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Volumn 584, Issue 15, 2010, Pages 3376-3380

Kinetic and thermodynamic properties of two barley thioredoxin h isozymes, HvTrxh1 and HvTrxh2

Author keywords

Dithiol disulfide exchange; Redox potential; Thiol pKa; Thioredoxin; Tryptophan fluorescence

Indexed keywords

BARLEY THIOREDOXIN H ISOZYME 1; BARLEY THIOREDOXIN H ISOZYME 2; IODOACETAMIDE; ISOENZYME; UNCLASSIFIED DRUG;

EID: 77955275306     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.06.028     Document Type: Article
Times cited : (16)

References (24)
  • 2
    • 0029165589 scopus 로고
    • Thioredoxin - a fold for all reasons
    • Martin J.L. Thioredoxin - a fold for all reasons. Structure 1995, 3:245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 4
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér E.S.J., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 2000, 267:6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 5
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis G.B., Holmgren A. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 1980, 255:10261-10265.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 6
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR
    • Forman-Kay J.D., Clore G.M., Gronenborn A.M. Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry 1992, 31:3442-3452.
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 8
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: a rheostat in the active site
    • Chivers P.T., Prehoda K.E., Raines R.T. The CXXC motif: a rheostat in the active site. Biochemistry 1997, 36:4061-4066.
    • (1997) Biochemistry , vol.36 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 9
    • 0025124855 scopus 로고
    • Yeast thioltransferase - the active site cysteines display differential reactivity
    • Gan Z.R., Sardana M.K., Jacobs J.W., Polokoff M.A. Yeast thioltransferase - the active site cysteines display differential reactivity. Arch. Biochem. Biophys. 1990, 282:110-115.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 110-115
    • Gan, Z.R.1    Sardana, M.K.2    Jacobs, J.W.3    Polokoff, M.A.4
  • 12
    • 0032539799 scopus 로고    scopus 로고
    • In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
    • Mouaheb N., Thomas D., Verdoucq L., Monfort P., Meyer Y. In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 1998, 95:3312-3317.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3312-3317
    • Mouaheb, N.1    Thomas, D.2    Verdoucq, L.3    Monfort, P.4    Meyer, Y.5
  • 13
    • 2342597074 scopus 로고    scopus 로고
    • Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: an early event in cereal germination
    • Wong J.H., Cai N., Tanaka C.K., Vensel W.H., Hurkman W.J., Buchanan B.B. Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: an early event in cereal germination. Plant Cell Physiol. 2004, 45:407-415.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 407-415
    • Wong, J.H.1    Cai, N.2    Tanaka, C.K.3    Vensel, W.H.4    Hurkman, W.J.5    Buchanan, B.B.6
  • 14
    • 0037636244 scopus 로고    scopus 로고
    • Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome
    • Maeda K., Finnie C., Østergaard O., Svensson B. Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome. Eur. J. Biochem. 2003, 270:2633-2643.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2633-2643
    • Maeda, K.1    Finnie, C.2    Østergaard, O.3    Svensson, B.4
  • 15
    • 38949203862 scopus 로고    scopus 로고
    • The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds: gene expression, protein profiles, and interactions between isoforms of thioredoxin h and thioredoxin reductase
    • Shahpiri A., Svensson B., Finnie C. The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds: gene expression, protein profiles, and interactions between isoforms of thioredoxin h and thioredoxin reductase. Plant Physiol. 2008, 146:789799.
    • (2008) Plant Physiol. , vol.146 , pp. 789799
    • Shahpiri, A.1    Svensson, B.2    Finnie, C.3
  • 16
    • 33846393586 scopus 로고    scopus 로고
    • Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
    • Maeda K., Hägglund P., Finnie C., Svensson B., Henriksen A. Structural basis for target protein recognition by the protein disulfide reductase thioredoxin. Structure 2006, 14:1701-1710.
    • (2006) Structure , vol.14 , pp. 1701-1710
    • Maeda, K.1    Hägglund, P.2    Finnie, C.3    Svensson, B.4    Henriksen, A.5
  • 17
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • Holmgren A. Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J. Biol. Chem. 1979, 254:9113-9119.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 18
    • 0015500758 scopus 로고
    • Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin
    • Holmgren A. Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin. J. Biol. Chem. 1972, 247:1992-1998.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1992-1998
    • Holmgren, A.1
  • 19
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause G., Lundström J., Barea J.L., Pueyo de la Cuesta C., Holmgren A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J. Biol. Chem. 1991, 266:9494-9500.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundström, J.2    Barea, J.L.3    Pueyo de la Cuesta, C.4    Holmgren, A.5
  • 20
    • 0030018518 scopus 로고    scopus 로고
    • On the reactivity and ionization of the active site cysteine residues of Escherichia coli thioredoxin
    • Takahashi N., Creighton T.E. On the reactivity and ionization of the active site cysteine residues of Escherichia coli thioredoxin. Biochemistry 1996, 35:8342-8353.
    • (1996) Biochemistry , vol.35 , pp. 8342-8353
    • Takahashi, N.1    Creighton, T.E.2
  • 21
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Åslund F., Berndt K.D., Holmgren A. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem. 1997, 272:30780-30786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Åslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 23
    • 33847710733 scopus 로고    scopus 로고
    • Kinetics of the intramolecular disulfide exchange between the periplasmic domains of DsbD
    • Rozhkova A., Glockshuber R. Kinetics of the intramolecular disulfide exchange between the periplasmic domains of DsbD. J. Mol. Biol. 2007, 367:1162-1170.
    • (2007) J. Mol. Biol. , vol.367 , pp. 1162-1170
    • Rozhkova, A.1    Glockshuber, R.2
  • 24
    • 44349183189 scopus 로고    scopus 로고
    • Crystal structures of barley thioredoxin h isoforms HvTrxh1 and HvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity
    • Maeda K., Hägglund P., Finnie C., Svensson B., Henriksen A. Crystal structures of barley thioredoxin h isoforms HvTrxh1 and HvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity. Protein Sci. 2008, 17:1015-1024.
    • (2008) Protein Sci. , vol.17 , pp. 1015-1024
    • Maeda, K.1    Hägglund, P.2    Finnie, C.3    Svensson, B.4    Henriksen, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.