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Volumn 168, Issue 3, 2012, Pages 604-615

Improvement of thermostability and activity of firefly luciferase through [TMG][Ac] ionic liquid mediator

Author keywords

Ionic liquids; Luciferase; Photinus pyralis; Tetramethylguanidine; Thermostability

Indexed keywords

FIREFLY LUCIFERASE; LUCIFERASE; PHOTINUS PYRALIS; TETRAMETHYLGUANIDINE; THERMOSTABILITY; TRIFLOUROACETATE; WILD TYPES;

EID: 84869129106     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-012-9803-8     Document Type: Article
Times cited : (16)

References (42)
  • 1
    • 75849152018 scopus 로고    scopus 로고
    • Firefly luciferase: An adenylate-forming enzyme for multicatalytic functions
    • Inouye, S. (2010). Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions. Cellular and Molecular Life Sciences, 67, 387-404.
    • (2010) Cellular and Molecular Life Sciences , vol.67 , pp. 387-404
    • Inouye, S.1
  • 3
    • 33847266332 scopus 로고    scopus 로고
    • Chemical, biological and evolutionary aspects of beetle bioluminescence
    • Etelvino, J. & Bechara, H. (2007). Chemical, biological and evolutionary aspects of beetle bioluminescence. ARKIVOC, viii, 311-323.
    • (2007) ARKIVOC , vol.8 , pp. 311-323
    • Etelvino, J.1    Bechara, H.2
  • 5
    • 0036865977 scopus 로고    scopus 로고
    • The origin, diversity, and structure function relationships of insect luciferases
    • Viviani, V. R. (2002). The origin, diversity, and structure function relationships of insect luciferases. Cellular and Molecular Life Sciences, 59, 1833-1850.
    • (2002) Cellular and Molecular Life Sciences , vol.59 , pp. 1833-1850
    • Viviani, V.R.1
  • 6
    • 0037431017 scopus 로고    scopus 로고
    • Functional conversion of fatty acyl-CoA synthetase to firefly luciferase by site-directed mutagenesis: A key substitution responsible for luminescence activity
    • Oba, Y., Ojika, M., & Inouye, S. (2003). Functional conversion of fatty acyl-CoA synthetase to firefly luciferase by site-directed mutagenesis: a key substitution responsible for luminescence activity. FEBS Letters, 540, 251-254.
    • (2003) FEBS Letters , vol.540 , pp. 251-254
    • Oba, Y.1    Ojika, M.2    Inouye, S.3
  • 7
    • 0035229251 scopus 로고    scopus 로고
    • Properties of firefly luciferase immobilized through a biotin carboxyl carrier protein domain
    • Eu, J., & Andrade, J. (2001). Properties of firefly luciferase immobilized through a biotin carboxyl carrier protein domain. Luminescence, 16, 57-63.
    • (2001) Luminescence , vol.16 , pp. 57-63
    • Eu, J.1    Andrade, J.2
  • 10
    • 0035965211 scopus 로고    scopus 로고
    • Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin
    • Gomi, K., & Kajiyama, N. (2001). Oxyluciferin, a luminescence product of firefly luciferase, is enzymatically regenerated into luciferin. Journal of Biological Chemistry, 276, 36508-36513.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 36508-36513
    • Gomi, K.1    Kajiyama, N.2
  • 11
    • 34247881853 scopus 로고    scopus 로고
    • The influence of insertion of a critical residue (Arg356) in structure and bioluminescence spectra of firefly luciferase
    • Tafreshi, N. Kh, Hosseinkhani, S., Sadeghizadeh, M., Sadeghi, M., Ranjbar, B., & Naderi-Manesh, H. (2007). The influence of insertion of a critical residue (Arg356) in structure and bioluminescence spectra of firefly luciferase. Journal of Biological Chemistry, 282, 8641-8647.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 8641-8647
