protoporphyrin IX-apohorseradish peroxidase
    • Jullian, C., J. E. Brunet, V. Thomas, and D. M. Jameson. 1989. Time-resolved fluorescence studies on protoporphyrin IX-apohorseradish peroxidase. Biochim. Biophys. Acta. 997:206-210.
    • (1989) Biochim. Biophys. Acta , vol.997 , pp. 206-210
    • Jullian, C.1    Brunet, J.E.2    Thomas, V.3    Jameson, D.M.4
  • 24
    • 0026714986 scopus 로고
    • Denaturation of human Cu/Zn superoxide dismutase by guanidine hydrochloride: A dynamic fluorescence study
    • Mei, G., N. Rosato, N. Silva, R. Rusch, E. Gratton, I. Savini, and A. Finazzi-Agro. 1992. Denaturation of human Cu/Zn Superoxide dismutase by guanidine hydrochloride: a dynamic fluorescence study. Biochemistry. 31:7224-7230.
    • (1992) Biochemistry , vol.31 , pp. 7224-7230
    • Mei, G.1    Rosato, N.2    Silva, N.3    Rusch, R.4    Gratton, E.5    Savini, I.6    Finazzi-Agro, A.7
  • 25
    • 0028942489 scopus 로고
    • Denaturation of horseradish peroxidase with urea and guanidine hydrochloride
    • Moosavi-Movajedi. A. A., and K. Nazari. 1995. Denaturation of horseradish peroxidase with urea and guanidine hydrochloride. Int. J. Biol. Macromol. 17:43-46.
    • (1995) Int. J. Biol. Macromol. , vol.17 , pp. 43-46
    • Moosavi-Movajedi, A.A.1    Nazari, K.2
  • 27
    • 0027402748 scopus 로고
    • A step towards understanding the folding mechanism of horseradish peroxidase
    • Pappa, H. S., and A. E. G. Cass. 1993. A step towards understanding the folding mechanism of horseradish peroxidase. Eur. J. Biochem. 212: 227-235.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 227-235
    • Pappa, H.S.1    Cass, A.E.G.2
  • 28
    • 0000750037 scopus 로고
    • Four isoperoxidases from horseradish root
    • Paul, K. G., and T. Stigbrand. 1970. Four isoperoxidases from horseradish root. Acta Chem. Scand. 24:3607-3617.
    • (1970) Acta Chem. Scand. , vol.24 , pp. 3607-3617
    • Paul, K.G.1    Stigbrand, T.2
  • 29
    • 0014010578 scopus 로고
    • Peroxidase isoenzymes from horseradish roots
    • Shannon, L. M., E. Kay, and J. Y. Lew. 1966. Peroxidase isoenzymes from horseradish roots. J. Biol. Chem. 241:2166-2172.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2166-2172
    • Shannon, L.M.1    Kay, E.2    Lew, J.Y.3
  • 30
    • 0342950167 scopus 로고
    • Protein fluorescence and conformational substates: The dynamics of human superoxide dismutase
    • Silva, N., G. Mei, and E. Gratton. 1994. Protein fluorescence and conformational substates: the dynamics of human superoxide dismutase. Comm. Mol. Cell. Biophys. 8:217-242.
    • (1994) Comm. Mol. Cell. Biophys. , vol.8 , pp. 217-242
    • Silva, N.1    Mei, G.2    Gratton, E.3
  • 32
    • 84981857769 scopus 로고
    • Measurements of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer
    • Spencer, R. D., and G. Weber. 1969. Measurements of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer. Ann. N.Y. Acad. Sci. 158:361-376.
    • (1969) Ann. N.Y. Acad. Sci. , vol.158 , pp. 361-376
    • Spencer, R.D.1    Weber, G.2
  • 33
    • 36849115843 scopus 로고
    • Influence of Brownian rotations and energy transfer upon the measurements of fluorescence lifetimes
    • Spencer, R. D., and G. Weber. 1970. Influence of Brownian rotations and energy transfer upon the measurements of fluorescence lifetimes. J. Chem. Phys. 52:1654-1663.
