Synonyms
Historical Background
The name thioredoxin (Trx) was first introduced by Peter Reichard for the enzyme providing electrons needed for the enzymatic reaction of ribonucleotide reductase, in 1964 (Buchanan et al. 2012). However, Trxs have been described in yeast before, using different names: fraction C of the sulfate-reducing system and enzyme II of the enzymatic system reducing L-methionine sulfoxide. E. coli Trx1 was sequenced in 1968, revealing the characteristic Cys-Gly-Pro-Cys active site motif. In 1975, the crystal structure of oxidized E. coli Trx1 was solved, describing the characteristic Trx fold for the first time. The role of essential plant proteins for the process of photosynthesis, identified as Trxs in 1976–1978, is one of the first descriptions of biological redox regulation (Buchanan et al. 2012). All these mentioned early advances...
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Benhar M. Nitric oxide and the thioredoxin system: a complex interplay in redox regulation. Biochim Biophys Acta. 2015;1850(12):2476–84. https://doi.org/10.1016/j.bbagen.2015.09.010.
Berndt C, Lillig CH. Thioredoxins and glutaredoxins. Functions and metal ion interactions. In: Sigel A, Sigel H, RKO S, editors. Metallothioneins and related chelators, Metal ions in life sciences5 Cambridge, UK: Royal Society of Chemistry; 2009. p. 413–39.
Berndt C, Schwenn J-D, Lillig CH. The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity. Chem Sci. 2015;6(12):7049–58. https://doi.org/10.1039/C5SC01501D.
Buchanan BB, Holmgren A, Jacquot J-P, Scheibe R. Fifty years in the thioredoxin field and a bountiful harvest. Biochim Biophys Acta. 2012;1820(11):1822–9. https://doi.org/10.1016/j.bbagen.2012.07.006.
Collet J-F, D’Souza JC, Jakob U, Bardwell JCA. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J Biol Chem. 2003;278(46):45325–32. https://doi.org/10.1074/jbc.M307818200.
Czech MP, Lawrence JC, Lynn WS. Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin. Proc Natl Acad Sci U S A. 1974;71(10):4173–7.
Deponte M, Lillig CH. Enzymatic control of cysteinyl thiol switches in proteins. Biol Chem. 2015;396(5):401–13. https://doi.org/10.1515/hsz-2014-0280.
Eklund H, Cambillau C, Sjöberg BM, Holmgren A, Jörnvall H, Höög JO, et al. Conformational and functional similarities between glutaredoxin and thioredoxins. EMBO J. 1984;3(7):1443–9.
Hanschmann E-M, Godoy JR, Berndt C, Hudemann C, Lillig CH. Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling. Antioxid Redox Signal. 2013;19(13):1539–605. https://doi.org/10.1089/ars.2012.4599.
Hashemy SI, Holmgren A. Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues. J Biol Chem. 2008;283(32):21890–8. https://doi.org/10.1074/jbc.M801047200.
Hirota K, Murata M, Sachi Y, Nakamura H, Takeuchi J, Mori K, et al. Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB. J Biol Chem. 1999;274(39):27891–7. https://doi.org/10.1074/jbc.274.39.27891.
Ingles-Prieto A, Ibarra-Molero B, Delgado-Delgado A, Perez-Jimenez R, Fernandez JM, Gaucher EA, et al. Conservation of protein structure over four billion years. Struct Lond Engl 1993. 2013;21(9):1690–7. https://doi.org/10.1016/j.str.2013.06.020.
Meyer Y, Belin C, Delorme-Hinoux V, Reichheld J-P, Riondet C. Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance. Antioxid Redox Signal. 2012;17(8):1124–60. https://doi.org/10.1089/ars.2011.4327.
Mikami Y, Shibuya N, Kimura Y, Nagahara N, Ogasawara Y, Kimura H. Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Biochem J. 2011;439(3):479–85. https://doi.org/10.1042/BJ20110841.
Netto LES, Antunes F. The roles of peroxiredoxin and thioredoxin in hydrogen peroxide sensing and in signal transduction. Mol Cells. 2016;39(1):65–71. https://doi.org/10.14348/molcells.2016.2349.
Palde PB, Carroll KS. A universal entropy-driven mechanism for thioredoxin-target recognition. Proc Natl Acad Sci U S A. 2015;112(26):7960–5. https://doi.org/10.1073/pnas.1504376112.
Tao L, Jiao X, Gao E, Lau WB, Yuan Y, Lopez B, et al. Nitrative inactivation of thioredoxin-1 and its role in postischemic myocardial apoptosis. Circulation. 2006;114(13):1395–402. https://doi.org/10.1161/CIRCULATIONAHA.106.625061.
Vazquez DS, Delfino JM, Santos J. Thioredoxin from Escherichia coli as a role model of molecular recognition, folding, dynamics and function. Protein Pept Lett. 2015;22(9):801–15. https://doi.org/10.2174/0929866522666150707114309.
Watson WH, Pohl J, Montfort WR, Stuchlik O, Reed MS, Powis G, et al. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J Biol Chem. 2003;278(35):33408–15. https://doi.org/10.1074/jbc.M211107200.
Xu Z, Zhong L. New insights into the posttranslational regulation of human cytosolic thioredoxin by S-palmitoylation. Biochem Biophys Res Commun. 2015;460(4):949–56. https://doi.org/10.1016/j.bbrc.2015.03.132.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this entry
Cite this entry
Hanschmann, EM., Berndt, C. (2018). Thioredoxin (TXN). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101939
Download citation
DOI: https://doi.org/10.1007/978-3-319-67199-4_101939
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-67198-7
Online ISBN: 978-3-319-67199-4
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences