Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins

Couturier J, Stroeher E, Albetel A-N, Roret T, Muthuramalingam M, Tarrago L, Seidel T, Tsan P, Jacquot J-P, Johnson MK, Dietz K-J, et al. (2011)
Journal of Biological Chemistry 286(31): 27515-27527.

Zeitschriftenaufsatz | Veröffentlicht| Englisch
 
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Autor/in
Couturier, Jeremy; Stroeher, Elke; Albetel, Angela-Nadia; Roret, Thomas; Muthuramalingam, MeenakumariUniBi; Tarrago, Lionel; Seidel, ThorstenUniBi; Tsan, Pascale; Jacquot, Jean-Pierre; Johnson, Michael K.; Dietz, Karl-JosefUniBi; Didierjean, Claude
Alle
Abstract / Bemerkung
Unlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides (i.e. protein-glutathione adducts), and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, was shown to be localized in chloroplasts. A comparison of the biochemical, structural, and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicated that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the x-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys(32)) is required for cluster formation. In addition, thiol titrations, fluorescence measurements, and mass spectrometry analyses showed that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter-or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism.
Erscheinungsjahr
2011
Zeitschriftentitel
Journal of Biological Chemistry
Band
286
Ausgabe
31
Seite(n)
27515-27527
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/2326540

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Couturier J, Stroeher E, Albetel A-N, et al. Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry. 2011;286(31):27515-27527.
Couturier, J., Stroeher, E., Albetel, A. - N., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., et al. (2011). Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry, 286(31), 27515-27527. doi:10.1074/jbc.M111.228726
Couturier, J., Stroeher, E., Albetel, A. - N., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J. - P., Johnson, M. K., et al. (2011). Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry 286, 27515-27527.
Couturier, J., et al., 2011. Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry, 286(31), p 27515-27527.
J. Couturier, et al., “Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins”, Journal of Biological Chemistry, vol. 286, 2011, pp. 27515-27527.
Couturier, J., Stroeher, E., Albetel, A.-N., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J.-P., Johnson, M.K., Dietz, K.-J., Didierjean, C., Rouhier, N.: Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry. 286, 27515-27527 (2011).
Couturier, Jeremy, Stroeher, Elke, Albetel, Angela-Nadia, Roret, Thomas, Muthuramalingam, Meenakumari, Tarrago, Lionel, Seidel, Thorsten, Tsan, Pascale, Jacquot, Jean-Pierre, Johnson, Michael K., Dietz, Karl-Josef, Didierjean, Claude, and Rouhier, Nicolas. “Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins”. Journal of Biological Chemistry 286.31 (2011): 27515-27527.

