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Volumn 5, Issue 11, 1996, Pages 2248-2254

Probing the structure and mobility of Pseudomonas aeruginosa azurin by circular dichroism and dynamic fluorescence anisotropy

Author keywords

entatic state; fluorescence lifetime distribution; site directed mutagenesis; solvent relaxation; tryptophan

Indexed keywords

METALLOPROTEIN;

EID: 0029833191     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051111     Document Type: Article
Times cited : (21)

References (35)
  • 2
    • 0038131900 scopus 로고
    • Fluorescence spectroscopy data analysis environment: A second generation global analysis program
    • Beechem JM, Gratton E. 1988. Fluorescence spectroscopy data analysis environment: A second generation global analysis program. Proc SPIE-Int Soc Opt Eng 909:70-81.
    • (1988) Proc SPIE-Int Soc Opt Eng , vol.909 , pp. 70-81
    • Beechem, J.M.1    Gratton, E.2
  • 3
    • 0023130391 scopus 로고
    • Cloning and sequencing of the azurin gene from Pseudomonas aeruginosa
    • Canters GW. 1987. Cloning and sequencing of the azurin gene from Pseudomonas aeruginosa. FEBS Lett 212:168-172.
    • (1987) FEBS Lett , vol.212 , pp. 168-172
    • Canters, G.W.1
  • 4
    • 0020483945 scopus 로고
    • Evolution of proteins formed by beta-sheets. 1. Plastocyanin and azurin
    • Chothia C, Lesk AM. 1982. Evolution of proteins formed by beta-sheets. 1. Plastocyanin and azurin. J Mol Biol 160:309-323.
    • (1982) J Mol Biol , vol.160 , pp. 309-323
    • Chothia, C.1    Lesk, A.M.2
  • 5
    • 0028327178 scopus 로고
    • Conformational dynamics of bovine Cu, Zn superoxide dismutase revealed by time-resolved fluorescence spectroscopy of me single tyrosine residue
    • Ferreira S, Stella L, Gratton E. 1994. Conformational dynamics of bovine Cu, Zn superoxide dismutase revealed by time-resolved fluorescence spectroscopy of me single tyrosine residue. Biophys J 66:1185-1196.
    • (1994) Biophys J , vol.66 , pp. 1185-1196
    • Ferreira, S.1    Stella, L.2    Gratton, E.3
  • 8
    • 0028345259 scopus 로고
    • Unique environment of Trp 48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy
    • Gilardi G, Mei G, Rosato N, Canters GW, Finazzi Agró A. 1994 Unique environment of Trp 48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy. Biochemistry 33:1425-1432.
    • (1994) Biochemistry , vol.33 , pp. 1425-1432
    • Gilardi, G.1    Mei, G.2    Rosato, N.3    Canters, G.W.4    Finazzi Agró, A.5
  • 10
    • 0029916957 scopus 로고    scopus 로고
    • X-ray crystal structure of the two site-specific mutants Ile 7 Ser and Phe 110 Ser of azurin from Pseudomonas aeruginosa
    • Hammann C, Messerschmidt A, Huber R, Nar H, Gilardi G, Canters GW. 1996. X-ray crystal structure of the two site-specific mutants Ile 7 Ser and Phe 110 Ser of azurin from Pseudomonas aeruginosa. J Mol Biol 255:362-366.
    • (1996) J Mol Biol , vol.255 , pp. 362-366
    • Hammann, C.1    Messerschmidt, A.2    Huber, R.3    Nar, H.4    Gilardi, G.5    Canters, G.W.6
  • 11
    • 0039097356 scopus 로고
    • Purification and properties of cytochrome oxidase from Pseudomonas aeruginosa
    • Horio T, Higashi T, Yamanaka T, Matsubara H, Okunuki K. 1961. Purification and properties of cytochrome oxidase from Pseudomonas aeruginosa. J Biol Chem 236:944-951.
    • (1961) J Biol Chem , vol.236 , pp. 944-951
    • Horio, T.1    Higashi, T.2    Yamanaka, T.3    Matsubara, H.4    Okunuki, K.5
  • 12
    • 0024504824 scopus 로고
    • Confirmation that multiexponential fluorescence decay behavior of holoazurin originates from conformational heterogeneity
    • Hutnik CM, Szabo AG. 1989a. Confirmation that multiexponential fluorescence decay behavior of holoazurin originates from conformational heterogeneity. Biochemistry 28:3923-3934.
    • (1989) Biochemistry , vol.28 , pp. 3923-3934
