메뉴 건너뛰기




Volumn 1784, Issue 11, 2008, Pages 1493-1500

Unraveling the mechanisms of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia

Author keywords

Aromatic interaction; Giardia; Glycolysis; Quenching; Spectroscopy; Triosephosphate isomerase; Tryptophan environment

Indexed keywords

PHENYLALANINE; TRIOSEPHOSPHATE ISOMERASE; TRYPTOPHAN;

EID: 54049151142     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.05.016     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0000944228 scopus 로고
    • Fluorescence-polarization spectrum and electronic energy transfer in tyrosine, tryptophan and related compounds
    • Weber G. Fluorescence-polarization spectrum and electronic energy transfer in tyrosine, tryptophan and related compounds. Biochem. J. 75 (1960) 335-345
    • (1960) Biochem. J. , vol.75 , pp. 335-345
    • Weber, G.1
  • 2
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem J.M., and Brand L. Time-resolved fluorescence of proteins. Annu. Rev. Biochem. 54 (1985) 43-71
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 3
    • 0025929570 scopus 로고
    • Fluorescence techniques for studding protein structure
    • Eftink M.R. Fluorescence techniques for studding protein structure. Methods Biochem. Anal. 35 (1991) 127-205
    • (1991) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 5
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • Wiley, Chichester
    • Ladokhin A.S. Fluorescence spectroscopy in peptide and protein analysis. Encyclopedia of Analytical Chemistry (2000), Wiley, Chichester 5762-5779
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762-5779
    • Ladokhin, A.S.1
  • 6
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian J.T., and Callis P.R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80 (2001) 2093-2109
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 7
    • 0017883676 scopus 로고
    • Relationship of thermal quenching of protein fluorescence to intramolecular structural mobility
    • Bushueva T.L., Busel E.P., and Burstein E.A. Relationship of thermal quenching of protein fluorescence to intramolecular structural mobility. Biochim. Biophys. Acta 534 (1978) 141-152
    • (1978) Biochim. Biophys. Acta , vol.534 , pp. 141-152
    • Bushueva, T.L.1    Busel, E.P.2    Burstein, E.A.3
  • 8
    • 0030965949 scopus 로고    scopus 로고
    • Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II
    • Jonasson P., Arosson G., Carlsson U., and Jonsson B.H. Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II. Biochemistry 36 (1997) 5142-5148
    • (1997) Biochemistry , vol.36 , pp. 5142-5148
    • Jonasson, P.1    Arosson, G.2    Carlsson, U.3    Jonsson, B.H.4
  • 9
    • 0032817737 scopus 로고    scopus 로고
    • Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase
    • Prompers J.J., Hilbers C.W., and Pepermans H.A.M. Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase. FEBS Lett. 456 (1999) 409-416
    • (1999) FEBS Lett. , vol.456 , pp. 409-416
    • Prompers, J.J.1    Hilbers, C.W.2    Pepermans, H.A.M.3
  • 10
    • 24044451239 scopus 로고    scopus 로고
    • Implication of a critical residue (Glu175) in structure and function of bacterial luciferase
    • Madvar A.R., Hosseinkhani S., Khajeh K., Ranjbar B., and Asoodeh A. Implication of a critical residue (Glu175) in structure and function of bacterial luciferase. FEBS Lett. 579 (2005) 4701-4706
    • (2005) FEBS Lett. , vol.579 , pp. 4701-4706
    • Madvar, A.R.1    Hosseinkhani, S.2    Khajeh, K.3    Ranjbar, B.4    Asoodeh, A.5
  • 11
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y., and Barkley M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry 37 (1998) 9976-9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 12
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: a mechanism of protein structure stabilization
    • Burley S.K., and Petsko G.A. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229 (1985) 23-28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 13
    • 0022450133 scopus 로고
    • Amino-aromatic interaction in proteins
    • Burley S.K., and Petsko G.A. Amino-aromatic interaction in proteins. FEBS Lett. 203 (1986) 139-143
    • (1986) FEBS Lett. , vol.203 , pp. 139-143
    • Burley, S.K.1    Petsko, G.A.2
  • 15
    • 0030909560 scopus 로고    scopus 로고
    • Immunosuppressor binding to theimmunophilin FKBP59 affects the local structural dynamics of a surface beta-strand: time-resolved fluorescence study
    • Rouviere N., Vincent M., Craescu C.T., and Gallay J. Immunosuppressor binding to theimmunophilin FKBP59 affects the local structural dynamics of a surface beta-strand: time-resolved fluorescence study. Biochemistry 36 (1997) 7339-7352
    • (1997) Biochemistry , vol.36 , pp. 7339-7352
    • Rouviere, N.1    Vincent, M.2    Craescu, C.T.3    Gallay, J.4
  • 16
    • 0034237284 scopus 로고    scopus 로고
    • Aromatic interaction in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan
    • Nanda V., and Brand L. Aromatic interaction in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan. Proteins 40 (2000) 112-125
    • (2000) Proteins , vol.40 , pp. 112-125
    • Nanda, V.1    Brand, L.2
  • 17
    • 0035877733 scopus 로고    scopus 로고
    • Aromatic amino acids are criticalfor stability of the bicoid homeodomain
    • Subramaniam V., Jovin T.M., and Rivera-Pomar R.V. Aromatic amino acids are criticalfor stability of the bicoid homeodomain. J. Biol. Chem. 276 (2001) 21506-21511
    • (2001) J. Biol. Chem. , vol.276 , pp. 21506-21511
    • Subramaniam, V.1    Jovin, T.M.2    Rivera-Pomar, R.V.3
  • 19
    • 0029954416 scopus 로고    scopus 로고
    • Deterministic pressure dissociation and unfolding of triosephosphate isomerasa: persistent heterogeneity of a protein dimmer
    • Rietveld A.W.M., and Ferreira S.T. Deterministic pressure dissociation and unfolding of triosephosphate isomerasa: persistent heterogeneity of a protein dimmer. Biochemistry 35 (1999) 7743-7751
    • (1999) Biochemistry , vol.35 , pp. 7743-7751
    • Rietveld, A.W.M.1    Ferreira, S.T.2
  • 20
    • 0030850229 scopus 로고    scopus 로고
    • Disecction of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermopilic bacterium Thermotoga maritime: design and characterization of the separate triosephosphate isomerasa
    • Beaucamp N., Hofmann A., Kellerer B., and Jaenicke R. Disecction of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermopilic bacterium Thermotoga maritime: design and characterization of the separate triosephosphate isomerasa. Protein Sci. 6 (1997) 2159-2165
    • (1997) Protein Sci. , vol.6 , pp. 2159-2165
    • Beaucamp, N.1    Hofmann, A.2    Kellerer, B.3    Jaenicke, R.4
  • 21
    • 0033524469 scopus 로고    scopus 로고
    • Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant
    • Gokhale R.S., Ray S.S., Balaram H., and Balaram P. Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant. Biochemistry 38 (1999) 423-431
    • (1999) Biochemistry , vol.38 , pp. 423-431
    • Gokhale, R.S.1    Ray, S.S.2    Balaram, H.3    Balaram, P.4
  • 22
    • 0034111423 scopus 로고    scopus 로고
    • The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triosephosphate isomerasa
    • Lambeir M., Backmann J., Ruiz-Sanz J., Filimonov V., Nielsen J.E., Kursula I., Norledge B.V., and Wierenga R.K. The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triosephosphate isomerasa. Eur. J. Biochem. 267 (2000) 2516-2524
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2516-2524
    • Lambeir, M.1    Backmann, J.2    Ruiz-Sanz, J.3    Filimonov, V.4    Nielsen, J.E.5    Kursula, I.6    Norledge, B.V.7    Wierenga, R.K.8
  • 23
    • 0034733388 scopus 로고    scopus 로고
    • A compact monomeric intermediate identified by NMR in the denaturation of dimeric triosephosphate isomerse
    • Morgan C.J., Wilkins D.K., Smith L.J., Kawata Y., and Dobson C.M. A compact monomeric intermediate identified by NMR in the denaturation of dimeric triosephosphate isomerse. J. Mol. Biol. 300 (2000) 11-16
    • (2000) J. Mol. Biol. , vol.300 , pp. 11-16
    • Morgan, C.J.1    Wilkins, D.K.2    Smith, L.J.3    Kawata, Y.4    Dobson, C.M.5
  • 26
    • 0037444807 scopus 로고    scopus 로고
    • Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme
    • Najera H., Costas M., and Fernández-Velasco D.A. Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme. Biochem. J. 370 (2003) 785-792
    • (2003) Biochem. J. , vol.370 , pp. 785-792
    • Najera, H.1    Costas, M.2    Fernández-Velasco, D.A.3
  • 27
    • 0346365102 scopus 로고    scopus 로고
    • Persistent conformational heterogeneity of triosephosphate isomerase: separation and characterization of conformational isomers in solution
    • Moreau V.H., Rietveld A.W.M., and Ferreira S.T. Persistent conformational heterogeneity of triosephosphate isomerase: separation and characterization of conformational isomers in solution. Biochemistry 42 (2003) 14831-14837
    • (2003) Biochemistry , vol.42 , pp. 14831-14837
    • Moreau, V.H.1    Rietveld, A.W.M.2    Ferreira, S.T.3
  • 29
    • 23844433968 scopus 로고    scopus 로고
    • Reversible equilibrium unfolding of triosephosphate isomerase from Trypanosoma cruzi in guanidinium hydrochloride involves stable dimeric and monomeric intermediates
