메뉴 건너뛰기




Volumn 43, Issue 50, 2004, Pages 15975-15982

Identity of the emitter in the bacterial luciferase luminescence reaction: Binding and fluorescence quantum yield studies of 5-decyl-4a-hydroxy-4a,5- dihydroriboflavin-5′-phosphate as a model

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLUMINESCENCE; CHEMILUMINESCENCE; COMPLEXATION; FLUORESCENCE; MUTAGENESIS; QUANTUM THEORY;

EID: 10844242140     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0480640     Document Type: Article
Times cited : (34)

References (42)
  • 1
    • 0022862648 scopus 로고
    • Bacterial luciferase: A carbon-13, nitrogen-15, and phosphorus-31 nuclear magnetic resonance investigation
    • Vervoort, J., Müller, F., O'Kane, D. J., Lee, J., and Bacher, A. (1986) Bacterial luciferase: A carbon-13, nitrogen-15, and phosphorus-31 nuclear magnetic resonance investigation, Biochemistry 25, 8067-8075.
    • (1986) Biochemistry , vol.25 , pp. 8067-8075
    • Vervoort, J.1    Müller, F.2    O'Kane, D.J.3    Lee, J.4    Bacher, A.5
  • 2
    • 0015714135 scopus 로고
    • Spectral properties of an oxygenated luciferase-flavin intermediate isolated by low-temperature chromatography
    • Hastings, J. W., Balny, C., LePeuch, C., and Douzou, P. (1973) Spectral properties of an oxygenated luciferase-flavin intermediate isolated by low-temperature chromatography, Proc. Natl. Acad. Sci. U.S.A. 70, 3468-3472.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 3468-3472
    • Hastings, J.W.1    Balny, C.2    LePeuch, C.3    Douzou, P.4
  • 3
    • 0016703679 scopus 로고
    • Fluorescence and bioluminescence of bacterial luciferase intermediates
    • Balny, C., and Hastings, J. W. (1975) Fluorescence and bioluminescence of bacterial luciferase intermediates, Biochemistry 14, 4719-4723.
    • (1975) Biochemistry , vol.14 , pp. 4719-4723
    • Balny, C.1    Hastings, J.W.2
  • 4
    • 0016760334 scopus 로고
    • The oxygenated bacterial luciferase-flavin intermediate. Reaction products via the light and dark pathways
    • Hastings, J. W., and Balny, C. (1975) The oxygenated bacterial luciferase-flavin intermediate. Reaction products via the light and dark pathways, J. Biol. Chem. 250, 7288-7293.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7288-7293
    • Hastings, J.W.1    Balny, C.2
  • 5
    • 0018801599 scopus 로고
    • Isolation and properties of bacterial luciferase-oxygenated flavin intermediate complexed with long-chain alcohols
    • Tu, S.-C. (1979) Isolation and properties of bacterial luciferase-oxygenated flavin intermediate complexed with long-chain alcohols, Biochemistry 18, 5940-5945.
    • (1979) Biochemistry , vol.18 , pp. 5940-5945
    • Tu, S.-C.1
  • 6
    • 0020478798 scopus 로고
    • Isolation and properties of bacterial luciferase intermediates containing different oxygenated flavins
    • Tu, S.-C. (1982) Isolation and properties of bacterial luciferase intermediates containing different oxygenated flavins, J. Biol. Chem. 257, 3719-3725.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3719-3725
    • Tu, S.-C.1
  • 7
    • 0022863121 scopus 로고
    • Identifications of the true carbon-13 nuclear magnetic resonance spectrum of the stable intermediate II in bacterial luciferase
    • Vervoort, J., Muller, F., Lee, J., van den Berg, W. A. M., and Moonen, C. T. W. (1986) Identifications of the true carbon-13 nuclear magnetic resonance spectrum of the stable intermediate II in bacterial luciferase, Biochemistry 25, 8062-8067.
    • (1986) Biochemistry , vol.25 , pp. 8062-8067
    • Vervoort, J.1    Muller, F.2    Lee, J.3    Van Den Berg, W.A.M.4    Moonen, C.T.W.5
  • 8
    • 0000374069 scopus 로고
    • Simple synthesis of a 4a-hydroperoxy adduct of a 1,5-dihydroflavine: Preliminary studies of a model for bacterial luciferase
    • Kemal, C., and Bruice, T. C. (1976) Simple synthesis of a 4a-hydroperoxy adduct of a 1,5-dihydroflavine: Preliminary studies of a model for bacterial luciferase, Proc. Natl. Acad. Sci. U.S.A. 73, 995-999.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 995-999
    • Kemal, C.1    Bruice, T.C.2
  • 9
    • 0027716533 scopus 로고
    • Spectral detection of an intermediate preceding the excited state in the bacterial luciferase reaction
    • Macheroux, P., Ghisla, S., and Hastings, J. W. (1993) Spectral detection of an intermediate preceding the excited state in the bacterial luciferase reaction, Biochemistry 32, 14183-14186.
    • (1993) Biochemistry , vol.32 , pp. 14183-14186
    • Macheroux, P.1    Ghisla, S.2    Hastings, J.W.3
  • 10
    • 0011997142 scopus 로고
    • On the role of some flavin adducts as one-electron donors
    • Bray, R. C., Engel, P. C., and Mayhew, S. G., Eds. Water de Gruyter and Co., Berlin, Germany
    • Mager, H. I. X., and Addink, R. (1984) On the role of some flavin adducts as one-electron donors, in Flavins and Flavoproteins (Bray, R. C., Engel, P. C., and Mayhew, S. G., Eds.) pp 37-40, Water de Gruyter and Co., Berlin, Germany.
    • (1984) Flavins and Flavoproteins , pp. 37-40
    • Mager, H.I.X.1    Addink, R.2
  • 11
    • 0003636920 scopus 로고
    • Studies on the bacterial luciferase reaction: Isotope effects on the light emission. Is a "CIEEL" mechanism involved?
    • Bray, R. C., Engel, P. C., and Mayhew, S. G., Eds. Water de Gruyter and Co., Berlin, Germany
    • Macheroux, P., Ghisla, S., Kurfürst, M., and Hastings, J. W. (1984) Studies on the bacterial luciferase reaction: Isotope effects on the light emission. Is a "CIEEL" mechanism involved?, in Flavins and Flavoproteins (Bray, R. C., Engel, P. C., and Mayhew, S. G., Eds.) pp 669-672, Water de Gruyter and Co., Berlin, Germany.
    • (1984) Flavins and Flavoproteins , pp. 669-672
    • Macheroux, P.1    Ghisla, S.2    Kurfürst, M.3    Hastings, J.W.4
  • 12
    • 0002379597 scopus 로고
    • One-electron transfers in flavin systems: Relevance to the postulated CIEEL mechanism in bacterial bioluminescence
    • Edmondson, D. E., and McCormick, D. B., Eds. Water de Gruyter and Co., Berlin, Germany
    • Mager, H. I. X., and Tu, S.-C. (1987) One-electron transfers in flavin systems: Relevance to the postulated CIEEL mechanism in bacterial bioluminescence, in Flavins and Flavoproteins (Edmondson, D. E., and McCormick, D. B., Eds.) pp 583-592, Water de Gruyter and Co., Berlin, Germany.
    • (1987) Flavins and Flavoproteins , pp. 583-592
    • Mager, H.I.X.1    Tu, S.-C.2
  • 13
    • 0021207341 scopus 로고
    • Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction
    • Kurfürst, M., Ghisla, S., and Hastings, J. W. (1984) Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction, Proc. Natl. Acad. Sci. U.S.A. 81, 2990-2994.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 2990-2994
    • Kurfürst, M.1    Ghisla, S.2    Hastings, J.W.3
  • 14
    • 0023091258 scopus 로고
    • Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction
    • Kurfürst, M., Macheroux, P., Ghisla, S., and Hastings, J. W. (1987) Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction, Biochim. Biophys. Acta 924, 104-110.
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 104-110
    • Kurfürst, M.1    Macheroux, P.2    Ghisla, S.3    Hastings, J.W.4
  • 15
    • 0019497804 scopus 로고
    • Bacterial bioluminescence: Spectral study of the emitters in the in vitro reaction
    • Matheson, I. B. C., Lee, J., and Müller, F. (1981) Bacterial bioluminescence: Spectral study of the emitters in the in vitro reaction, Proc. Natl. Acad. Sci. U.S.A. 78, 948-952.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 948-952
    • Matheson, I.B.C.1    Lee, J.2    Müller, F.3
  • 16
    • 0015951494 scopus 로고
    • Fluorescence and optical characteristics of reduced flavins and flavoproteins
    • Ghisla, S., Massey, V., Lhoste, J.-M., and Mayhew, S. G. (1974) Fluorescence and optical characteristics of reduced flavins and flavoproteins, Biochemistry 14, 589-597.
