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Volumn 270, Issue 17, 2003, Pages 3565-3571

Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: Evidence for the participation of other residues

Author keywords

Gamma and pulse radiolysis; Intramolecular long range electron transfer; Lysozyme; One electron oxidation

Indexed keywords

EGG WHITE; LYSOZYME; TRYPTOPHAN; TYROSINE;

EID: 0041322950     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03741.x     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0016927359 scopus 로고
    • Photochemical inactivation of enzymes
    • Grossweiner, L.I. (1976) Photochemical inactivation of enzymes. Curr. Top. Radiat. Res. Q. 11, 141-199.
    • (1976) Curr. Top. Radiat. Res. Q. , vol.11 , pp. 141-199
    • Grossweiner, L.I.1
  • 2
    • 0018538777 scopus 로고
    • Applications of pulse radiolysis to protein chemistry
    • Klapper, M.H. & Faraggi, M. (1979) Applications of pulse radiolysis to protein chemistry. Q. Rev. Biophys. 12, 465-519.
    • (1979) Q. Rev. Biophys. , vol.12 , pp. 465-519
    • Klapper, M.H.1    Faraggi, M.2
  • 4
    • 0037035536 scopus 로고    scopus 로고
    • Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase
    • Feng, C., Kedia, R.V., Hazzard, J.T., Hurley, J.K., Tollin, G. & Enemark, J.H. (2002) Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase. Biochemistry 41, 5816-5821.
    • (2002) Biochemistry , vol.41 , pp. 5816-5821
    • Feng, C.1    Kedia, R.V.2    Hazzard, J.T.3    Hurley, J.K.4    Tollin, G.5    Enemark, J.H.6
  • 5
    • 0036713565 scopus 로고    scopus 로고
    • Repair of amino acid radicals of apolipoprotein B100 of low-density lipoproteins by flavonoids. A pulse radiolysis study with quercetin and rutin
    • Filipe, P., Morliere, P., Patterson, L.K., Hug, G.L., Maziere, J.-C., Maziere, C., Freitas, J.P., Fernandes, A. & Santus, R. (2002) Repair of amino acid radicals of apolipoprotein B100 of low-density lipoproteins by flavonoids. A pulse radiolysis study with quercetin and rutin. Biochemistry 41, 11057-11064.
    • (2002) Biochemistry , vol.41 , pp. 11057-11064
    • Filipe, P.1    Morliere, P.2    Patterson, L.K.3    Hug, G.L.4    Maziere, J.-C.5    Maziere, C.6    Freitas, J.P.7    Fernandes, A.8    Santus, R.9
  • 7
    • 33845183951 scopus 로고
    • Long-range electron transfer between tyrosine and tryptophan in peptides
    • Faraggi, M., DeFelippis, M.R. & Klapper, M.H. (1989) Long-range electron transfer between tyrosine and tryptophan in peptides. J. Am. Chem. Soc. 111, 5141-5145.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5141-5145
    • Faraggi, M.1    DeFelippis, M.R.2    Klapper, M.H.3
  • 8
    • 0025108014 scopus 로고
    • Evidence for through-bond long range electron transfer in peptides
    • DeFelippis, M.R., Faraggi, M. & Klapper, M.H. (1990) Evidence for through-bond long range electron transfer in peptides. J. Am. Chem. Soc. 112, 5640-5642.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5640-5642
    • DeFelippis, M.R.1    Faraggi, M.2    Klapper, M.H.3
  • 9
    • 0026767871 scopus 로고
    • Long range electron transfer along an alpha-helix
    • Lee, H., Faraggi, M. & Klapper, M.H. (1992) Long range electron transfer along an alpha-helix. Biochim. Biophys. Acta 1159, 286-294.
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 286-294
    • Lee, H.1    Faraggi, M.2    Klapper, M.H.3
  • 10
    • 0025334451 scopus 로고
    • Intramolecular electron transfer in peptides containing methionine, tryptophan and tyrosine: A pulse radiolysis study
    • Bobrowski, K., Wierzchowski, K.L., Holcman, J. & Ciurak, M. (1990) Intramolecular electron transfer in peptides containing methionine, tryptophan and tyrosine: a pulse radiolysis study. Int. J. Radiat. Biol. 57, 919-932.
    • (1990) Int. J. Radiat. Biol. , vol.57 , pp. 919-932
    • Bobrowski, K.1    Wierzchowski, K.L.2    Holcman, J.3    Ciurak, M.4
  • 11
    • 0019327137 scopus 로고
    • Direct demonstration of electron transfer between tryptophan and tyrosine in proteins
    • Prütz, W.A., Butler, J., Land, E.J. & Swallow, A.J. (1980) Direct demonstration of electron transfer between tryptophan and tyrosine in proteins. Biochem. Biophys. Res. Commun. 96, 513-520.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 513-520
    • Prütz, W.A.1    Butler, J.2    Land, E.J.3    Swallow, A.J.4
  • 13
    • 0024384199 scopus 로고
    • Pulse radiolytic measurement of redox potentials: The tyrosine and tryptophan radicals
    • DeFelippis, M.R., Murthy, C.P., Faraggi, M. & Klapper, M.H. (1989) Pulse radiolytic measurement of redox potentials: the tyrosine and tryptophan radicals. Biochemistry 8, 4847-4853.
    • (1989) Biochemistry , vol.8 , pp. 4847-4853
    • DeFelippis, M.R.1    Murthy, C.P.2    Faraggi, M.3    Klapper, M.H.4
  • 16
    • 0024411525 scopus 로고
    • Temperature dependence of intramolecular electron transfer as a probe for predenaturational changes in lysozyme
    • Bobrowski, K., Holcman, J. & Wierzchowski, K.L. (1989) Temperature dependence of intramolecular electron transfer as a probe for predenaturational changes in lysozyme. Free Rad. Res. Commun. 6, 235-241.
