Protein Information

Name thioredoxin
Synonyms ADF; TRX 1; TRX1; ATL derived factor; SASP; Surface associated sulphydryl protein; TRDX; TRX…

Compound Information

Name sulfoxide
CAS 5-[2-(octylsulfinyl)propyl]-1,3-benzodioxole

Reference List

PubMed Abstract RScore(About this table)
18255097 Ranaivoson FM, Antoine M, Kauffmann B, Boschi-Muller S, Aubry A, Branlant G, Favier F: A structural analysis of the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis. J Mol Biol. 2008 Mar 14;377(1):268-80. Epub 2008 Jan 16.

The methionine sulfoxide reductases (Msrs) are thioredoxin-dependent oxidoreductases that catalyse the reduction of the sulfoxide function of the oxidized methionine residues.
32(0,1,1,2) Details
17761174 Vieira Dos Santos C, Laugier E, Tarrago L, Massot V, Issakidis-Bourguet E, Rouhier N, Rey P: Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B. FEBS Lett. 2007 Sep 18;581(23):4371-6. Epub 2007 Aug 14.

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20236937 Tarrago L, Laugier E, Zaffagnini M, Marchand CH, Le Marechal P, Lemaire SD, Rey P: The plant thioredoxin CDSP32 regenerates 1-CYS methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid. J Biol Chem. 2010 Mar 17.

2(0,0,0,2) Details
20306235 Hawkes WC, Alkan Z: Regulation of Redox Signaling by Selenoproteins. Biol Trace Elem Res. 2010 Mar 20.


Thioredoxin reductases (three genes) use nicotinamide adenine dinucleotide phosphate to reduce oxidized thioredoxin and its homologs, which regulate a plethora of redox signaling events.
2(0,0,0,2) Details
18990697 Fomenko DE, Novoselov SV, Natarajan SK, Lee BC, Koc A, Carlson BA, Lee TH, Kim HY, Hatfield DL, Gladyshev VN: MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form. J Biol Chem. 2009 Feb 27;284(9):5986-93. Epub 2008 Nov 6.

Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively.
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19733575 Ranaivoson FM, Neiers F, Kauffmann B, Boschi-Muller S, Branlant G, Favier F: Methionine sulfoxide reductase B displays a high level of flexibility. J Mol Biol. 2009 Nov 20;394(1):83-93. Epub 2009 Sep 4.

MsrB are stereospecific to R epimer on the sulfur of sulfoxide.
For the subclass of MsrB whose recycling process passes through the formation of an intradisulfide bond, the recycling reducer is thioredoxin.
2(0,0,0,2) Details
18452709 Kim HY, Kim JR: Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine. Biochem Biophys Res Commun. 2008 Jul 4;371(3):490-4. Epub 2008 Apr 29.

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19958171 Ugarte N, Petropoulos I, Friguet B: Oxidized Mitochondrial Protein Degradation and Repair in Aging and Oxidative Stress. Antioxid Redox Signal. 2010 Mar 8.


Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix.
1(0,0,0,1) Details
17500063 Gand A, Antoine M, Boschi-Muller S, Branlant G: Characterization of the amino acids involved in substrate specificity of methionine sulfoxide reductase A. J Biol Chem. 2007 Jul 13;282(28):20484-91. Epub 2007 May 11.

Methionine sulfoxide reductases (Msrs) are ubiquitous enzymes that catalyze the thioredoxin-dependent reduction of methionine sulfoxide (MetSO) back to methionine.
MsrAs are stereo-specific toward the S epimer on the sulfur of the sulfoxide, whereas MsrBs are specific toward the R isomer.
1(0,0,0,1) Details
19457862 Tarrago L, Laugier E, Zaffagnini M, Marchand C, Le Marechal P, Rouhier N, Lemaire SD, Rey P: Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins. J Biol Chem. 2009 Jul 10;284(28):18963-71. Epub 2009 May 20.

2(0,0,0,2) Details
18722338 Lee TH, Kim HY: An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide. Arch Biochem Biophys. 2008 Oct 15;478(2):175-80. Epub 2008 Aug 9.

However, a resolving Cys was required for the thioredoxin (Trx)-dependent recycling process of the Sec-containing form.
1(0,0,0,1) Details
18667555 Atack JM, Kelly DJ: Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni. Microbiology. 2008 Aug;154(Pt 8):2219-30.


Cj0637 and Cj1112 were overexpressed, purified and shown by a coupled thioredoxin-thioredoxin reductase-NADPH assay to catalyse the stereospecific reduction of the S and R diastereoisomers, respectively, of the model compound methyl p-tolyl sulphoxide.
1(0,0,0,1) Details
18206120 Rouhier N, Koh CS, Gelhaye E, Corbier C, Favier F, Didierjean C, Jacquot JP: Redox based anti-oxidant systems in plants: biochemical and structural analyses. Biochim Biophys Acta. 2008 Nov;1780(11):1249-60. Epub 2008 Jan 16.