40 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Structure analysis of yeast glutaredoxin Grx6 protein produced in Escherichia coli.
Abdalla M, Eltayb WA, El-Arabey AA, Mo R, Dafaalla TIM, Hamouda HI, Bhat EA, Awadasseid A, Ali HAA., Genes Environ 40(), 2018
PMID: 30123389
Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.
Zannini F, Roret T, Przybyla-Toscano J, Dhalleine T, Rouhier N, Couturier J., Antioxidants (Basel) 7(10), 2018
PMID: 30322144
Structural insights into the binding of buckwheat glutaredoxin with GSH and regulation of its catalytic activity.
Zhang X, Wang W, Li C, Zhao Y, Yuan H, Tan X, Wu L, Wang Z, Wang H., J Inorg Biochem 173(), 2017
PMID: 28478310
Glutathione, Glutaredoxins, and Iron.
Berndt C, Lillig CH., Antioxid Redox Signal 27(15), 2017
PMID: 28537421
1H, 13C and 15N resonance assignment of the cytosolic dithiol glutaredoxin 1 from the pathogen Trypanosoma brucei.
Stefani M, Sturlese M, Manta B, Löhr F, Mammi S, Comini M, Bellanda M., Biomol NMR Assign 10(1), 2016
PMID: 26386962
Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.
Abdalla M, Dai YN, Chi CB, Cheng W, Cao DD, Zhou K, Ali W, Chen Y, Zhou CZ., Acta Crystallogr F Struct Biol Commun 72(pt 10), 2016
PMID: 27710937
A comprehensive study of thiol reduction gene expression under stress conditions in Arabidopsis thaliana.
Belin C, Bashandy T, Cela J, Delorme-Hinoux V, Riondet C, Reichheld JP., Plant Cell Environ 38(2), 2015
PMID: 24428628
Arabidopsis glutaredoxin S17 and its partner, the nuclear factor Y subunit C11/negative cofactor 2α, contribute to maintenance of the shoot apical meristem under long-day photoperiod.
Knuesting J, Riondet C, Maria C, Kruse I, Bécuwe N, König N, Berndt C, Tourrette S, Guilleminot-Montoya J, Herrero E, Gaymard F, Balk J, Belli G, Scheibe R, Reichheld JP, Rouhier N, Rey P., Plant Physiol 167(4), 2015
PMID: 25699589
Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1.
Couturier J, Wu HC, Dhalleine T, Pégeot H, Sudre D, Gualberto JM, Jacquot JP, Gaymard F, Vignols F, Rouhier N., Mol Plant 7(1), 2014
PMID: 24203231
Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.
Yogavel M, Tripathi T, Gupta A, Banday MM, Rahlfs S, Becker K, Belrhali H, Sharma A., Acta Crystallogr D Biol Crystallogr 70(pt 1), 2014
PMID: 24419382
Evolutionary development of redox regulation in chloroplasts.
Balsera M, Uberegui E, Schürmann P, Buchanan BB., Antioxid Redox Signal 21(9), 2014
PMID: 24483204
[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis.
Banci L, Brancaccio D, Ciofi-Baffoni S, Del Conte R, Gadepalli R, Mikolajczyk M, Neri S, Piccioli M, Winkelmann J., Proc Natl Acad Sci U S A 111(17), 2014
PMID: 24733926
Structure-to-function relationships of bacterial translocator protein (TSPO): a focus on Pseudomonas.
Leneveu-Jenvrin C, Connil N, Bouffartigues E, Papadopoulos V, Feuilloley MG, Chevalier S., Front Microbiol 5(), 2014
PMID: 25477872
The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1.
Pégeot H, Koh CS, Petre B, Mathiot S, Duplessis S, Hecker A, Didierjean C, Rouhier N., Front Plant Sci 5(), 2014
PMID: 25566286
Two Sinorhizobium meliloti glutaredoxins regulate iron metabolism and symbiotic bacteroid differentiation.
Benyamina SM, Baldacci-Cresp F, Couturier J, Chibani K, Hopkins J, Bekki A, de Lajudie P, Rouhier N, Jacquot JP, Alloing G, Puppo A, Frendo P., Environ Microbiol 15(3), 2013
PMID: 22891731
Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.
Comini MA, Krauth-Siegel RL, Bellanda M., Antioxid Redox Signal 19(7), 2013
PMID: 22978520
Oxidative folding in chloroplasts.
Kieselbach T., Antioxid Redox Signal 19(1), 2013
PMID: 23289792
Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity.
Manta B, Pavan C, Sturlese M, Medeiros A, Crispo M, Berndt C, Krauth-Siegel RL, Bellanda M, Comini MA., Antioxid Redox Signal 19(7), 2013
PMID: 23259530
Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.
Liu X, Liu S, Feng Y, Liu JZ, Chen Y, Pham K, Deng H, Hirschi KD, Wang X, Cheng N., Proc Natl Acad Sci U S A 110(23), 2013
PMID: 23690600
Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.
Zhang B, Bandyopadhyay S, Shakamuri P, Naik SG, Huynh BH, Couturier J, Rouhier N, Johnson MK., J Am Chem Soc 135(40), 2013
PMID: 24032439
Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803.
Sánchez-Riego AM, López-Maury L, Florencio FJ., Front Plant Sci 4(), 2013
PMID: 24204369
Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties.
Zaffagnini M, Fermani S, Costa A, Lemaire SD, Trost P., Front Plant Sci 4(), 2013
PMID: 24282406
Glutaredoxin GRXS13 plays a key role in protection against photooxidative stress in Arabidopsis.
Laporte D, Olate E, Salinas P, Salazar M, Jordana X, Holuigue L., J Exp Bot 63(1), 2012
PMID: 21963612
A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies.
Chi XW, Lin CT, Jiang YC, Wen L, Lin CT., Plant Biol (Stuttg) 14(4), 2012
PMID: 22288388
Atypical thioredoxins in poplar: the glutathione-dependent thioredoxin-like 2.1 supports the activity of target enzymes possessing a single redox active cysteine.
Chibani K, Tarrago L, Gualberto JM, Wingsle G, Rey P, Jacquot JP, Rouhier N., Plant Physiol 159(2), 2012
PMID: 22523226
Protein-thiol oxidation and cell death: regulatory role of glutaredoxins.
Allen EM, Mieyal JJ., Antioxid Redox Signal 17(12), 2012
PMID: 22530666
Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance.
Meyer Y, Belin C, Delorme-Hinoux V, Reichheld JP, Riondet C., Antioxid Redox Signal 17(8), 2012
PMID: 22531002
Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro.
Bedhomme M, Adamo M, Marchand CH, Couturier J, Rouhier N, Lemaire SD, Zaffagnini M, Trost P., Biochem J 445(3), 2012
PMID: 22607208
Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin.
Wang L, Ouyang B, Li Y, Feng Y, Jacquot JP, Rouhier N, Xia B., Protein Cell 3(9), 2012
PMID: 22886498
The biological roles of glutaredoxins.
Ströher E, Millar AH., Biochem J 446(3), 2012
PMID: 22928493
Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A.
Couturier J, Vignols F, Jacquot JP, Rouhier N., FEBS Lett 586(21), 2012
PMID: 23022439

62 References

Daten bereitgestellt von Europe PubMed Central.

