메뉴 건너뛰기




Volumn 49, Issue 4, 2010, Pages 810-820

Thiol-disulfide exchange between glutaredoxin and glutathione

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATALYTIC MECHANISMS; EXCHANGE REACTION; GLUTATHIONES; GLUTATHIONYLATION; IN-LINE; ISOTHERMAL TITRATION CALORIMETRY; NON-COVALENT INTERACTION; OXIDOREDUCTASES; STANDARD REDUCTION POTENTIALS; THERMAL STABILITY; THIOL-DISULFIDE; THIOLATES; THIOREDOXINS;

EID: 75149140987     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9015956     Document Type: Article
Times cited : (39)

References (48)
  • 1
    • 41449113782 scopus 로고    scopus 로고
    • Redox Characteristics of the Eukaryotic Cytosol
    • López-Mirabel, H. R., and Winther, J. R. (2008) Redox Characteristics of the Eukaryotic Cytosol. Biochim. Biophys. Acta 1783, 629-640.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 629-640
    • López-Mirabel, H.R.1    Winther, J.R.2
  • 2
    • 3042802690 scopus 로고    scopus 로고
    • Glutathione: An Overview of Biosynthesis and Modulation
    • Anderson, M. E. (1998) Glutathione: An Overview of Biosynthesis and Modulation. Chem. - Biol. Interact. 111-112, 1-14.
    • (1998) Chem. - Biol. Interact , vol.111-112 , pp. 1-14
    • Anderson, M.E.1
  • 3
    • 0346788873 scopus 로고    scopus 로고
    • Kinetics of Superoxide Scavenging by Glutathione: An Evaluation of Its Role in the Removal of Mitochondrial Superoxide
    • Jones, C. M., Lawrence, A., Wardman, P., and Burkitt, M. J. (2003) Kinetics of Superoxide Scavenging by Glutathione: An Evaluation of Its Role in the Removal of Mitochondrial Superoxide. Biochem. Soc. Trans. 31, 1337-1339.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 1337-1339
    • Jones, C.M.1    Lawrence, A.2    Wardman, P.3    Burkitt, M.J.4
  • 4
    • 0026795635 scopus 로고
    • Protein Oxidation and Aging
    • Stadtman, E. R. (1992) Protein Oxidation and Aging. Science 257, 1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 5
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of Protein Function by Glutathionylation
    • Ghezzi, P. (2005) Regulation of Protein Function by Glutathionylation. Free Radical Res. 39, 573-580.
    • (2005) Free Radical Res , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 6
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of Reversible Protein Glutathionylation in Redox Signaling and Oxidative Stress
    • Gallogly, M. M., and Mieyal, J. J. (2007) Mechanisms of Reversible Protein Glutathionylation in Redox Signaling and Oxidative Stress. Curr. Opin. Pharmacol. 7, 381-391.
    • (2007) Curr. Opin. Pharmacol , vol.7 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 7
    • 34447534530 scopus 로고    scopus 로고
    • Protein Glutathionylation and Oxidative Stress
    • Niwa, T. (2007) Protein Glutathionylation and Oxidative Stress. J. Chromatogr. B 855, 59-65.
    • (2007) J. Chromatogr. B , vol.855 , pp. 59-65
    • Niwa, T.1
  • 8
    • 3142663363 scopus 로고    scopus 로고
    • S-Glutathionylation of Ras Mediates Redox-sensitive Signaling by Angiotensin II in Vascular Smooth Muscle Cells
    • Adachi, T., Pimentel, D. R., Heibeck, T., Hou, X., Lee, Y. J., Jiang, B., Ido, Y., and Cohen, R. A. (2004) S-Glutathionylation of Ras Mediates Redox-sensitive Signaling by Angiotensin II in Vascular Smooth Muscle Cells. J. Biol. Chem. 279, 29857-29862.