    • (1974) Biochemistry , vol.14 , pp. 589-597
    • Ghisla, S.1    Massey, V.2    Lhoste, J.-M.3    Mayhew, S.G.4
  • 17
    • 0001604907 scopus 로고
    • Reversible one-electron generation of 4a,5-substituted flavin radical cations: Models for a postulated key intermediate in bacterial bioluminescence
    • Mager, H. I. X., Sazou, D., Liu, Y. H., Tu, S.-C., and Kadish, K. M. (1988) Reversible one-electron generation of 4a,5-substituted flavin radical cations: Models for a postulated key intermediate in bacterial bioluminescence, J. Am. Chem. Soc. 110, 3759-3762.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3759-3762
    • Mager, H.I.X.1    Sazou, D.2    Liu, Y.H.3    Tu, S.-C.4    Kadish, K.M.5
  • 18
    • 0001259549 scopus 로고
    • Spontaneous formation of flavin radicals in aqueous solution by comproportionation of a flavinium cation and a flavin pseudobase
    • Mager, H. I. X., and Tu, S.-C. (1988) Spontaneous formation of flavin radicals in aqueous solution by comproportionation of a flavinium cation and a flavin pseudobase, Tetrahedron 44, 5669-5674.
    • (1988) Tetrahedron , vol.44 , pp. 5669-5674
    • Mager, H.I.X.1    Tu, S.-C.2
  • 19
    • 0025427961 scopus 로고
    • Electrochemical luminescence with N(5)-ethyl-4a-hydroxy-3-methyl-4a,5- dihydrolumiflavin. The mechanism of bacterial luciferase
    • Kaaret, T. W., and Bruice, T. C. (1990) Electrochemical luminescence with N(5)-ethyl-4a-hydroxy-3-methyl-4a,5-dihydrolumiflavin. The mechanism of bacterial luciferase, Photochem. Photobiol. 51, 629-633.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 629-633
    • Kaaret, T.W.1    Bruice, T.C.2
  • 20
    • 0041020142 scopus 로고
    • Oxygenated flavin intermediates of bacterial luciferase and flavoprotein aromatic hydroxylases: Enzymology and chemical models
    • Baumstark, A. L., Ed. Jai Press, Greenwich, CT
    • Tu, S.-C. (1991) Oxygenated flavin intermediates of bacterial luciferase and flavoprotein aromatic hydroxylases: Enzymology and chemical models, in Advances in Oxygenated Processes (Baumstark, A. L., Ed.) Vol. 3, pp 115-140, Jai Press, Greenwich, CT.
    • (1991) Advances in Oxygenated Processes , vol.3 , pp. 115-140
    • Tu, S.-C.1
  • 22
    • 0020382035 scopus 로고
    • Bacterial bioluminescence: Isolation and expression of the luciferase genes from Vibrio harveyi
    • Belas, R., Mileham, A., Cohn, D., Hilmen, M., Simon, M., and Silverman, M. (1982) Bacterial bioluminescence: Isolation and expression of the luciferase genes from Vibrio harveyi, Science 218, 791-793.
    • (1982) Science , vol.218 , pp. 791-793
    • Belas, R.1    Mileham, A.2    Cohn, D.3    Hilmen, M.4    Simon, M.5    Silverman, M.6
  • 24
    • 0025254079 scopus 로고
    • Elicitation of an oxidase activity in bacterial luciferase by site-directed mutation of a noncatalytic residue
    • Xi, L., Cho, K. W., Herndon, M. E., and Tu, S.-C. (1990) Elicitation of an oxidase activity in bacterial luciferase by site-directed mutation of a noncatalytic residue, J. Biol. Chem. 265, 4200-4203.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4200-4203
    • Xi, L.1    Cho, K.W.2    Herndon, M.E.3    Tu, S.-C.4
  • 25
    • 0000033633 scopus 로고
    • Bacterial luciferase: Assay, purification, and properties
    • Hastings, J. W., Baldwin, T. O., and Nicoli, M. Z. (1978) Bacterial luciferase: Assay, purification, and properties, Methods Enzymol. 57, 135-152.