Thioredoxin--a fold for all reasons.
Martin JL., Structure 3(3), 1995
PMID: 7788290
A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.
Fernandes AP, Fladvad M, Berndt C, Andresen C, Lillig CH, Neubauer P, Sunnerhagen M, Holmgren A, Vlamis-Gardikas A., J. Biol. Chem. 280(26), 2005
PMID: 15833738
Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.
Rouhier N, Unno H, Bandyopadhyay S, Masip L, Kim SK, Hirasawa M, Gualberto JM, Lattard V, Kusunoki M, Knaff DB, Georgiou G, Hase T, Johnson MK, Jacquot JP., Proc. Natl. Acad. Sci. U.S.A. 104(18), 2007
PMID: 17460036
Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae.
Rodriguez-Manzaneque MT, Ros J, Cabiscol E, Sorribas A, Herrero E., Mol. Cell. Biol. 19(12), 1999
PMID: 10567543
Plant glutaredoxins: still mysterious reducing systems.
Rouhier N, Gelhaye E, Jacquot JP., Cell. Mol. Life Sci. 61(11), 2004
PMID: 15170506
Evolution and diversity of glutaredoxins in photosynthetic organisms.
Couturier J, Jacquot JP, Rouhier N., Cell. Mol. Life Sci. 66(15), 2009
PMID: 19506802
Exploring the active site of plant glutaredoxin by site-directed mutagenesis.
Rouhier N, Gelhaye E, Jacquot JP., FEBS Lett. 511(1-3), 2002
PMID: 11821065
Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor.
Rouhier N, Gelhaye E, Sautiere PE, Brun A, Laurent P, Tagu D, Gerard J, de Fay E, Meyer Y, Jacquot JP., Plant Physiol. 127(3), 2001
PMID: 11706208
Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins.
Tarrago L, Laugier E, Zaffagnini M, Marchand C, Le Marechal P, Rouhier N, Lemaire SD, Rey P., J. Biol. Chem. 284(28), 2009
PMID: 19457862
Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B.
Vieira Dos Santos C, Laugier E, Tarrago L, Massot V, Issakidis-Bourguet E, Rouhier N, Rey P., FEBS Lett. 581(23), 2007
PMID: 17761174
Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae.
Greetham D, Vickerstaff J, Shenton D, Perrone GG, Dawes IW, Grant CM., BMC Biochem. 11(), 2010
PMID: 20074363
Protein S-glutathionylation: a regulatory device from bacteria to humans.
Dalle-Donne I, Rossi R, Colombo G, Giustarini D, Milzani A., Trends Biochem. Sci. 34(2), 2009
PMID: 19135374
Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.
Bandyopadhyay S, Gama F, Molina-Navarro MM, Gualberto JM, Claxton R, Naik SG, Huynh BH, Herrero E, Jacquot JP, Johnson MK, Rouhier N., EMBO J. 27(7), 2008
PMID: 18354500
Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.
Rodriguez-Manzaneque MT, Tamarit J, Belli G, Ros J, Herrero E., Mol. Biol. Cell 13(4), 2002
PMID: 11950925
Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.
Lillig CH, Berndt C, Vergnolle O, Lonn ME, Hudemann C, Bill E, Holmgren A., Proc. Natl. Acad. Sci. U.S.A. 102(23), 2005
PMID: 15917333
Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site.
Feng Y, Zhong N, Rouhier N, Hase T, Kusunoki M, Jacquot JP, Jin C, Xia B., Biochemistry 45(26), 2006
PMID: 16800625
Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin.
Iwema T, Picciocchi A, Traore DA, Ferrer JL, Chauvat F, Jacquamet L., Biochemistry 48(26), 2009
PMID: 19505088
Structure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.
Couturier J, Koh CS, Zaffagnini M, Winger AM, Gualberto JM, Corbier C, Decottignies P, Jacquot JP, Lemaire SD, Didierjean C, Rouhier N., J. Biol. Chem. 284(14), 2009
PMID: 19158074
Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity.
Couturier J, Didierjean C, Jacquot JP, Rouhier N., Biochem. Biophys. Res. Commun. 403(3-4), 2010
PMID: 21094149