    • (1970) J. Chem. Phys. , vol.52 , pp. 1654-1663
    • Spencer, R.D.1    Weber, G.2
  • 34
    • 0015503823 scopus 로고
    • Heme-modification studies on horseradish peroxidase
    • Tamura, M., T. Asakura, and T. Yonetani. 1972. Heme-modification studies on horseradish peroxidase. Biochim. Biophys. Acta. 268: 292-304.
    • (1972) Biochim. Biophys. Acta , vol.268 , pp. 292-304
    • Tamura, M.1    Asakura, T.2    Yonetani, T.3
  • 35
    • 49749199032 scopus 로고
    • Cleavage of the heme-protein link by acid methyl-ethylketone
    • Teale, F. W. J. 1959. Cleavage of the heme-protein link by acid methyl-ethylketone. Biochim. Biophys. Acta. 35:543.
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 36
    • 0019882308 scopus 로고
    • The protoporphyrin-apohorseradish complex as a horseradish peroxidase analog. A fluorimetric study of the heme pocket
    • Ugarova, N. N., A. P. Savitski, and I. V. Berezin. 1981. The protoporphyrin-apohorseradish complex as a horseradish peroxidase analog. A fluorimetric study of the heme pocket. Biochim. Biophys. Acta. 662: 210-219.
    • (1981) Biochim. Biophys. Acta , vol.662 , pp. 210-219
    • Ugarova, N.N.1    Savitski, A.P.2    Berezin, I.V.3
  • 37
    • 0025883412 scopus 로고
    • Oxygen diffusion near the heme binding site of horseradish peroxidase
    • Vargas, V., J. E. Brunet, and D. M. Jameson. 1991. Oxygen diffusion near the heme binding site of horseradish peroxidase. Biochem. Biophys. Res. Commun. 178:104-109.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 104-109
    • Vargas, V.1    Brunet, J.E.2    Jameson, D.M.3
  • 38
    • 0029875017 scopus 로고    scopus 로고
    • Enzymatic and fluorescence studies of four single-tryptophan mutants of rat testis fructose 6-phosphate, 2-kinase: Fructose 2,6-bisphosphatase
    • Watanabe, F., D. M. Jameson, and K. Uyeda. 1996. Enzymatic and fluorescence studies of four single-tryptophan mutants of rat testis fructose 6-phosphate, 2-kinase: fructose 2,6-bisphosphatase. Protein Sci. 5:904-913.
    • (1996) Protein Sci. , vol.5 , pp. 904-913
    • Watanabe, F.1    Jameson, D.M.2    Uyeda, K.3
  • 39
    • 0001320041 scopus 로고
    • Fluorescence polarization spectrum and electronic energy transfer in proteins
    • Weber, G. 1960. Fluorescence polarization spectrum and electronic energy transfer in proteins. Biochem. J. 75:345-352.
    • (1960) Biochem. J. , vol.75 , pp. 345-352
    • Weber, G.1
  • 40
    • 0000878381 scopus 로고
    • Electronic energy transfer in haem proteins
    • Weber, G., and F. W. J. Teale. 1959. Electronic energy transfer in haem proteins. Disc. Faraday Soc. 27:134-141.
    • (1959) Disc. Faraday Soc. , vol.27 , pp. 134-141
    • Weber, G.1    Teale, F.W.J.2
  • 41
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase
    • Welinder, K. G. 1979. Amino acid sequence studies of horseradish peroxidase. Eur. J. Biochem. 96:483-502.
    • (1979) Eur. J. Biochem. , vol.96 , pp. 483-502
    • Welinder, K.G.1
  • 42
    • 0022427616 scopus 로고
    • Plant peroxidases. Their primary, secondary and tertiary structures and relation to cytochrome c peroxidase
    • Welinder, K. G. 1985. Plant peroxidases. Their primary, secondary and tertiary structures and relation to cytochrome c peroxidase. Eur. J. Biochem. 151:497-504.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 497-504
    • Welinder, K.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.