    • Kh, T.N.1    Hosseinkhani, S.2    Sadeghizadeh, M.3    Sadeghi, M.4    Ranjbar, B.5    Naderi-Manesh, H.6
  • 12
    • 50649119298 scopus 로고    scopus 로고
    • Kinetics of inhibition of firefly luciferase by oxyluciferin and dehydroluciferyl-adenylate
    • Ribeiro, C., & da Silva, J. C. G. E. (2008). Kinetics of inhibition of firefly luciferase by oxyluciferin and dehydroluciferyl-adenylate. Photochemical & Photobiological Sciences, 7, 1085-1090.
    • (2008) Photochemical & Photobiological Sciences , vol.7 , pp. 1085-1090
    • Ribeiro, C.1    Da Silva, J.C.G.E.2
  • 13
    • 4544325959 scopus 로고    scopus 로고
    • Inhibitory effect of lipoic acid on firefly luciferase bioluminescence
    • Niwa, K., & Ohmiya, Y. (2004). Inhibitory effect of lipoic acid on firefly luciferase bioluminescence. Biochemical and Biophysical Research Communications, 323, 625-629.
    • (2004) Biochemical and Biophysical Research Communications , vol.323 , pp. 625-629
    • Niwa, K.1    Ohmiya, Y.2
  • 14
    • 0037334448 scopus 로고    scopus 로고
    • Method enabling firefly luciferase-based bioluminometric assays at elevated temperatures
    • Eriksson, J., Nordström, T., & Nyrén, P. (2003). Method enabling firefly luciferase-based bioluminometric assays at elevated temperatures. Analytical Biochemistry, 314, 158-161.
    • (2003) Analytical Biochemistry , vol.314 , pp. 158-161
    • Eriksson, J.1    Nordström, T.2    Nyrén, P.3
  • 16
    • 43549103310 scopus 로고    scopus 로고
    • Site-directed mutagenesis of firefly luciferase: Implication of conserved residue(s) in bioluminescence emission spectra among firefly luciferases
    • Tafreshi, N. Kh, Sadeghizadeh, M., Emamzadeh, R., Ranjbar, B., Naderi-Manesh, H., & Hosseinkhani, S. (2008). Site-directed mutagenesis of firefly luciferase: implication of conserved residue(s) in bioluminescence emission spectra among firefly luciferases. Biochemical Journal, 412, 27-33.
    • (2008) Biochemical Journal , vol.412 , pp. 27-33
    • Kh, T.N.1    Sadeghizadeh, M.2    Emamzadeh, R.3    Ranjbar, B.4    Naderi-Manesh, H.5    Hosseinkhani, S.6
  • 18
    • 0037013986 scopus 로고    scopus 로고
    • Improved practical usefulness of firefly luciferase by gene chimerization and random mutagenesis
    • Hirokawa, K., & Kajiyama, N. (2002). Improved practical usefulness of firefly luciferase by gene chimerization and random mutagenesis. Biochimica et Biophysica Acta, 1597, 271-279.
    • (2002) Biochimica et Biophysica Acta , vol.1597 , pp. 271-279
    • Hirokawa, K.1    Kajiyama, N.2
  • 20
    • 34250176165 scopus 로고    scopus 로고
    • Increase in bioluminescence intensity of firefly luciferase using genetic modification
    • Fujii, H., Noda, K., Asami, Y., Kuroda, A., Sakata, M., & Tokida, A. (2007). Increase in bioluminescence intensity of firefly luciferase using genetic modification. Analytical Biochemistry, 366, 131-136.
    • (2007) Analytical Biochemistry , vol.366 , pp. 131-136
    • Fujii, H.1    Noda, K.2    Asami, Y.3    Kuroda, A.4    Sakata, M.5    Tokida, A.6
  • 22
    • 77952106011 scopus 로고    scopus 로고
    • A novel method of protein extraction from yeast using ionic liquid solution
    • Liy, G., Wang, X., Tana, S. N., Tsaic, H. H., Yonga, J.W. H., & Hua, L. (2010). A novel method of protein extraction from yeast using ionic liquid solution. Talanta, 81, 1861-1864.