    • (2004) J. Biol. Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 9
    • 0027238801 scopus 로고
    • Thioltransferase Is a Specific Glutathionyl Mixed Disulfide Oxidoreductase
    • Gravina, S. A., and Mieyal, J. J. (1993) Thioltransferase Is a Specific Glutathionyl Mixed Disulfide Oxidoreductase. Biochemistry 32, 3368-3376.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 10
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions far beyond a Simple Thioredoxin Backup System
    • Fernandes, A. P., and Holmgren, A. (2004) Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions far beyond a Simple Thioredoxin Backup System. Antioxid. Redox Signaling 6, 63-74.
    • (2004) Antioxid. Redox Signaling , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 11
    • 67649800278 scopus 로고    scopus 로고
    • Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase
    • Avval, F. Z., and Holmgren, A. (2009) Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase. J. Biol. Chem. 284, 8233-8240.
    • (2009) J. Biol. Chem , vol.284 , pp. 8233-8240
    • Avval, F.Z.1    Holmgren, A.2
  • 12
    • 0028181442 scopus 로고
    • The Nuclear Magnetic Resonance Solution Structure of the Mixed Disulfide between Escherichia coli Glutaredoxin(C14S) and Glutathione
    • Bushweller, J. H., Billeter, M., Holmgren, A., and Wüthrich, K. (1994) The Nuclear Magnetic Resonance Solution Structure of the Mixed Disulfide between Escherichia coli Glutaredoxin(C14S) and Glutathione. J. Mol. Biol. 235, 1585-1597.
    • (1994) J. Mol. Biol , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wüthrich, K.4
  • 13
    • 33947327219 scopus 로고    scopus 로고
    • Structure of Glutaredoxin Grx1p C30S Mutant from Yeast
    • Hakansson, K. O., and Winther, J. R. (2007) Structure of Glutaredoxin Grx1p C30S Mutant from Yeast. Acta Crystallogr. D63, 288-294.
    • (2007) Acta Crystallogr , vol.D63 , pp. 288-294
    • Hakansson, K.O.1    Winther, J.R.2
  • 14
    • 0033582607 scopus 로고    scopus 로고
    • NMR Structure of Escherichia coli Glutaredoxin 3-Glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism
    • Nordstrand, K., Åslund, F., Holmgren, A., Otting, G., and Berndt, K. D. (1999) NMR Structure of Escherichia coli Glutaredoxin 3-Glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism. J. Mol. Biol. 286, 541-552.
    • (1999) J. Mol. Biol , vol.286 , pp. 541-552
    • Nordstrand, K.1    Åslund, F.2    Holmgren, A.3    Otting, G.4    Berndt, K.D.5
  • 15
    • 47349101604 scopus 로고    scopus 로고
    • Glutathionylation-Triggered Conformational Changes of Glutaredoxin Grx1 from the Yeast Saccharomyces cerevisiae
    • Yu, J., Zhang, N.-N., Yin, P.-D., Cui, P.-X., and Zhou, C.-Z. (2008) Glutathionylation-Triggered Conformational Changes of Glutaredoxin Grx1 from the Yeast Saccharomyces cerevisiae. Proteins 72, 1077-1083.
    • (2008) Proteins , vol.72 , pp. 1077-1083
    • Yu, J.1    Zhang, N.-N.2    Yin, P.-D.3    Cui, P.-X.4    Zhou, C.-Z.5
  • 16
    • 0032497928 scopus 로고    scopus 로고
    • Reactivity of the Human Thioltransferase (Glutaredoxin) C7S, C25S, C78S, C82S Mutant and NMR Solution Structure of Its Glutathionyl Mixed Disulfide Intermediate Reflect Catalytic Specificity
    • Yang, Y., Jao, S., Nanduri, S., Starke, D. W., Mieyal, J. J., and Qin, J. (1998) Reactivity of the Human Thioltransferase (Glutaredoxin) C7S, C25S, C78S, C82S Mutant and NMR Solution Structure of Its Glutathionyl Mixed Disulfide Intermediate Reflect Catalytic Specificity. Biochemistry 37, 17145-17156.
