ACS Publications. Most Trusted. Most Cited. Most Read

OR SEARCH CITATIONS

My Activity
Publications
CONTENT TYPES

Figure 1Loading Img
Download Hi-Res ImageDownload to MS-PowerPointCite This:Biochemistry 2014, 53, 38, 6113-6125
RETURN TO ISSUEPREVArticleNEXT

Deconstructing the Catalytic Efficiency of Peroxiredoxin-5 Peroxidatic Cysteine

View Author Information
† †Laboratorio de Fisicoquímica Biológica, ‡Laboratorio de Química Teórica y Computacional and ⊥Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay
§ Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Montevideo, Uruguay
∥ Laboratory of Cell Biology, Institut des Sciences de la Vie, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium
# Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo, Uruguay
*E-mail: [email protected]. Telephone/fax: 598 2525 0749.
Cite this: Biochemistry 2014, 53, 38, 6113–6125
Publication Date (Web):September 3, 2014
https://doi.org/10.1021/bi500389m
Copyright © 2014 American Chemical Society
Request reuse permissions

    Article Views

    869

    Altmetric

    -

    Citations

    59
    LEARN ABOUT THESE METRICS
    Other access options
    Get e-Alerts
    Supporting Info (2)»
    SUBJECTS:

    Abstract

    Abstract Image

    Human peroxiredoxin-5 (PRDX5) is a thiol peroxidase that reduces H2O2 105 times faster than free cysteine. To assess the influence of two conserved residues on the reactivity of the critical cysteine (C47), we determined the reaction rate constants of PRDX5, wild type (WT), T44V and R127Q with one substrate electrophile (H2O2) and a nonspecific electrophile (monobromobimane). We also studied the corresponding reactions of low molecular weight (LMW) thiolates in order to construct a framework against which we could compare our proteins. To obtain a detailed analysis of the structural and energetic changes involved in the reaction between WT PRDX5 and H2O2, we performed ONIOM quantum mechanics/molecular mechanics (QM/MM) calculations with a QM region including 60 atoms of substrate and active site described by the B3LYP density functional and the 6-31+G(d,p) basis set; the rest of the protein was included in the MM region. Brønsted correlations reveal that the absence of T44 can increase the general nucleophilicity of the C47 but decreases the specific reactivity toward H2O2 by a factor of 103. The R127Q mutation causes C47 to behave like a LMW thiolate in the two studied reactions. QM/MM results with WT PRDX5 showed that hydrogen bonds in the active site are the cornerstone of two effects that make catalysis possible: the enhancement of thiolate nucleophilicity upon substrate ingress and the stabilization of the transition state. In both effects, T44 has a central role. These effects occur in a precise temporal sequence that ensures that the selective nucleophilicity of C47 is available only for peroxide substrates.

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    Supporting Information

    ARTICLE SECTIONS
    Jump To

    Figure S1. Rationale for choosing the dielectric constant. Figure S2. UV titration curves and fits for the thiols used in the article. Table S1. Microscopic ionization constants for the aminothiols studied. Figure S3. pH profiles of the initial slope of fluorescence increase for PRDX5 T44V and R127Q reacting with mBBr at 25 °C. Table S2. Wiberg bond orders for relevant pairs of atoms at the active site of PRXD5 and EHOMO for points along the reaction coordinate. Table S3. NPA atomic charges for relevant atoms and functional groups at the active site of PRXD5 along the reaction coordinate. Table S4. Wiberg bond orders for proton acceptor/donor interactions at the active site of PRDX5. Figure S4. Evolution of the principal atomic pair distances involved in the heavy atom reorganization and proton transfer processes. Table S5. Coordinates for the optimized geometries of the IC, TS, and FC. Video SV1. An animated sequence of the structure evolution along the reaction coordinate obtained from the QM/MM calculations. This material is available free of charge via the Internet at http://pubs.acs.org.

    Terms & Conditions

    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    This article is cited by 59 publications.

