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Abstract| Volume 262, ISSUE 33, P15900-15907, November 25, 1987

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Sugar transport by the bacterial phosphotransferase system. The intrinsic fluorescence of enzyme I.

Open AccessPublished:November 25, 1987DOI:https://doi.org/10.1016/S0021-9258(18)47674-0
Sugar transport by the bacterial phosphotransferase system. The intrinsic fluorescence of enzyme I.
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      Enzyme I of the bacterial phosphoenolpyruvate: glycose phosphotransferase system has 2 tryptophan residues/monomer, as determined spectrophotometrically. The tryptophan fluorescence has been investigated with the aid of nanosecond time-resolved techniques. The decay of the fluorescence intensity was analyzed in terms of a biexponential function. The contribution of the emission associated with the shorter decay constant increases from 17-19% at 1 degree C to 43-44% at room temperature. Decay-associated spectra obtained with Enzyme I indicate different spectral distributions associated with the two decay constants. The measurement of tumbling of Enzyme I as a function of temperature revealed a transition of rotational rates between 5 and 15.5 degrees C. Global analysis allowed decomposition of the anisotropy decay into a formulation consistent with monomer and dimer rotational contributions.

      REFERENCES

        • Kundig W.
        • Gosh S.
        • Roseman S.
        Proc. Natl. Acad. Sci. U. S. A. 1964; 52: 1067-1074
        • Postma P.W.
        • Roseman S.
        Biochim. Biophys. Acta. 1976; 457: 213-257
        • Meadow N.D.
        • Kukuruzinska M.A.
        • Roseman S.
        Martonosi A. Enzymes of Biological Membranes. 3. Plenum Press, New York1984: 523-559
        • Waygood E.B.
        • Weigel N.
        • Nakazawa A.
        • Kukuruzinska M.A.
        • Roseman S.
        Proc. Can. Fed. Biol. Soc. 1977; 20: 54
        • Kukuruzinska M.A.
        • Harrington W.F.
        • Roseman S.
        J. Biol. Chem. 1982; 257: 14470-14476
        • Weigel N.
        • Kukuruzinska M.A.
        • Nakazawa A.
        • Waygood E.B.
        • Roseman S.
        J. Biol. Chem. 1982; 257: 14477-14491
        • Kukuruzinska M.A.
        • Turner B.N.
        • Ackers G.K.
        • Roseman S.
        J. Biol. Chem. 1984; 259: 11679-11681
        • Saier Jr., M.H.
        • Roseman S.
        J. Biol. Chem. 1976; 251: 6606-6615
        • Weigel N.
        • Waygood E.B.
        • Kukuruzinska M.A.
        • Nakazawa A.
        • Roseman S.
        J. Biol. Chem. 1982; 257: 14461-14469