    • (1998) Biochemistry , vol.37 , pp. 17145-17156
    • Yang, Y.1    Jao, S.2    Nanduri, S.3    Starke, D.W.4    Mieyal, J.J.5    Qin, J.6
  • 18
    • 0026799490 scopus 로고
    • Structural and Functional Characterization of the Mutant Escherichia coli Glutaredoxin(C14S) and Its Mixed Disulfide with Glutathione
    • Bushweller, J. H.,Åslund, F.,Wüuthrich, K., and Holmgren, A. (1992) Structural and Functional Characterization of the Mutant Escherichia coli Glutaredoxin(C14S) and Its Mixed Disulfide with Glutathione. Biochemistry 31, 9288-9293.
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Åslund, F.2    Wüuthrich, K.3    Holmgren, A.4
  • 19
    • 33144474685 scopus 로고    scopus 로고
    • Mechanistic Insight Provided by Glutaredoxin within a Fusion to Redox-Sensitive Yellow Fluorescent Protein
    • Bjöornberg, O., Østergaard, H., and Winther, J. R. (2006) Mechanistic Insight Provided by Glutaredoxin within a Fusion to Redox-Sensitive Yellow Fluorescent Protein. Biochemistry 45, 2362-2371.
    • (2006) Biochemistry , vol.45 , pp. 2362-2371
    • Bjöornberg, O.1    Østergaard, H.2    Winther, J.R.3
  • 20
    • 2042476756 scopus 로고
    • Hydrogen Donor System for Escherichia coli Ribonucleoside-Diphosphate Reductase Dependent upon Glutathione
    • Holmgren, A. (1976) Hydrogen Donor System for Escherichia coli Ribonucleoside-Diphosphate Reductase Dependent upon Glutathione. Proc. Natl. Acad. Sci. U.S.A. 73, 2275-2279.
    • (1976) Proc. Natl. Acad. Sci. U.S.A , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 21
    • 33750621913 scopus 로고    scopus 로고
    • Insights into Deglutathionylation Reactions. Different Intermediates in the Glutaredoxin and Protein Disulfide Isomerase Catalyzed Reactions Are Defined by the γ-Linkage Present in Glutathione
    • Peltoniemi, M. J., Karala, A.-R., Jurvansuu, J. K., Kinnula, V. L., and Ruddock, L. W. (2006) Insights into Deglutathionylation Reactions. Different Intermediates in the Glutaredoxin and Protein Disulfide Isomerase Catalyzed Reactions Are Defined by the γ-Linkage Present in Glutathione. J. Biol. Chem. 281, 33107-33114.
    • (2006) J. Biol. Chem , vol.281 , pp. 33107-33114
    • Peltoniemi, M.J.1    Karala, A.-R.2    Jurvansuu, J.K.3    Kinnula, V.L.4    Ruddock, L.W.5
  • 22
    • 0032959801 scopus 로고    scopus 로고
    • Direct NMR Observation of the Cys-14 Thiol Proton of Reduced Escherichia coli Glutaredoxin-3 Supports the Presence of an Active Site Thiol-Thiolate Hydrogen Bond
    • Nordstrand, K., Åslund, F., Meunier, S., Holmgren, A., Otting, G., and Berndt, K. D. (1999) Direct NMR Observation of the Cys-14 Thiol Proton of Reduced Escherichia coli Glutaredoxin-3 Supports the Presence of an Active Site Thiol-Thiolate Hydrogen Bond. FEBS Lett. 449, 196-200.
    • (1999) FEBS Lett , vol.449 , pp. 196-200
    • Nordstrand, K.1    Åslund, F.2    Meunier, S.3    Holmgren, A.4    Otting, G.5    Berndt, K.D.6
  • 24
    • 64549161166 scopus 로고    scopus 로고
    • Kinetic and Thermodynamic Aspects of Cellular Thiol-Disulfide Redox Regulation
    • Jensen, K. S., Hansen, R. E., and Winther, J. R. (2009) Kinetic and Thermodynamic Aspects of Cellular Thiol-Disulfide Redox Regulation. Antioxid. Redox Signaling 11, 1047-1058.