    1. Lukas Lang, Ann-Cathrin Wolf, Mareike Riedel, Lea Thibol, Fabian Geissel, Kristina Feld, Jannik Zimmermann, Bruce Morgan, Georg Manolikakes, Marcel Deponte. Substrate Promiscuity and Hyperoxidation Susceptibility as Potential Driving Forces for the Co-evolution of Prx5-Type and Prx6-Type 1-Cys Peroxiredoxin Mechanisms. ACS Catalysis 2023, 13 (6) , 3627-3643. https://doi.org/10.1021/acscatal.2c04896
    2. Jyoti Singh, Daniel Whitaker, Benjamin Thoma, Saidul Islam, Callum S. Foden, Abil E. Aliev, Tom D. Sheppard, Matthew W. Powner. Prebiotic Catalytic Peptide Ligation Yields Proteinogenic Peptides by Intramolecular Amide Catalyzed Hydrolysis Facilitating Regioselective Lysine Ligation in Neutral Water. Journal of the American Chemical Society 2022, 144 (23) , 10151-10155. https://doi.org/10.1021/jacs.2c03486
    3. Kearsley M. Dillon, John B. Matson. A Review of Chemical Tools for Studying Small Molecule Persulfides: Detection and Delivery. ACS Chemical Biology 2021, 16 (7) , 1128-1141. https://doi.org/10.1021/acschembio.1c00255
    4. J. A. Semelak, F. Battistini, R. Radi, M. Trujillo, A. Zeida, D. A. Estrin. Multiscale Modeling of Thiol Overoxidation in Peroxiredoxins by Hydrogen Peroxide. Journal of Chemical Information and Modeling 2020, 60 (2) , 843-853. https://doi.org/10.1021/acs.jcim.9b00817
    5. Ari Zeida, Madia Trujillo, Gerardo Ferrer-Sueta, Ana Denicola, Darío A. Estrin, Rafael Radi. Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols. Chemical Reviews 2019, 119 (19) , 10829-10855. https://doi.org/10.1021/acs.chemrev.9b00371
    6. Stephanie Portillo-Ledesma, Lía M. Randall, Derek Parsonage, Joaquín Dalla Rizza, P. Andrew Karplus, Leslie B. Poole, Ana Denicola, Gerardo Ferrer-Sueta. Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing. Biochemistry 2018, 57 (24) , 3416-3424. https://doi.org/10.1021/acs.biochem.8b00188
    7. Milos R. Filipovic, Jasmina Zivanovic, Beatriz Alvarez, and Ruma Banerjee . Chemical Biology of H2S Signaling through Persulfidation. Chemical Reviews 2018, 118 (3) , 1253-1337. https://doi.org/10.1021/acs.chemrev.7b00205
    8. Gerardo Ferrer-Sueta, Nicolás Campolo, Madia Trujillo, Silvina Bartesaghi, Sebastián Carballal, Natalia Romero, Beatriz Alvarez, and Rafael Radi . Biochemistry of Peroxynitrite and Protein Tyrosine Nitration. Chemical Reviews 2018, 118 (3) , 1338-1408. https://doi.org/10.1021/acs.chemrev.7b00568
    9. Pramod K. Yadav, Michael Martinov, Victor Vitvitsky, Javier Seravalli, Rudolf Wedmann, Milos R. Filipovic, and Ruma Banerjee . Biosynthesis and Reactivity of Cysteine Persulfides in Signaling. Journal of the American Chemical Society 2016, 138 (1) , 289-299. https://doi.org/10.1021/jacs.5b10494
    10. Ari Zeida, Aníbal M. Reyes, Pablo Lichtig, Martín Hugo, Diego S. Vazquez, Javier Santos, F. Luis González Flecha, Rafael Radi, Dario A. Estrin, and Madia Trujillo . Molecular Basis of Hydroperoxide Specificity in Peroxiredoxins: The Case of AhpE from Mycobacterium tuberculosis. Biochemistry 2015, 54 (49) , 7237-7247. https://doi.org/10.1021/acs.biochem.5b00758
    11. Derek Parsonage, Kimberly J. Nelson, Gerardo Ferrer-Sueta, Samantha Alley, P. Andrew Karplus, Cristina M. Furdui, and Leslie B. Poole . Dissecting Peroxiredoxin Catalysis: Separating Binding, Peroxidation, and Resolution for a Bacterial AhpC. Biochemistry 2015, 54 (7) , 1567-1575. https://doi.org/10.1021/bi501515w
    12. Arden Perkins, Leslie B. Poole, and P. Andrew Karplus . Tuning of Peroxiredoxin Catalysis for Various Physiological Roles. Biochemistry 2014, 53 (49) , 7693-7705. https://doi.org/10.1021/bi5013222
    13. Lara Vogelsang, Jürgen Eirich, Iris Finkemeier, Karl-Josef Dietz. Specificity and dynamics of H2O2 detoxification by the cytosolic redox regulatory network as revealed by in vitro reconstitution. Redox Biology 2024, 72 , 103141. https://doi.org/10.1016/j.redox.2024.103141
    14. Dayana Benchoam, Ernesto Cuevasanta, Joseph V. Roman, Ruma Banerjee, Beatriz Alvarez. Acidity of persulfides and its modulation by the protein environments in sulfide quinone oxidoreductase and thiosulfate sulfurtransferase. Journal of Biological Chemistry 2024, 300 (5) , 107149. https://doi.org/10.1016/j.jbc.2024.107149
    15. Patrick A. Cardwell, Carlo Del Moro, Michael P. Murphy, Adrian J. Lapthorn, Richard C. Hartley. Human mitochondrial glutathione transferases: Kinetic parameters and accommodation of a mitochondria-targeting group in substrates. Bioorganic & Medicinal Chemistry 2024, 278 , 117712. https://doi.org/10.1016/j.bmc.2024.117712
    16. Sebastián F. Villar, Laura Corrales‐González, Belén Márquez de los Santos, Joaquín Dalla Rizza, Ari Zeida, Ana Denicola, Gerardo Ferrer‐Sueta. Kinetic and structural assessment of the reduction of human 2‐Cys peroxiredoxins by thioredoxins. The FEBS Journal 2024, 291 (4) , 778-794. https://doi.org/10.1111/febs.17006
    17. Noriko Noguchi, Yoshiro Saito, Etsuo Niki. Actions of Thiols, Persulfides, and Polysulfides as Free Radical Scavenging Antioxidants. Antioxidants & Redox Signaling 2023, 39 (10-12) , 728-743. https://doi.org/10.1089/ars.2022.0191
    18. Dayana Benchoam, Ernesto Cuevasanta, Jonathan A. Semelak, Mauricio Mastrogiovanni, Darío A. Estrin, Matías N. Möller, Beatriz Alvarez. Disulfides form persulfides at alkaline pH leading to potential overestimations in the cold cyanolysis method. Free Radical Biology and Medicine 2023, 207 , 63-71. https://doi.org/10.1016/j.freeradbiomed.2023.07.006
    19. Kei Goto, Tsukasa Sano, Ryosuke Masuda, Shotaro Otaka, Ryutaro Kimura, Shohei Sase, Satoru Kuwano. Stable cysteine sulfenic acid: synthesis by direct oxidation of a thiol, crystallographic analysis, and elucidation of reactivities. Phosphorus, Sulfur, and Silicon and the Related Elements 2023, 198 (6) , 466-470. https://doi.org/10.1080/10426507.2023.2195650
    20. Dayana Benchoam, Ernesto Cuevasanta, Matías N. Möller, Beatriz Alvarez. Persulfides and Their Reactions in Biological Contexts. 2022, 49-76. https://doi.org/10.1002/9781119799900.ch3
    21. Małgorzata Iciek, Anna Bilska-Wilkosz, Michał Kozdrowicki, Magdalena Górny. Reactive sulfur species and their significance in health and disease. Bioscience Reports 2022, 42 (9) https://doi.org/10.1042/BSR20221006
