메뉴 건너뛰기




Volumn 271, Issue 17, 2004, Pages 3481-3487

Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation

Author keywords

One electron oxidation; Radiolysis; Thioredoxin; Tryptophan35 oxidation

Indexed keywords

AZIDE; THIOREDOXIN; TRYPTOPHAN; TYROSINE;

EID: 4544325179     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04279.x     Document Type: Article
Times cited : (24)

References (43)
  • 2
    • 0038393058 scopus 로고    scopus 로고
    • Oxidation of nuclear thioredoxin during oxidative stress
    • Watson, W.H. & Jones, D.P. (2003) Oxidation of nuclear thioredoxin during oxidative stress. FEBS Lett. 543, 144-147.
    • (2003) FEBS Lett. , vol.543 , pp. 144-147
    • Watson, W.H.1    Jones, D.P.2
  • 3
    • 0033429334 scopus 로고    scopus 로고
    • Stable markers of oxidant damage to proteins and their application in the study of human disease
    • Davies, M.J., Fu, S., Wang, H. & Dean, R.T. (1999) Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Rad. Biol. Med. 27, 1151-1163.
    • (1999) Free Rad. Biol. Med. , vol.27 , pp. 1151-1163
    • Davies, M.J.1    Fu, S.2    Wang, H.3    Dean, R.T.4
  • 5
    • 0026060848 scopus 로고
    • Long range electron transfer between tyrosine and tryptophan in hen egg-white lysozyme
    • Weinstein, M., Alfassi, Z.B., De Felippis, M.R. & Faraggi, M. (1991) Long range electron transfer between tyrosine and tryptophan in hen egg-white lysozyme. Biochim. Biophys. Acta 1076, 173-178,
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 173-178
    • Weinstein, M.1    Alfassi, Z.B.2    De Felippis, M.R.3    Faraggi, M.4
  • 6
    • 0041322950 scopus 로고    scopus 로고
    • Re-evaluation of intramolecular long range electron transfer between tyrosine and tryptophan in lysozymes. Evidence for the participation of other residues
    • Stuart-Audette, M., Blouquit, Y., Faraggi, M., Sicard-Roselli, C., Houée-Levin, C. & Jollès, P. (2003) Re-evaluation of intramolecular long range electron transfer between tyrosine and tryptophan in lysozymes. Evidence for the participation of other residues. Eur. J. Biochem. 270, 1-7.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1-7
    • Stuart-Audette, M.1    Blouquit, Y.2    Faraggi, M.3    Sicard-Roselli, C.4    Houée-Levin, C.5    Jollès, P.6
  • 7
    • 0034425036 scopus 로고    scopus 로고
    • Crystal structure of the W35A mutant thioredoxin h from Chlamydomonas reinhardtii: The substitution of the conserved active site Trp leads to modifications in the environment of the two catalytic cysteines
    • Menchise, V., Corbier, C., Didierjean, C., Jacquot, J.-P., Benedetti, E., Saviano, M. & Aubry, A. (2001) Crystal structure of the W35A mutant thioredoxin h from Chlamydomonas reinhardtii: the substitution of the conserved active site Trp leads to modifications in the environment of the two catalytic cysteines. Biopolymers 56, 1-7.
    • (2001) Biopolymers , vol.56 , pp. 1-7
    • Menchise, V.1    Corbier, C.2    Didierjean, C.3    Jacquot, J.-P.4    Benedetti, E.5    Saviano, M.6    Aubry, A.7
  • 9
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund, H., Gleason, F.K. & Holmgren, A. (1991) Structural and functional relations among thioredoxins of different species. Proteins 11, 13-28.
    • (1991) Proteins , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 10
    • 0031442195 scopus 로고    scopus 로고
    • General acid/base catalysis in the active site of Escherichia coli thioredoxin
    • Chivers, P.T. & Raines, R.T. (1997) General acid/base catalysis in the active site of Escherichia coli thioredoxin. Biochemistry 36, 15810-15816.
    • (1997) Biochemistry , vol.36 , pp. 15810-15816
    • Chivers, P.T.1    Raines, R.T.2
  • 11
    • 0031024788 scopus 로고    scopus 로고
    • Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57
    • Dyson, H.J., Jeng, M.F., Tennant, L.L., Slaby, I., Lindell, M., Cui, D.S., Kuprin, S. & Holmgren, A. (1997) Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 36, 2622-2636.
    • (1997) Biochemistry , vol.36 , pp. 2622-2636
    • Dyson, H.J.1    Jeng, M.F.2    Tennant, L.L.3    Slaby, I.4    Lindell, M.5    Cui, D.S.6    Kuprin, S.7    Holmgren, A.8
  • 12
    • 0029310608 scopus 로고