    • Hutnik, C.M.1    Szabo, A.G.2
  • 13
    • 0024580265 scopus 로고
    • A time-resolved fluorescence study of azurin and metalloazurin derivatives
    • Hutnik CM, Szabo AG. 1989b. A time-resolved fluorescence study of azurin and metalloazurin derivatives. Biochemistry 28:3935-3939.
    • (1989) Biochemistry , vol.28 , pp. 3935-3939
    • Hutnik, C.M.1    Szabo, A.G.2
  • 14
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim PS, Baldwin RL. 1982. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem 51:459-489.
    • (1982) Annu Rev Biochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 15
    • 0019201754 scopus 로고
    • Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes
    • Lipari G, Szabo A. 1980. Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes. Biophys J 30:489-506.
    • (1980) Biophys J , vol.30 , pp. 489-506
    • Lipari, G.1    Szabo, A.2
  • 16
    • 0024464461 scopus 로고
    • Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor
    • Manning MC, Woody RW. 1989. Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. Biochemistry 28:8609-8613.
    • (1989) Biochemistry , vol.28 , pp. 8609-8613
    • Manning, M.C.1    Woody, R.W.2
  • 17
    • 0026714986 scopus 로고
    • Denaturation of human Cu/Zn superoxide dismutase by guanidine hydrochloride: A dynamic fluorescence study
    • Mei G, Rosato N, Silva N, Rusch R, Gratton E, Savini I, Finazzi Agró A. 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 Agró, A.7
  • 18
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0
    • Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW. 1991. Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. J Mol Biol 221:765-772.
    • (1991) J Mol Biol , vol.221 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 19
    • 0026642328 scopus 로고
    • Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 Å resolution
    • Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW. 1992. Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 Å resolution. FEBS Lett 306:119-124.
    • (1992) FEBS Lett , vol.306 , pp. 119-124
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 20
    • 0017157155 scopus 로고
    • A purification procedure for the soluble cytochrome oxidase and some other respiratory proteins from Pseudomonas aeruginosa
    • Parr SR, Barber D, Greenwood C, Phillips BW, Melling J. 1976. A purification procedure for the soluble cytochrome oxidase and some other respiratory proteins from Pseudomonas aeruginosa. Biochem J 157:423-430.
    • (1976) Biochem J , vol.157 , pp. 423-430
    • Parr, S.R.1    Barber, D.2    Greenwood, C.3    Phillips, B.W.4    Melling, J.5
  • 21
    • 0023659379 scopus 로고
    • Internal motion and electron transfer in proteins: A picosecond fluorescence study of three homologous azurins
    • Petrich JW, Longworth JW, Fleming GR. 1987. Internal motion and electron transfer in proteins: A picosecond fluorescence study of three homologous azurins. Biochemistry 26:2711-2722.
    • (1987) Biochemistry , vol.26 , pp. 2711-2722
    • Petrich, J.W.1    Longworth, J.W.2    Fleming, G.R.3
  • 22
    • 0024284014 scopus 로고
    • 5′-3′ exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis
    • Sayers JR, Schmidt W, Eckstein F. 1988. 5′-3′ exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis. Nucleic Acids Res 16:791-802.
    • (1988) Nucleic Acids Res , vol.16 , pp. 791-802
    • Sayers, J.R.1    Schmidt, W.2    Eckstein, F.3
  • 24
    • 0001200103 scopus 로고
    • Spectroscopic studies of stellacyanin, plastocyanin and azurin. Electronic structure of the blue copper sites
    • Solomon EI, Hare JW, Dooley DM, Dawson JH, Stephens PJ, Gray HB. 1980. Spectroscopic studies of stellacyanin, plastocyanin and azurin. Electronic structure of the blue copper sites. J Am Chem Soc 102:168-178.