    22. Ernesto Cuevasanta, Dayana Benchoam, Jonathan A. Semelak, Matías N. Möller, Ari Zeida, Madia Trujillo, Beatriz Alvarez, Darío A. Estrin. Possible molecular basis of the biochemical effects of cysteine-derived persulfides. Frontiers in Molecular Biosciences 2022, 9 https://doi.org/10.3389/fmolb.2022.975988
    23. Xiaojia He, Zachery R. Jarrell, Yongliang Liang, Matthew Ryan Smith, Michael L. Orr, Lucian Marts, Young-Mi Go, Dean P. Jones. Vanadium pentoxide induced oxidative stress and cellular senescence in human lung fibroblasts. Redox Biology 2022, 55 , 102409. https://doi.org/10.1016/j.redox.2022.102409
    24. Brandán Pedre, Uladzimir Barayeu, Daria Ezeriņa, Tobias P. Dick. The mechanism of action of N-acetylcysteine (NAC): The emerging role of H2S and sulfane sulfur species. Pharmacology & Therapeutics 2021, 228 , 107916. https://doi.org/10.1016/j.pharmthera.2021.107916
    25. Mégane A. Poncin, Pierre Van Meerbeeck, Joshua D. Simpson, André Clippe, François Tyckaert, Fabrice Bouillenne, Hervé Degand, André Matagne, Pierre Morsomme, Bernard Knoops, David Alsteens. Role of the Redox State of Human Peroxiredoxin-5 on Its TLR4-Activating DAMP Function. Antioxidants 2021, 10 (12) , 1902. https://doi.org/10.3390/antiox10121902
    26. Carlos A. Tairum, Melina Cardoso Santos, Carlos Alexandre Breyer, Ana Laura Pires de Oliveira, Vitoria Isabela Montanhero Cabrera, Guilherme Toledo-Silva, Gustavo Maruyama Mori, Marcos Hikari Toyama, Luis Eduardo Soares Netto, Marcos Antonio de Oliveira. Effects of Serine or Threonine in the Active Site of Typical 2-Cys Prx on Hyperoxidation Susceptibility and on Chaperone Activity. Antioxidants 2021, 10 (7) , 1032. https://doi.org/10.3390/antiox10071032
    27. Jesalyn Bolduc, Katarina Koruza, Ting Luo, Julia Malo Pueyo, Trung Nghia Vo, Daria Ezeriņa, Joris Messens. Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities. Redox Biology 2021, 42 , 101959. https://doi.org/10.1016/j.redox.2021.101959
    28. Lucía Turell, Martina Steglich, Maria J. Torres, Matías Deambrosi, Laura Antmann, Cristina M. Furdui, Francisco J. Schopfer, Beatriz Alvarez. Sulfenic acid in human serum albumin: Reaction with thiols, oxidation and spontaneous decay. Free Radical Biology and Medicine 2021, 165 , 254-264. https://doi.org/10.1016/j.freeradbiomed.2021.01.039
    29. Dayana Benchoam, Jonathan A. Semelak, Ernesto Cuevasanta, Mauricio Mastrogiovanni, Juan S. Grassano, Gerardo Ferrer-Sueta, Ari Zeida, Madia Trujillo, Matías N. Möller, Darío A. Estrin, Beatriz Alvarez. Acidity and nucleophilic reactivity of glutathione persulfide. Journal of Biological Chemistry 2020, 295 (46) , 15466-15481. https://doi.org/10.1074/jbc.RA120.014728
    30. Nho Cong Luong, Yumi Abiko, Takahiro Shibata, Koji Uchida, Eiji Warabi, Midori Suzuki, Takuya Noguchi, Atsushi Matsuzawa, Yoshito Kumagai. Redox cycling of 9,10-phenanthrenequinone activates epidermal growth factor receptor signaling through S-oxidation of protein tyrosine phosphatase 1B. The Journal of Toxicological Sciences 2020, 45 (6) , 349-363. https://doi.org/10.2131/jts.45.349