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 1047-1058
    • Jensen, K.S.1    Hansen, R.E.2    Winther, J.R.3
  • 25
    • 0028871804 scopus 로고
    • How to Measure and Predict the Molar Absorption Coefficient of a
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to Measure and Predict the Molar Absorption Coefficient of a Protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein. Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 26
    • 0024356301 scopus 로고
    • Rapid Measurement of Binding Constants and Heats of Binding Using a New Titration Calorimeter
    • Wiseman, T., Williston, S., Brandts, J. F., and Lin, L.-N. (1989) Rapid Measurement of Binding Constants and Heats of Binding Using a New Titration Calorimeter. Anal. Biochem. 179, 131-137.
    • (1989) Anal. Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 27
    • 0028672570 scopus 로고
    • Determination of Accurate Thermodynamics of Binding by Titration Microcalorimetry
    • Bundle, D. R., and Sigurskjold, B. W. (1994) Determination of Accurate Thermodynamics of Binding by Titration Microcalorimetry. Methods Enzymol. 247, 288-305.
    • (1994) Methods Enzymol , vol.247 , pp. 288-305
    • Bundle, D.R.1    Sigurskjold, B.W.2
  • 30
    • 22544442178 scopus 로고    scopus 로고
    • Differential Scanning Calorimetry in Life Sciences: Thermodynamics, Stability, Molecular Recognition and Application in Drug Design
    • Bruylants, G., Wouters, J., and Michaux, C. (2005) Differential Scanning Calorimetry in Life Sciences: Thermodynamics, Stability, Molecular Recognition and Application in Drug Design. Curr. Med. Chem. 12, 2011-2020.
    • (2005) Curr. Med. Chem , vol.12 , pp. 2011-2020
    • Bruylants, G.1    Wouters, J.2    Michaux, C.3
  • 31
    • 75149156554 scopus 로고    scopus 로고
    • Freire, E., Luque, I., and Townsend, B. (2001) ASACalc v1.2: Calculation of Accessible Surface Areas, Biocalorimetry Center, Johns Hopkins University.
    • Freire, E., Luque, I., and Townsend, B. (2001) ASACalc v1.2: Calculation of Accessible Surface Areas, Biocalorimetry Center, Johns Hopkins University.
  • 32
    • 0015222647 scopus 로고
    • The Interpretation of Protein Structures: Estimation of StaticAccessibility
    • Lee, B., and Richards, F. M. (1971) The Interpretation of Protein Structures: Estimation of StaticAccessibility. J.Mol. Biol. 55, 379-400.
    • (1971) J.Mol. Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 33
    • 0022539027 scopus 로고
    • Peptide and Protein Molecular Weight Determination by Electrophoresis Using a High-Molarity Tris Buffer System without Urea
    • Fling, S. P., and Gregerson, D. S. (1986) Peptide and Protein Molecular Weight Determination by Electrophoresis Using a High-Molarity Tris Buffer System without Urea. Anal. Biochem. 155, 83-88.
    • (1986) Anal. Biochem , vol.155 , pp. 83-88
    • Fling, S.P.1    Gregerson, D.S.2
  • 34
    • 0035981605 scopus 로고    scopus 로고
    • Thermodynamic Quantities for the Ionization Reactions of Buffers
    • Goldberg, R. N., Kishore, N., and Lennen, R. M. (2002) Thermodynamic Quantities for the Ionization Reactions of Buffers. J. Phys. Chem. Ref. Data 31, 231-370.
    • (2002) J. Phys. Chem. Ref. Data , vol.31 , pp. 231-370
    • Goldberg, R.N.1    Kishore, N.2    Lennen, R.M.3
  • 35
    • 0026756702 scopus 로고
    • Thermodynamics of Structural Stability and Cooperative Folding Behavior in Proteins
    • Murphy, K. P., and Freire, E. (1992) Thermodynamics of Structural Stability and Cooperative Folding Behavior in Proteins. Adv. Protein Chem. 43, 313-361.
    • (1992) Adv. Protein Chem , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 36
    • 0025124855 scopus 로고
    • Yeast Thioltransferase - The Active Site Cysteines Display Differential reactivity
    • Gan, Z.-R., Sardana, M. K., Jacobs, J. W., and Polokoff, M. A. (1990) Yeast Thioltransferase - The Active Site Cysteines Display Differential reactivity. Arch. Biochem. Biophys. 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
  • 37
    • 0025887464 scopus 로고
    • Thioltransferase in Human Red Blood Cells: Kinetics and Equilibrium
    • Mieyal, J. J., Starke, D. W., Gravina, S. A., and Hocevar, B. A. (1991) Thioltransferase in Human Red Blood Cells: Kinetics and Equilibrium. Biochemistry 30, 8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 38
    • 0025788552 scopus 로고
    • Identification and Characterization of the Functional Amino Acids at the Active Center of Pig Liver Thioltransferase by Site-Directed Mutagenesis
    • Yang, Y., and Wells, W. W. (1991) Identification and Characterization of the Functional Amino Acids at the Active Center of Pig Liver Thioltransferase by Site-Directed Mutagenesis. J. Biol. Chem. 266, 12759-12765.
    • (1991) J. Biol. Chem , vol.266 , pp. 12759-12765
    • Yang, Y.1    Wells, W.W.2
  • 39
    • 33947087226 scopus 로고
    • Nuclear Magnetic Resonance Studies of the Acid-Base Chemistry of Amino Acids and Peptides. I. Microscopic Ionization Constants of Glutathione and Methylmercury-Complexed Glutathione
    • Rabenstein, D. L. (1973) Nuclear Magnetic Resonance Studies of the Acid-Base Chemistry of Amino Acids and Peptides. I. Microscopic Ionization Constants of Glutathione and Methylmercury-Complexed Glutathione. J. Am. Chem. Soc. 95, 2797-2803.
    • (1973) J. Am. Chem. Soc , vol.95 , pp. 2797-2803
    • Rabenstein, D.L.1
  • 40
    • 0028360184 scopus 로고
    • Reactivity and Ionization of the Active Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in Vivo
    • Nelson, J. W., and Creighton, T. E. (1994) Reactivity and Ionization of the Active Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in Vivo. Biochemistry 33, 5974-5983.
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 41
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of Linked Protonation Effects in Protein Binding Reactions Using Isothermal Titration Calorimetry
    • Baker, B. M., and Murphy, K. P. (1996) Evaluation of Linked Protonation Effects in Protein Binding Reactions Using Isothermal Titration Calorimetry. Biophys. J. 71, 2049-2055.
    • (1996) Biophys. J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 42
    • 57749093461 scopus 로고    scopus 로고
    • Quantifying Escherichia coli Glutaredoxin-3 Substrate Specificity Using Ligand-induced Stability
    • Elgán, T. H., and Berndt, K. D. (2008) Quantifying Escherichia coli Glutaredoxin-3 Substrate Specificity Using Ligand-induced Stability. J. Biol. Chem. 283, 32839-32847.
    • (2008) J. Biol. Chem , vol.283 , pp. 32839-32847
    • Elgán, T.H.1    Berndt, K.D.2
  • 43
    • 0000519682 scopus 로고
    • Reduction-Potential of Glutathione
    • Rost, J., and Rapoport, S. (1964) Reduction-Potential of Glutathione. Nature 201, 185.
    • (1964) Nature , vol.201 , pp. 185
    • Rost, J.1    Rapoport, S.2
  • 44
    • 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., and Holmgren, A. (1997) Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria. J. Biol. Chem. 272, 30780-30786.
    • (1997) J. Biol. Chem , vol.272 , pp. 30780-30786
    • Åslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 47
    • 0025118967 scopus 로고
    • Molecular and Cellular Aspects of Thiol-Disulfide Exchange
    • Gilbert, H. F. (1990) Molecular and Cellular Aspects of Thiol-Disulfide Exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63, 69-172.
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 48
    • 33847087446 scopus 로고
    • Rate Constants and Equilibrium Constants for Thiol-Disulfide Interchange Reactions Involving Oxidized Glutathione
    • Szajewski, R. P., and Whitesides, G. M. (1980) Rate Constants and Equilibrium Constants for Thiol-Disulfide Interchange Reactions Involving Oxidized Glutathione. J. Am. Chem. Soc. 102, 2011-2026.
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whitesides, G.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.