    • (1980) J Am Chem Soc , vol.102 , pp. 168-178
    • Solomon, E.I.1    Hare, J.W.2    Dooley, D.M.3    Dawson, J.H.4    Stephens, P.J.5    Gray, H.B.6
  • 26
    • 0001252358 scopus 로고
    • Fluorescence anisotropy: Theory and applications
    • Lakowicz JR, ed. New York. Plenum Press
    • Steiner RF. 1983. Fluorescence anisotropy: Theory and applications. In. Lakowicz JR, ed. Principles of fluorescence spectroscopy. New York. Plenum Press.
    • (1983) Principles of Fluorescence Spectroscopy
    • Steiner, R.F.1
  • 27
    • 0015997959 scopus 로고
    • Aromatic contribution to circular dichroism spectra of proteins
    • Strickland EH. 1974. Aromatic contribution to circular dichroism spectra of proteins. CRC Crit Rev Biochem 2:113-175.
    • (1974) CRC Crit Rev Biochem , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 28
    • 0013440731 scopus 로고
    • UV resonance raman examination of the azurin tryptophan environment and energy relaxation pathways
    • Sweeney JA, Harmon PA, Asher SA, Hutnik CM, Szabo AG. 1991. UV resonance raman examination of the azurin tryptophan environment and energy relaxation pathways. J Am Chem Soc 113:7531-7537.
    • (1991) J Am Chem Soc , vol.113 , pp. 7531-7537
    • Sweeney, J.A.1    Harmon, P.A.2    Asher, S.A.3    Hutnik, C.M.4    Szabo, A.G.5
  • 29
    • 0020730977 scopus 로고
    • Conformational heterogeneity of the copper binding site in azurin
    • Szabo AG, Stepanik TM, Wayner DM, Young NM. 1983. Conformational heterogeneity of the copper binding site in azurin. Biophys J 41:233-244.
    • (1983) Biophys J , vol.41 , pp. 233-244
    • Szabo, A.G.1    Stepanik, T.M.2    Wayner, D.M.3    Young, N.M.4
  • 30
    • 0344300566 scopus 로고
    • Analysis of protein structure by circular dichroism spectroscopy Purdic N, Brittain HG, eds
    • Amsterdam: Elsevier
    • Towell JF III, Manning MC. 1994. Analysis of protein structure by circular dichroism spectroscopy In: Purdic N, Brittain HG, eds. Analytical applications of circular dichroism Amsterdam: Elsevier. pp 175-205.
    • (1994) Analytical Applications of Circular Dichroism , pp. 175-205
    • Towell III, J.F.1    Manning, M.C.2
  • 31
    • 0025252558 scopus 로고
    • Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome-C551 and nitrite reductase
    • van de Kamp M, Silvestrini MC, Brunori M, van Beeumen J, Hali FC, Canters GW. 1990. Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome-C551 and nitrite reductase. Eur J Biochem 194:109-118.
    • (1990) Eur J Biochem , vol.194 , pp. 109-118
    • Van De Kamp, M.1    Silvestrini, M.C.2    Brunori, M.3    Van Beeumen, J.4    Hali, F.C.5    Canters, G.W.6
  • 32
    • 0027527209 scopus 로고
    • Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
    • Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. 1993. Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains. Biochemistry 32:10303-10313.
    • (1993) Biochemistry , vol.32 , pp. 10303-10313
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.R.4
  • 33
    • 0028822917 scopus 로고
    • Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins
    • Williams RJP. 1995. Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. Eur J Biochem 234:363-381.
    • (1995) Eur J Biochem , vol.234 , pp. 363-381
    • Williams, R.J.P.1
  • 34
    • 0017822448 scopus 로고
    • Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins
    • Woody RW. 1978. Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins. Biopolymers 17:1451-1467.
    • (1978) Biopolymers , vol.17 , pp. 1451-1467
    • Woody, R.W.1
  • 35
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody RW. 1994. Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur Biophys J 23:253-262.
    • (1994) Eur Biophys J , vol.23 , pp. 253-262
    • Woody, R.W.1


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