Behm M., Jacquot J.., 2000
Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis.
Horling F, Lamkemeyer P, Konig J, Finkemeier I, Kandlbinder A, Baier M, Dietz KJ., Plant Physiol. 131(1), 2003
PMID: 12529539
Regulation of gene expression by photosynthetic signals triggered through modified CO2 availability.
Wormuth D, Baier M, Kandlbinder A, Scheibe R, Hartung W, Dietz KJ., BMC Plant Biol. 6(), 2006
PMID: 16916444
Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements.
Seidel T, Golldack D, Dietz KJ., FEBS Lett. 579(20), 2005
PMID: 16061227
Protein measurement using bicinchoninic acid: elimination of interfering substances.
Brown RE, Jarvis KL, Hyland KJ., Anal. Biochem. 180(1), 1989
PMID: 2817336

Kabsch W.., 1993
The CCP4 suite: programs for protein crystallography.
Collaborative Computational Project, Number 4., Acta Crystallogr. D Biol. Crystallogr. 50(Pt 5), 1994
PMID: 15299374
Scaling and assessment of data quality.
Evans P., Acta Crystallogr. D Biol. Crystallogr. 62(Pt 1), 2005
PMID: 16369096

Vagin A., Teplyakov A.., 1997
Refinement of macromolecular structures by the maximum-likelihood method.
Murshudov GN, Vagin AA, Dodson EJ., Acta Crystallogr. D Biol. Crystallogr. 53(Pt 3), 1997
PMID: 15299926
Features and development of Coot.
Emsley P, Lohkamp B, Scott WG, Cowtan K., Acta Crystallogr. D Biol. Crystallogr. 66(Pt 4), 2010
PMID: 20383002
MolProbity: all-atom structure validation for macromolecular crystallography.
Chen VB, Arendall WB 3rd, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC., Acta Crystallogr. D Biol. Crystallogr. 66(Pt 1), 2009
PMID: 20057044
AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage.
Cheng NH, Liu JZ, Brock A, Nelson RS, Hirschi KD., J. Biol. Chem. 281(36), 2006
PMID: 16829529
Redox-dependent regulation of the stress-induced zinc-finger protein SAP12 in Arabidopsis thaliana.
Stroher E, Wang XJ, Roloff N, Klein P, Husemann A, Dietz KJ., Mol Plant 2(2), 2008
PMID: 19825620
Glutaredoxin from calf thymus. Purification to homogeneity.
Luthman M, Holmgren A., J. Biol. Chem. 257(12), 1982
PMID: 7045093
Functional analysis and expression characteristics of chloroplastic Prx IIE.
Gama F, Brehelin C, Gelhaye E, Meyer Y, Jacquot JP, Rey P, Rouhier N., Physiol Plant 133(3), 2008
PMID: 18422870
A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis.
Nikkola M, Gleason FK, Saarinen M, Joelson T, Bjornberg O, Eklund H., J. Biol. Chem. 266(24), 1991
PMID: 1874748
NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.
Nordstrand K, slund F, Holmgren A, Otting G, Berndt KD., J. Mol. Biol. 286(2), 1999
PMID: 9973569
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Xia TH, Bushweller JH, Sodano P, Billeter M, Bjornberg O, Holmgren A, Wuthrich K., Protein Sci. 1(3), 1992
PMID: 1304339
Glutaredoxins and thioredoxins in plants.
Meyer Y, Siala W, Bashandy T, Riondet C, Vignols F, Reichheld JP., Biochim. Biophys. Acta 1783(4), 2007
PMID: 18047840
Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions.
Gao XH, Zaffagnini M, Bedhomme M, Michelet L, Cassier-Chauvat C, Decottignies P, Lemaire SD., FEBS Lett. 584(11), 2010
PMID: 20406640
In vivo targets of S-thiolation in Chlamydomonas reinhardtii.
Michelet L, Zaffagnini M, Vanacker H, Le Marechal P, Marchand C, Schroda M, Lemaire SD, Decottignies P., J. Biol. Chem. 283(31), 2008
PMID: 18534986
Glutaredoxins: roles in iron homeostasis.
Rouhier N, Couturier J, Johnson MK, Jacquot JP., Trends Biochem. Sci. 35(1), 2009
PMID: 19811920
How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
Berndt C, Hudemann C, Hanschmann EM, Axelsson R, Holmgren A, Lillig CH., Antioxid. Redox Signal. 9(1), 2007
PMID: 17115894
The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.
Ceylan S, Seidel V, Ziebart N, Berndt C, Dirdjaja N, Krauth-Siegel RL., J. Biol. Chem. 285(45), 2010
PMID: 20826822
Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae.
Discola KF, de Oliveira MA, Rosa Cussiol JR, Monteiro G, Barcena JA, Porras P, Padilla CA, Guimaraes BG, Netto LE., J. Mol. Biol. 385(3), 2008
PMID: 18992757

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