    • (2010) Talanta , vol.81 , pp. 1861-1864
    • Liy, G.1    Wang, X.2    Tana, S.N.3    Tsaic, H.H.4    Yonga, J.W.H.5    Hua, L.6
  • 24
    • 70849097690 scopus 로고    scopus 로고
    • Effects of structural difference of ionic liquids on the catalysis of horseradish peroxidase
    • Hong, E., Park, J., Yoo, I., & Ryu, K. (2009). Effects of structural difference of ionic liquids on the catalysis of horseradish peroxidase. Journal of Microbiology and Biotechnology, 19, 713-717.
    • (2009) Journal of Microbiology and Biotechnology , vol.19 , pp. 713-717
    • Hong, E.1    Park, J.2    Yoo, I.3    Ryu, K.4
  • 25
    • 63249085417 scopus 로고    scopus 로고
    • Magnetic nanoparticles supported ionic liquids for lipase immobilization: Enzyme activity in catalyzing esterification
    • Jiang, Y., Guo, C., Xia, H., Mahmood, I., Liu, C., & Liu, H. (2009). Magnetic nanoparticles supported ionic liquids for lipase immobilization: Enzyme activity in catalyzing esterification. Journal of Molecular Catalysis B: Enzymatic, 58, 103-109.
    • (2009) Journal of Molecular Catalysis B: Enzymatic , vol.58 , pp. 103-109
    • Jiang, Y.1    Guo, C.2    Xia, H.3    Mahmood, I.4    Liu, C.5    Liu, H.6
  • 27
    • 32644450417 scopus 로고    scopus 로고
    • Brønsted guanidine acid-base ionic liquids: Novel reaction media for the palladium-catalyzed heck reaction
    • Li, S., Lin, Y., Xie, H., Zhang, S., & Xu, J. (2006). Brønsted guanidine acid-base ionic liquids: novel reaction media for the palladium-catalyzed heck reaction. Organic Letters, 8, 391-394.
    • (2006) Organic Letters , vol.8 , pp. 391-394
    • Li, S.1    Lin, Y.2    Xie, H.3    Zhang, S.4    Xu, J.5
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 29
    • 79959841388 scopus 로고    scopus 로고
    • Design of disulfide bridge as an alternative mechanism for color shift in firefly luciferase and development of secreted luciferase
    • Nazari, M., & Hosseinkhani, S. (2011). Design of disulfide bridge as an alternative mechanism for color shift in firefly luciferase and development of secreted luciferase. Photochemical Photobiological Sciences, 10, 1203-1215.
    • (2011) Photochemical Photobiological Sciences , vol.10 , pp. 1203-1215
    • Nazari, M.1    Hosseinkhani, S.2
  • 31
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process
    • Collins, K. D. (2004). Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process. Methods, 34, 300-311.
    • (2004) Methods , vol.34 , pp. 300-311
    • Collins, K.D.1
  • 32
    • 0000743390 scopus 로고
    • Viscosity B-coefficients of ions in solution
    • Jenkins, H. D. W., & Marcus, Y. (1995). Viscosity B-coefficients of ions in solution. Chemical Reviews, 95, 2695-2724.
    • (1995) Chemical Reviews , vol.95 , pp. 2695-2724
    • Jenkins, H.D.W.1    Marcus, Y.2
  • 33
    • 70350225355 scopus 로고    scopus 로고
    • Hofmeister effects: An explanation for the impact of ionic liquids on biocatalysis
    • Yang, Z. (2009). Hofmeister effects: an explanation for the impact of ionic liquids on biocatalysis. Journal of Biotechnology, 144, 12-22.
    • (2009) Journal of Biotechnology , vol.144 , pp. 12-22
    • Yang, Z.1
  • 34
    • 0006479869 scopus 로고
    • Chaotropicions and their interaction with proteins
    • Hanstein, W. G. (1979). Chaotropicions and their interaction with proteins. Journal of Solid-phase Biochemistry, 4, 189-206.