    • (1978) Methods Enzymol. , vol.57 , pp. 135-152
    • Hastings, J.W.1    Baldwin, T.O.2    Nicoli, M.Z.3
  • 26
    • 84981440745 scopus 로고
    • Die reduktive alkylierung des flavinkerns; struktur und reaktivität von dihydroflavinen
    • Ghisla, S., Hartmann, U., Hemmerich, P., and Müller, F. (1973) Die reduktive alkylierung des flavinkerns; struktur und reaktivität von dihydroflavinen, Justus Liebigs Ann. Chem. 1388-1415.
    • (1973) Justus Liebigs Ann. Chem. , pp. 1388-1415
    • Ghisla, S.1    Hartmann, U.2    Hemmerich, P.3    Müller, F.4
  • 27
    • 0011965293 scopus 로고
    • Electron transfer-II. Accumulation of 5-ethyl-3-methyllumiflavin radical by spontaneous conversions of 5-ethyl-3-methyllumiflavinium salts
    • Mager, H. I. X., and Addink, R. (1985) Electron transfer-II. Accumulation of 5-ethyl-3-methyllumiflavin radical by spontaneous conversions of 5-ethyl-3-methyllumiflavinium salts, Tetrahedron 41, 183-190.
    • (1985) Tetrahedron , vol.41 , pp. 183-190
    • Mager, H.I.X.1    Addink, R.2
  • 28
    • 0017885783 scopus 로고
    • Structural studies on bacterial luciferase using energy transfer and emission anisotropy
    • Tu, S.-C., Wu, C.-W., and Hastings, J. W. (1978) Structural studies on bacterial luciferase using energy transfer and emission anisotropy, Biochemistry 17, 987-993.
    • (1978) Biochemistry , vol.17 , pp. 987-993
    • Tu, S.-C.1    Wu, C.-W.2    Hastings, J.W.3
  • 29
    • 0014858180 scopus 로고
    • Fluorescence properties of flavins in various solvents
    • Kotaki, A., and Yagi, K. (1970) Fluorescence properties of flavins in various solvents, J. Biochem. 68, 509-516.
    • (1970) J. Biochem. , vol.68 , pp. 509-516
    • Kotaki, A.1    Yagi, K.2
  • 30
    • 0001511660 scopus 로고
    • Recherches sur la formation de complexes mineraux en solution, et sur leur stabilite
    • Job, P. (1928) Recherches sur la formation de complexes mineraux en solution, et sur leur stabilite, Ann. Chim. 9, 113-134.
    • (1928) Ann. Chim. , vol.9 , pp. 113-134
    • Job, P.1
  • 31
    • 0028142439 scopus 로고
    • Mechanism of aldehyde inhibition of Vibrio harveyi luciferase. Identification of two aldehyde sites and relationship between aldehyde and flavin binding
    • Lei, B., Cho, K. W., and Tu, S.-C. (1994) Mechanism of aldehyde inhibition of Vibrio harveyi luciferase. Identification of two aldehyde sites and relationship between aldehyde and flavin binding, J. Biol. Chem. 269, 5612-5618.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5612-5618
    • Lei, B.1    Cho, K.W.2    Tu, S.-C.3
  • 32
    • 0000445754 scopus 로고
    • The oxidation of reduced flavin mononucleotide by molecular oxgen
    • Gibson, Q. H., and Hastings, J. W. (1962) The oxidation of reduced flavin mononucleotide by molecular oxgen, Biochem. J. 83, 368-377.
    • (1962) Biochem. J. , vol.83 , pp. 368-377
    • Gibson, Q.H.1    Hastings, J.W.2
  • 33
    • 0016188369 scopus 로고
    • Mutated luciferases with altered bioluminescence emission spectra
    • Cline, T. W., and Hastings, J. W. (1974) Mutated luciferases with altered bioluminescence emission spectra, J. Biol. Chem. 249, 4668-4669.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4668-4669
    • Cline, T.W.1    Hastings, J.W.2
  • 34
    • 1542533724 scopus 로고    scopus 로고
    • Changes in the kinetics and emission spectrum on mutation of the chromophore-binding platform in Vibrio harveyi luciferase
    • Lin, L. Y., Szittner, R., Friedman, R., and Meighen, E. A. (2004) Changes in the kinetics and emission spectrum on mutation of the chromophore-binding platform in Vibrio harveyi luciferase, Biochemistry 43, 3183-3194.