    • Chlamydomonas reinhardtii thioredoxins: Structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties
    • Stein, M., Jacquot, J.-P., Jeannette, E., Decottignies, P., Hodges, M., Lancelin, J.M., Mittard, V., Schmitter, J.M. & Miginiac-Maslow, M. (1995) Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. Plant Mol. Biol. 28, 487-503.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 487-503
    • Stein, M.1    Jacquot, J.-P.2    Jeannette, E.3    Decottignies, P.4    Hodges, M.5    Lancelin, J.M.6    Mittard, V.7    Schmitter, J.M.8    Miginiac-Maslow, M.9
  • 13
    • 0034622573 scopus 로고    scopus 로고
    • Redox properties of protein disulfide bond in oxidized thioredoxin and lysozyme: A pulse radiolysis study
    • El Hanine Lmoumène, C., Conte. D., Jacquot, J.-P. & Houée-Levin, C. (2000) Redox properties of protein disulfide bond in oxidized thioredoxin and lysozyme: a pulse radiolysis study. Biochemistry 39, 9295-9301.
    • (2000) Biochemistry , vol.39 , pp. 9295-9301
    • El Hanine Lmoumène, C.1    Conte, D.2    Jacquot, J.-P.3    Houée-Levin, C.4
  • 14
    • 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
  • 15
    • 37049084188 scopus 로고
    • Reevaluation of the thiocyanate dosimeter for pulse radiolysis
    • Buxton, G.V. & Stuart, C.R. (1995) Reevaluation of the thiocyanate dosimeter for pulse radiolysis. J. Chem. Soc. Faraday Trans. 91, 279-281.
    • (1995) J. Chem. Soc. Faraday Trans. , vol.91 , pp. 279-281
    • Buxton, G.V.1    Stuart, C.R.2
  • 16
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1-100 kDa
    • Schägger, H. & von Jagow, O. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1-100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, O.2
  • 17
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren, A. (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 19
    • 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
  • 20
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met (35) in neurotoxic beta-amyloid peptide. A molecular modeling study
    • Pogocki, D. & Schoneich, C. (2002) Redox properties of Met (35) in neurotoxic beta-amyloid peptide. A molecular modeling study. Chem. Res. Toxicol. 15, 408-418.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 408-418
    • Pogocki, D.1    Schoneich, C.2
  • 21
    • 0034684267 scopus 로고    scopus 로고
    • Intramolecular sulfure-oxygen bond formation in radical cations of N-acetylmethionine amide
    • Schoneich, C., Pogocki, D., Wisniowski, P., Hug, G.L. & Bobrowski, K. (2000) Intramolecular sulfure-oxygen bond formation in radical cations of N-acetylmethionine amide. J. Am. Chem. Soc. 122, 10224-10225.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10224-10225
    • Schoneich, C.1    Pogocki, D.2    Wisniowski, P.3    Hug, G.L.4    Bobrowski, K.5
  • 22
    • 0037425479 scopus 로고    scopus 로고
    • Effect of solvent viscosity, polarity and pH on the charge transfer between tryptophan radical and tyrosine in bovine serum albumin: A pulse radiolysis study
    • Joshi, R. & Mukherjee, T. (2003) Effect of solvent viscosity, polarity and pH on the charge transfer between tryptophan radical and tyrosine in bovine serum albumin: a pulse radiolysis study. Biophys. Chem. 103, 89-98.
    • (2003) Biophys. Chem. , vol.103 , pp. 89-98
    • Joshi, R.1    Mukherjee, T.2
  • 23
    • 0037051840 scopus 로고    scopus 로고
    • Charge transfer between tryptophan and tyrosine in casein: A pulse radiolysis study
    • Joshi, R. & Mukherjee, T. (2002) Charge transfer between tryptophan and tyrosine in casein: a pulse radiolysis study. Biophys. Chem. 96, 15-19.
    • (2002) Biophys. Chem. , vol.96 , pp. 15-19
    • Joshi, R.1    Mukherjee, T.2
  • 25
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause, G. & Holmgren, A. (1991) Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. J. Biol. Chem. 266, 4056-4066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 26
    • 0018722293 scopus 로고
    • Charge transfer in peptides. Pulse radiolysis investigation of one-electron reactions in dipeptides of tryptophan and tyrosine