      10. Saffen, D. W. (1985) Ph.D. dissertation, The Johns Hopkins University

        • Konev S.V.
        Fluorescence and Phosphorescence of Protein and Nucleic Acids. Plenum Press, New York1967
        • Neyroz P.
        • Ross J.B.A.
        • Knutson J.R.
        • Brand L.
        Szabo A.G. Masotti L. Excited-State Probes in Biochemistry and Biology. Plenum Press, New York1987
        • Brand L.
        • Everse J.
        • Kaplan N.O.
        Biochemistry. 1962; 1: 423-434
        • Schechter A.N.
        • Chen R.F.
        • Anfinsen C.B.
        Science. 1970; 167: 886-887
        • Burstein E.A.
        • Permyakov E.A.
        • Yashin V.A.
        • Burkhanov S.A.
        • Finazzi Agro A.
        Biochim. Biophys. Acta. 1977; 491: 155-159
        • Beechem J.M.
        • Brand L.
        Annu. Rev. Biochem. 1985; 54: 43-71
        • Laemmli U.K.
        Nature. 1970; 227: 680-685
        • Layne E.
        Methods Enzymol. 1957; 3: 447-454
        • Lowry O.H.
        • Rosebrough N.J.
        • Farr A.L.
        • Randall R.J.
        J. Biol. Chem. 1951; 193: 265-275
        • Bensadoun A.
        • Weinstein D.
        Anal. Biochem. 1976; 70: 241-250
        • Azumi T.
        • McGlynn S.P.
        J. Chem. Phys. 1962; 37: 2413-2420
        • Paoletti J.
        • LePecq J.B.
        Anal. Biochem. 1969; 31: 33-41
        • Ware R.W.
        Lamola A. Creation and Detection of the Excited State. 1. Marcel Dekkar Inc., New York1972: 213-302 (part A)
        • Yguerabide J.
        Methods Enzymol. 1972; 26: 498-578
        • O'Connor D.V.
        • Phillips D.
        Time-correlated Single Photon Counting. Academic Press, New York1984
        • Badea M.G.
        • Brand L.
        Methods Enzymol. 1979; 61: 378-425
        • Wahl Ph
        • Auchet J.C.
        • Donzel B.
        Rev. Sci. Instrum. 1974; 45: 28-32
        • Dale R.E.
        • Chen L.A.
        • Brand L.
        J. Biol. Chem. 1977; 252: 7500-7510
        • Knight A.E.W.
        • Selinger B.K.
        Spectrochim. Acta Part A Mol. Spectrosc. 1971; 27: 1223
        • Grinvald A.
        • Steinberg I.Z.
        Anal. Biochem. 1974; 59: 583-598
        • Bevington P.R.
        Data Reduction and Error Analysis for the Physical Sciences. McGraw-Hill Publications, Minneapolis, MN1969
        • Knutson J.R.
        • Beechem J.M.
        • Brand L.
        Chem. Phys. Lett. 1983; 102: 501-507
        • Wahl Ph
        • Auchet J.C.
        Biochim. Biophys. Acta. 1972; 285: 99-117
        • Privat J.P.
        • Wahl Ph.
        • Auchet J.C.
        Biophys. Chem. 1980; 11: 239-248
        • Eisenfeld J.
        • Ford C.C.
        Biophys. J. 1979; 26: 73-83
        • Beechem J.M.
        • Ameloot M.
        • Brand L.
        Szabo A.G. Masotti L. Excited-State Probes in Biochemistry and Biology. Plenum Press, New York1987 (in press)
        • Beechem J.M.
        • Ameloot M.
        • Brand L.
        Anal. Instrum. 1985; 14: 379-402
        • Ameloot M.
        • Beechem J.M.
        • Brand L.
        Biophys. Chem. 1986; 23: 155-171
        • Knutson J.R.
        • Walbridge D.G.
        • Brand L.
        Biochemistry. 1982; 21: 4671-4679
        • Wahl Ph.
        Biochim. Biophys. Acta. 1969; 175: 55-64
        • Tao T.
        Biopolymers. 1969; 8: 609-632
        • Ehrenberg M.
        • Rigler R.
        Chem. Phys. Lett. 1972; 14: 539
        • Edelhoch H.
        Biochemistry. 1967; 6: 1948-1954
        • Johnson M.L.
        Biophys. J. 1983; 44: 101-106
        • Zelen M.
        • Severo N.
        Abramowitz M. Stegun I. National Bureau of Standards Handbook of Mathematical Functions. GPO, Wash. D. C.1964: 946
        • Ackers G.K.
        • Johnson M.L.
        • Mills F.C.
        • Halvorson H.R.
        • Shapiro S.
        Biochemistry. 1975; 14: 5128-5134
        • Brand L.
        • Knutson J.R.
        • Davenport L.
        • Beechem J.M.
        • Dale R.E.
        • Walbridge D.
        • Kowalczyk A.A.
        Spectroscopy and the Dynamics of Molecular Biological Systems. Academic Press, Orlando, FL1985
        • Ross J.B.A.
        • Schmidt C.J.
        • Brand L.
        Biochemistry. 1981; 20: 4369-4377
        • Weber G.
        McElroy W.D. Glass B. Light and Life. Johns Hopkins University Press, Baltimore1961: 82-107

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      Published online: November 25, 1987

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      DOI: https://doi.org/10.1016/S0021-9258(18)47674-0

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      © 1987 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

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