We provide in this paper a comparative biochemical and structural analysis of the major thiol oxidoreductases (thioredoxin and glutaredoxin) of photosynthetic organisms in relation with their reductases and with target proteins, especially those involved either in the detoxication of peroxides such as hydrogen peroxide (thiol-peroxidases) or in the repair of oxidized methionines in proteins (methionine sulfoxide reductases).
1(0,0,0,1) Details
19665240 Wu TM, Hsu YT, Sung MS, Hsu YT, Lee TM: Expression of genes involved in redox homeostasis and antioxidant defense in a marine macroalga Ulva fasciata by excess copper. Aquat Toxicol. 2009 Oct 4;94(4):275-85. Epub 2009 Jul 19.


Redox-related genes, methionine sulfoxide reductase A (UfMsrA), thioredoxin (UfTrx), cyclophilin (UfCyp), and ferritin (UfFer) that were up-regulated by excess Cu [Wu, T.M., Lee, T.M., 2008.
1(0,0,0,1) Details
18651754 Quinternet M, Tsan P, Neiers F, Beaufils C, Boschi-Muller S, Averlant-Petit MC, Branlant G, Cung MT: Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis. Biochemistry. 2008 Aug 19;47(33):8577-89. Epub 2008 Jul 24.


The N-terminal domain, which possesses a CXXC motif, was recently shown to regenerate in vitro the reduced forms of the methionine sulfoxide reductase domains of PilB from their oxidized forms, as does the thioredoxin 1 from E. coli, via a disulfide bond exchange.
1(0,0,0,1) Details
17660280 Fukushima E, Shinka Y, Fukui T, Atomi H, Imanaka T: Methionine sulfoxide reductase from the hyperthermophilic archaeon Thermococcus kodakaraensis, an enzyme designed to function at suboptimal growth temperatures. J Bacteriol. 2007 Oct;189(19):7134-44. Epub 2007 Jul 27.


Methionine sulfoxide reductase (Msr) catalyzes the thioredoxin-dependent reduction and repair of methionine sulfoxide (MetO).
1(0,0,0,1) Details
17766244 Neiers F, Sonkaria S, Olry A, Boschi-Muller S, Branlant G: Characterization of the amino acids from Neisseria meningitidis methionine sulfoxide reductase B involved in the chemical catalysis and substrate specificity of the reductase step. J Biol Chem. 2007 Nov 2;282(44):32397-405. Epub 2007 Aug 31.

Methionine sulfoxide reductases (Msrs) are antioxidant repair enzymes that catalyze the thioredoxin-dependent reduction of methionine sulfoxide back to methionine.
The Msr family is composed of two structurally unrelated classes of enzymes named MsrA and MsrB, which display opposite stereoselectivities toward the S and R isomers of the sulfoxide function, respectively.
1(0,0,0,1) Details
18513221 Morel M, Kohler A, Martin F, Gelhaye E, Rouhier N: Comparison of the thiol-dependent antioxidant systems in the ectomycorrhizal Laccaria bicolor and the saprotrophic Phanerochaete chrysosporium. New Phytol. 2008;180(2):391-407. Epub 2008 May 28.


The two reducing systems (thioredoxin (Trx) and glutathione/glutaredoxin (Grx)) are of particular importance against oxidative insults, both for detoxification, through the regeneration of thiol-peroxidases, and for developmental, physiological and signalling processes.
1(0,0,0,1) Details
19049972 Le DT, Lee BC, Marino SM, Zhang Y, Fomenko DE, Kaya A, Hacioglu E, Kwak GH, Koc A, Kim HY, Gladyshev VN: Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae. J Biol Chem. 2009 Feb 13;284(7):4354-64. Epub 2008 Dec 2.

Molecular modeling and cysteine residue targeting by thioredoxin pointed to Cys (101) as catalytic and Cys (125) as resolving residues in yeast fRMsr.
MsrA and MsrB are the best known Msrs that repair methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO) residues in proteins, respectively.
1(0,0,0,1) Details
17460202 Koc A, Gladyshev VN: Methionine sulfoxide reduction and the aging process. Ann N Y Acad Sci. 2007 Apr;1100:383-6.


Methionine sulfoxide reductases, MsrA and MsrB, are thioredoxin-dependent oxidoreductases that reduce oxidized forms of methionine, methionine sulfoxides, in a stereospecific manner.
1(0,0,0,1) Details
18581249 Vinokur V, Grinberg L, Berenshtein E, Gross M, Moskovitz J, Reznick AZ, Chevion M, Eliashar R: Methionine-centered redox cycle in organs of the aero-digestive tract of young and old rats. Biogerontology. 2009 Feb;10(1):43-52. Epub 2008 Jun 26.


The levels of cytosolic thioredoxin (Trx), thioredoxin reductase (TrxR), and methionine sulfoxide reductase (Msr), all tended to decline with age.
1(0,0,0,1) Details
18845767 Luo S, Levine RL: Methionine in proteins defends against oxidative stress. FASEB J. 2009 Feb;23(2):464-72. Epub 2008 Oct 9.


Most cells contain methionine sulfoxide reductases, which catalyze a thioredoxin-dependent reduction of methionine sulfoxide back to methionine.
1(0,0,0,1) Details
17673175 Ding D, Sagher D, Laugier E, Rey P, Weissbach H, Zhang XH: Studies on the reducing systems for plant and animal thioredoxin-independent methionine sulfoxide reductases B. Biochem Biophys Res Commun. 2007 Sep 28;361(3):629-33. Epub 2007 Jul 25.

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