    • (1989) Free Rad. Res. Commun. , vol.6 , pp. 235-241
    • Bobrowski, K.1    Holcman, J.2    Wierzchowski, K.L.3
  • 20
    • 0019816864 scopus 로고
    • Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions
    • Artymiuk, P.J. & Blake, C.C.P. (1981) Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions. J. Mol. Biol. 152, 737-762.
    • (1981) J. Mol. Biol. , vol.152 , pp. 737-762
    • Artymiuk, P.J.1    Blake, C.C.P.2
  • 21
    • 0025194489 scopus 로고
    • 1H NMR studies of human lysozyme: Spectral assignment and comparison with hen lysozyme
    • 1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. Biochemistry 29, 7201-7214.
    • (1990) Biochemistry , vol.29 , pp. 7201-7214
    • Redfield, C.1    Dobson, C.M.2
  • 22
    • 0027970593 scopus 로고
    • Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: Calcium-binding lysozymes and their relationship with alpha-lactalbumins
    • Acharya, K.R., Stuart, D.I., Phillips, D.C., McKenzie, H.A. & Teahan, C.G. (1994) Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: calcium-binding lysozymes and their relationship with alpha-lactalbumins. J. Protein Chem. 13, 569-584.
    • (1994) J. Protein Chem. , vol.13 , pp. 569-584
    • Acharya, K.R.1    Stuart, D.I.2    Phillips, D.C.3    McKenzie, H.A.4    Teahan, C.G.5
  • 23
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • Jollès, P. & Jollès, J. (1984) What's new in lysozyme research? Mol. Cell Biochem. 63, 165-189.
    • (1984) Mol. Cell Biochem. , vol.63 , pp. 165-189
    • Jollès, P.1    Jollès, J.2
  • 24
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 25
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, J.C. & von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, J.C.1    Von Hippel, P.H.2
  • 26
    • 0025572691 scopus 로고
    • - radical induced cleavage of disulfide bonds in proteins. A gamma-ray and pulse radiolysis mechanistic investigation
    • - radical induced cleavage of disulfide bonds in proteins. A gamma-ray and pulse radiolysis mechanistic investigation. Biochemistry 29, 10978-10989.
    • (1990) Biochemistry , vol.29 , pp. 10978-10989
    • Favaudon, V.1    Tourbez, H.2    Houée-Levin, C.3    Lhoste, J.-M.4
  • 30
    • 33847800381 scopus 로고
    • Laser flash photolysis of aqueous tryptophan
    • Dudley, F.D., Santus, R. & Grossweiner, L.I. (1975) Laser flash photolysis of aqueous tryptophan. J. Phys. Chem. 79, 2711-2716.
    • (1975) J. Phys. Chem. , vol.79 , pp. 2711-2716
    • Dudley, F.D.1    Santus, R.2    Grossweiner, L.I.3
  • 31
    • 0041590408 scopus 로고    scopus 로고
    • Oxidative dimerization of proteins: Role of tyrosine accessibility
    • Audette, M., Blouquit, Y. & Houée-Levin, C. (2000) Oxidative dimerization of proteins: role of tyrosine accessibility. Arch. Biochem. Biophys. 76, 673-681.
    • (2000) Arch. Biochem. Biophys. , vol.76 , pp. 673-681
    • Audette, M.1    Blouquit, Y.2    Houée-Levin, C.3
  • 33
    • 0005780537 scopus 로고    scopus 로고
    • HPLC analysis of γ-irradiation-induced products of tryptophan in peptides and lysozyme
    • Van Wickern, B., Simat, T. & Steinhart, H. (1997) HPLC analysis of γ-irradiation-induced products of tryptophan in peptides and lysozyme. Z. Lebensm. Unters Forsch. A. 205, 446-451.
    • (1997) Z. Lebensm. Unters Forsch. A. , vol.205 , pp. 446-451
    • Van Wickern, B.1    Simat, T.2    Steinhart, H.3
  • 34
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • Garrison, W.M. (1987) Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. 87, 381-398.
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 35
    • 0036769570 scopus 로고    scopus 로고
    • A DFT study of electron and hole localisation in a peptide containing asparagin
    • Houée-Levin, C. & Bergès, J. (2002) A DFT study of electron and hole localisation in a peptide containing asparagin. Eur. Phy. J. D 20, 551-555.
    • (2002) Eur. Phy. J. D , vol.20 , pp. 551-555
    • Houée-Levin, C.1    Bergès, J.2
  • 36
    • 0030971178 scopus 로고    scopus 로고
    • Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. 7. Trp → TyrO radical transformation in hen egg-white lysozyme. Effects of pH, temperature, Trp62 oxidation and inhibitor binding
    • Bobrowski, K., Holcman, J., Poznanski, J. & Wierzchowski, K.L. (1997) Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. 7. Trp → TyrO radical transformation in hen egg-white lysozyme. Effects of pH, temperature, Trp62 oxidation and inhibitor binding. Biophys. Chem. 63, 153-166.
    • (1997) Biophys. Chem. , vol.63 , pp. 153-166
    • Bobrowski, K.1    Holcman, J.2    Poznanski, J.3    Wierzchowski, K.L.4
  • 37
    • 0027337098 scopus 로고
    • 1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme
    • 1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme. Eur. J. Biochem. 215, 255-266.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 255-266
    • Bartik, K.1    Dobson, C.M.2    Redfield, C.3


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