    • Chánez-Cárdenas M.E., Pérez-Hernández G., Sánchez-Rebollar B.G., Costas M., and Vázquez-Contreras E. Reversible equilibrium unfolding of triosephosphate isomerase from Trypanosoma cruzi in guanidinium hydrochloride involves stable dimeric and monomeric intermediates. Biochemistry 44 (2005) 10883-10892
    • (2005) Biochemistry , vol.44 , pp. 10883-10892
    • Chánez-Cárdenas, M.E.1    Pérez-Hernández, G.2    Sánchez-Rebollar, B.G.3    Costas, M.4    Vázquez-Contreras, E.5
  • 32
    • 0037293775 scopus 로고    scopus 로고
    • Unusual fluorescence of W168 in Plasmodium falciparum triosephosphate isomerase, probed by single-tryptophan mutants
    • Pattanaik P., Ravindra G., Sengupta C., Maithal K., Balaram P., and Balaram H. Unusual fluorescence of W168 in Plasmodium falciparum triosephosphate isomerase, probed by single-tryptophan mutants. Eur. J. Biochem. 270 (2003) 745-756
    • (2003) Eur. J. Biochem. , vol.270 , pp. 745-756
    • Pattanaik, P.1    Ravindra, G.2    Sengupta, C.3    Maithal, K.4    Balaram, P.5    Balaram, H.6
  • 33
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 35
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace N.C., Vajdos F., Fee L., Grimsley G., and Gray V. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, N.C.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, V.5
  • 36
    • 0025912338 scopus 로고
    • Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors
    • Hubbard S.J., Campbell S.F., and Thornton J.M. Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. J. Mol. Biol. 220 (1991) 507-530
    • (1991) J. Mol. Biol. , vol.220 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 37
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chotia. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105 (1976) 1-14
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-14
    • Chotia1
  • 38
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 40
    • 0024259064 scopus 로고
    • Red-edged-excitation fluorescence spectroscopy of single-tryptophan proteins
    • Demchenko A.P. Red-edged-excitation fluorescence spectroscopy of single-tryptophan proteins. Eur. Biophys. J. 16 (1988) 121-129
    • (1988) Eur. Biophys. J. , vol.16 , pp. 121-129
    • Demchenko, A.P.1
  • 41
    • 54049158665 scopus 로고
    • Intramolecular proton transfer quenching in tryptophan and tryptamine: temperature dependence
    • Lakowicz J.R. (Ed), SPIE, USA
    • Eftink M.R., and Hu D. Intramolecular proton transfer quenching in tryptophan and tryptamine: temperature dependence. In: Lakowicz J.R. (Ed). Time-Resolved Laser Spectroscopy in Biochemistry IV (1994), SPIE, USA 384-389
    • (1994) Time-Resolved Laser Spectroscopy in Biochemistry IV , pp. 384-389
    • Eftink, M.R.1    Hu, D.2
  • 42
    • 33745512491 scopus 로고    scopus 로고
    • Short range photoinduced electron transfer in proteins: QM-MM simulations of tryptophan and flavin fluorescence quenching in proteins
    • Callis P.R., and Liu T. Short range photoinduced electron transfer in proteins: QM-MM simulations of tryptophan and flavin fluorescence quenching in proteins. Chem. Phys. 326 (2006) 230-239
    • (2006) Chem. Phys. , vol.326 , pp. 230-239
    • Callis, P.R.1    Liu, T.2
  • 43
    • 0001598267 scopus 로고
    • Quenching interaction and non-exponential decay:tryptophan 138 of bacteriophage T4 lysozyme
    • Gilst M.V., Tang C., Roth A., and Hudson B. Quenching interaction and non-exponential decay:tryptophan 138 of bacteriophage T4 lysozyme. J. Fluorescence 4 (1994) 203-207
    • (1994) J. Fluorescence , vol.4 , pp. 203-207
    • Gilst, M.V.1    Tang, C.2    Roth, A.3    Hudson, B.4
  • 44
    • 0018271712 scopus 로고
    • Proximity relationships of tryptophanyl residues and oxygen binding site in Levantina hierosolima hemocyanin. A fluorimetric study
    • Shaklai N., Gafni A., and Daniel E. Proximity relationships of tryptophanyl residues and oxygen binding site in Levantina hierosolima hemocyanin. A fluorimetric study. Biochemistry 17 (1978) 4438-4442
    • (1978) Biochemistry , vol.17 , pp. 4438-4442
    • Shaklai, N.1    Gafni, A.2    Daniel, E.3
  • 45
    • 0025741701 scopus 로고
    • Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence
    • Loewenthal R., Sancho J., and Fersht A.R. Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence. Biochemistry 30 (1991) 6775-6779
    • (1991) Biochemistry , vol.30 , pp. 6775-6779
    • Loewenthal, R.1    Sancho, J.2    Fersht, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.