    • (2004) Biochemistry , vol.43 , pp. 3183-3194
    • Lin, L.Y.1    Szittner, R.2    Friedman, R.3    Meighen, E.A.4
  • 35
    • 0027310218 scopus 로고
    • Crystal structure of a flavoprotein related to the subunits of bacterial luciferase
    • Moore, S. A., James, M. N. G., O'Kane, D. J., and Lee, J. (1993) Crystal structure of a flavoprotein related to the subunits of bacterial luciferase, EMBO J. 12, 1767-1774.
    • (1993) EMBO J. , vol.12 , pp. 1767-1774
    • Moore, S.A.1    James, M.N.G.2    O'Kane, D.J.3    Lee, J.4
  • 36
    • 0028260179 scopus 로고
    • Preparation of P-flavin-bound and P-flavin-free luciferase and P-flavin-bound β-subunit of luciferase from Photobacterium phosphoreum
    • Kasai, S. (1994) Preparation of P-flavin-bound and P-flavin-free luciferase and P-flavin-bound β-subunit of luciferase from Photobacterium phosphoreum, J. Biochem. 115, 670-674.
    • (1994) J. Biochem. , vol.115 , pp. 670-674
    • Kasai, S.1
  • 37
    • 0035894561 scopus 로고    scopus 로고
    • Characterization of the binding of Photobacterium phosphoreum P-flavin by Vibrio harveyi luciferase
    • Wei, C. J., Lei, B., and Tu, S.-C. (2001) Characterization of the binding of Photobacterium phosphoreum P-flavin by Vibrio harveyi luciferase, Arch. Biochem. Biophys. 396, 199-206.
    • (2001) Arch. Biochem. Biophys. , vol.396 , pp. 199-206
    • Wei, C.J.1    Lei, B.2    Tu, S.-C.3
  • 38
    • 0025378002 scopus 로고
    • Dithionite treatment of flavins: Spectral evidence for covalent adduct formation and effect on in vitro bacterial bioluminescence
    • Mager, H. I. X., and Tu, S.-C. (1990) Dithionite treatment of flavins: Spectral evidence for covalent adduct formation and effect on In vitro bacterial bioluminescence, Photochem. Photobiol. 51, 223-229.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 223-229
    • Mager, H.I.X.1    Tu, S.-C.2
  • 39
    • 0016146987 scopus 로고
    • Bacterial luciferase. Chemistry of the reactive sulfhydryl
    • Nicoli, M. Z., Meighen, E. A., and Hastings, J. W. (1974) Bacterial luciferase. Chemistry of the reactive sulfhydryl, J. Biol. Chem. 249, 2385-2392.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2385-2392
    • Nicoli, M.Z.1    Meighen, E.A.2    Hastings, J.W.3
  • 40
    • 0024838349 scopus 로고
    • Chemical modification and characterization of the α cysteine 106 at the Vibrio harveyi luciferase active center
    • Paquatte, O., and Tu, S.-C. (1989) Chemical modification and characterization of the α cysteine 106 at the Vibrio harveyi luciferase active center, Photochem. Photobiol. 50, 817-825.
    • (1989) Photochem. Photobiol. , vol.50 , pp. 817-825
    • Paquatte, O.1    Tu, S.-C.2
  • 41
    • 0034918673 scopus 로고    scopus 로고
    • Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data
    • Lin, L. Y., Sulea, T., Szittner, R., Vassilyev, V., Purisima, E. O., and Meighen, E. A. (2001) Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data, Protein Sci. 10, 1563-1571.
    • (2001) Protein Sci. , vol.10 , pp. 1563-1571
    • Lin, L.Y.1    Sulea, T.2    Szittner, R.3    Vassilyev, V.4    Purisima, E.O.5    Meighen, E.A.6
  • 42
    • 0037031250 scopus 로고    scopus 로고
    • Implications of the reactive thiol and the proximal non-pro line cis-peptide bond in the structure and function of Vibrio harveyi luciferase
    • Lin, L. Y., Sulea, T., Szittner, R., Kor, C., Purisima, E. O., and Meighen, E. A. (2002) Implications of the reactive thiol and the proximal non-pro line cis-peptide bond in the structure and function of Vibrio harveyi luciferase, Biochemistry 41, 9938-9945.
    • (2002) Biochemistry , vol.41 , pp. 9938-9945
    • Lin, L.Y.1    Sulea, T.2    Szittner, R.3    Kor, C.4    Purisima, E.O.5    Meighen, E.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.