    • Prütz, W.A. & Land, E.J. (1979) Charge transfer in peptides. Pulse radiolysis investigation of one-electron reactions in dipeptides of tryptophan and tyrosine. Int. J. Radiat. Biol. 36, 513-520.
    • (1979) Int. J. Radiat. Biol. , vol.36 , pp. 513-520
    • Prütz, W.A.1    Land, E.J.2
  • 27
    • 0001118058 scopus 로고
    • Charge transfer in peptides. Intramolecular radical transformations involving methionine, tryptophan and tyrosine
    • Prütz, W.A., Siebert, F., Butler, J., Land, E.J., Menez, A. & Montenay-Garestier, T. (1982) Charge transfer in peptides. Intramolecular radical transformations involving methionine, tryptophan and tyrosine. Biochim. Biophys. Acta 705, 139-149.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 139-149
    • Prütz, W.A.1    Siebert, F.2    Butler, J.3    Land, E.J.4    Menez, A.5    Montenay-Garestier, T.6
  • 29
    • 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
  • 30
    • 0035476417 scopus 로고    scopus 로고
    • Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism
    • Menchise, V., Corbier, C., Didierjean, C., Saviano, M., Benedetti, E., Jacquot. J.-P. & Aubry, A. (2001) Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism. Biochem. J. 359, 65-75.
    • (2001) Biochem. J. , vol.359 , pp. 65-75
    • Menchise, V.1    Corbier, C.2    Didierjean, C.3    Saviano, M.4    Benedetti, E.5    Jacquot, J.-P.6    Aubry, A.7
  • 31
    • 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
  • 32
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus, R.A. & Sutin, N. (1985) Electron transfers in chemistry and biology. Biochim. Biophys. Acta 811, 265-322.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 33
    • 33749130604 scopus 로고
    • Distance dependence of electron transfer rates
    • Hush, N.S. (1985) Distance dependence of electron transfer rates. Coord. Chem. Rev. 64, 135-157.
    • (1985) Coord. Chem. Rev. , vol.64 , pp. 135-157
    • Hush, N.S.1
  • 34
    • 0345318403 scopus 로고
    • Long-distance electron transfer in proteins and model systems
    • McLendon, G. (1988) Long-distance electron transfer in proteins and model systems. Acc. Chem. Res. 21, 160-167.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 160-167
    • McLendon, G.1
  • 36
    • 0038676610 scopus 로고    scopus 로고
    • Free radical reactions of methionine in peptides: Mechanisms relevant to β-amyloid oxidation and Alzheimer's disease
    • Schöneich, C., Pogoski, D., Hug, G.L. & Bobrowski, K. (2003) Free radical reactions of methionine in peptides: Mechanisms relevant to β-amyloid oxidation and Alzheimer's disease. J. Am. Chem. Soc. 125, 13700-137013.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13700-137013
    • Schöneich, C.1    Pogoski, D.2    Hug, G.L.3    Bobrowski, K.4
  • 38
    • 0041590408 scopus 로고    scopus 로고
    • Oxidative dimerisation of proteins: Role of tyrosine accessibility
    • Audette, M., Blouquit, Y. & Houée-Levin, C. (2000) Oxidative dimerisation 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
  • 39
    • 0031248670 scopus 로고    scopus 로고
    • Ab initio calculations on arginine-disulfide complexes modelling the one-electron reduction of lysozyme. Comparison to an experimental reinvestigation
    • Berges, J., Kassab, E., Conte, D., Adjadj, E. & Houée-Levin, C. (1997) Ab initio calculations on arginine-disulfide complexes modelling the one-electron reduction of lysozyme. Comparison to an experimental reinvestigation. J. Phys. Chem. 101, 7809-7881.
    • (1997) J. Phys. Chem. , vol.101 , pp. 7809-7881
    • Berges, J.1    Kassab, E.2    Conte, D.3    Adjadj, E.4    Houée-Levin, C.5
  • 40
    • 0033551437 scopus 로고    scopus 로고
    • Effects of structure on alpha C-H bond enthalpies of amino acid residues: Relevance to H transfers in enzyme mechanisms and in protein oxidation
    • Rauk, A., Yu, D., Taylor, J., Shustov, G.V., Block, D.A. & Armstrong, D.A. (1999) Effects of structure on alpha C-H bond enthalpies of amino acid residues: relevance to H transfers in enzyme mechanisms and in protein oxidation. Biochemistry 38, 9089-9096.
    • (1999) Biochemistry , vol.38 , pp. 9089-9096
    • Rauk, A.1    Yu, D.2    Taylor, J.3    Shustov, G.V.4    Block, D.A.5    Armstrong, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.