    • (1979) Journal of Solid-phase Biochemistry , vol.4 , pp. 189-206
    • Hanstein, W.G.1
  • 35
    • 34447136294 scopus 로고    scopus 로고
    • Biocatalysis in ionic liquids
    • Rantwijk, F., & Sheldon, R. A. (2007). Biocatalysis in ionic liquids. Chemistry Review, 107, 2757-2785.
    • (2007) Chemistry Review , vol.107 , pp. 2757-2785
    • Rantwijk, F.1    Sheldon, R.A.2
  • 36
    • 49349104098 scopus 로고    scopus 로고
    • Pronounced ionic liquid effect in the synthesis of biologically active isatin-3-oxime derivatives under acid catalysis
    • Pinto, A. C., Moreira Lapis, A. A., Silva, B. V. D., Bastos, R. S., Dupont, J., & Neto, B. A. D. (2008). Pronounced ionic liquid effect in the synthesis of biologically active isatin-3-oxime derivatives under acid catalysis. Tetrahedron Letters, 49, 5639-5641.
    • (2008) Tetrahedron Letters , vol.49 , pp. 5639-5641
    • Pinto, A.C.1    Moreira Lapis, A.A.2    Silva, B.V.D.3    Bastos, R.S.4    Dupont, J.5    Neto, B.A.D.6
  • 37
    • 79953320824 scopus 로고    scopus 로고
    • Ionic liquids in biotransformations: From proof-of-concept to emerging deep-eutectic-solvents
    • Maria, P. D. D., & Maugeri, Z. (2011). Ionic liquids in biotransformations: from proof-of-concept to emerging deep-eutectic-solvents. Current Opinion in Chemical Biology, 15, 220-225.
    • (2011) Current Opinion in Chemical Biology , vol.15 , pp. 220-225
    • Maria, P.D.D.1    Maugeri, Z.2
  • 38
    • 53649084467 scopus 로고    scopus 로고
    • Effect of Hofmeister ions on protein thermal stability: Roles of ion hydration and peptide groups?
    • Sedlák, E., Stagg, L., & Wittung-Stafshede, P. (2008). Effect of Hofmeister ions on protein thermal stability: roles of ion hydration and peptide groups? Archives of Biochemistry and Biophysics, 479, 69-73.
    • (2008) Archives of Biochemistry and Biophysics , vol.479 , pp. 69-73
    • Sedlák, E.1    Stagg, L.2    Wittung-Stafshede, P.3
  • 39
    • 38349164736 scopus 로고    scopus 로고
    • Supported ionic liquid enzymatic catalysis for the production of biodiesel
    • Gamba, M., Lapis, A. A. M., & Dupont, J. (2008). Supported ionic liquid enzymatic catalysis for the production of biodiesel. Advanced Synthesis and Catalysis, 350, 160-164.
    • (2008) Advanced Synthesis and Catalysis , vol.350 , pp. 160-164
    • Gamba, M.1    Lapis, A.A.M.2    Dupont, J.3
  • 40
    • 77955269306 scopus 로고    scopus 로고
    • RACE-based amplification of cDNA and expression of a luciferin- regenerating enzyme (LRE): An attempt towards persistent bioluminescent signal
    • Emamzadeh, R., Hosseinkhani, S., Hemati, R., & Sadeghizadeh, M. (2010). RACE-based amplification of cDNA and expression of a luciferin-regenerating enzyme (LRE): An attempt towards persistent bioluminescent signal. Enzyme Microbial Technology, 47, 159-165.
    • (2010) Enzyme Microbial Technology , vol.47 , pp. 159-165
    • Emamzadeh, R.1    Hosseinkhani, S.2    Hemati, R.3    Sadeghizadeh, M.4
  • 42
    • 79953720833 scopus 로고    scopus 로고
    • Molecular enigma of multicolor bioluminescence of firefly luciferase
    • Hosseinkhani, S. (2010). Molecular enigma of multicolor bioluminescence of firefly luciferase. Cellular and Molecular Life Sciences, 68, 1167-1182.
    • (2010) Cellular and Molecular Life Sciences , vol.68 , pp. 1167-1182
    • Hosseinkhani, S.1


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