    31. Jenner Bonanata, E. Laura Coitiño. Understanding the mechanism of H2S oxidation by flavin-dependent sulfide oxidases: a DFT/IEF-PCM study. Journal of Molecular Modeling 2019, 25 (10) https://doi.org/10.1007/s00894-019-4197-y
    32. Ernesto Cuevasanta, Aníbal M. Reyes, Ari Zeida, Mauricio Mastrogiovanni, María Inés De Armas, Rafael Radi, Beatriz Alvarez, Madia Trujillo. Kinetics of formation and reactivity of the persulfide in the one-cysteine peroxiredoxin from Mycobacterium tuberculosis. Journal of Biological Chemistry 2019, 294 (37) , 13593-13605. https://doi.org/10.1074/jbc.RA119.008883
    33. Lía M. Randall, Joaquín Dalla Rizza, Derek Parsonage, Javier Santos, Ryan A. Mehl, W. Todd Lowther, Leslie B. Poole, Ana Denicola. Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193. Free Radical Biology and Medicine 2019, 141 , 492-501. https://doi.org/10.1016/j.freeradbiomed.2019.07.016
    34. Nan Shu, Lasse G. Lorentzen, Michael J. Davies. Reaction of quinones with proteins: Kinetics of adduct formation, effects on enzymatic activity and protein structure, and potential reversibility of modifications. Free Radical Biology and Medicine 2019, 137 , 169-180. https://doi.org/10.1016/j.freeradbiomed.2019.04.026
    35. Bruno Manta, Matías N. Möller, Mariana Bonilla, Matías Deambrosi, Karin Grunberg, Massimo Bellanda, Marcelo A. Comini, Gerardo Ferrer-Sueta. Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites. Journal of Biological Chemistry 2019, 294 (9) , 3235-3248. https://doi.org/10.1074/jbc.RA118.006366
    36. Soma Jobbagy, Dario A. Vitturi, Sonia R. Salvatore, Lucía Turell, Maria F. Pires, Emilia Kansanen, Carlos Batthyany, Jack R. Lancaster, Bruce A. Freeman, Francisco J. Schopfer. Electrophiles modulate glutathione reductase activity via alkylation and upregulation of glutathione biosynthesis. Redox Biology 2019, 21 , 101050. https://doi.org/10.1016/j.redox.2018.11.008
    37. Dayana Benchoam, Ernesto Cuevasanta, Matías Möller, Beatriz Alvarez. Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species. Antioxidants 2019, 8 (2) , 48. https://doi.org/10.3390/antiox8020048
    38. Celien Lismont, Marcus Nordgren, Chantal Brees, Bernard Knoops, Paul P. Van Veldhoven, Marc Fransen. Peroxisomes as Modulators of Cellular Protein Thiol Oxidation: A New Model System. Antioxidants & Redox Signaling 2019, 30 (1) , 22-39. https://doi.org/10.1089/ars.2017.6997
    39. Brandán Pedre, David Young, Daniel Charlier, Álvaro Mourenza, Leonardo Astolfi Rosado, Laura Marcos-Pascual, Khadija Wahni, Edo Martens, Alfonso G. de la Rubia, Vsevolod V. Belousov, Luis M. Mateos, Joris Messens. Structural snapshots of OxyR reveal the peroxidatic mechanism of H 2 O 2 sensing. Proceedings of the National Academy of Sciences 2018, 115 (50) https://doi.org/10.1073/pnas.1807954115
    40. Lucía Turell, Martina Steglich, Beatriz Alvarez. The chemical foundations of nitroalkene fatty acid signaling through addition reactions with thiols. Nitric Oxide 2018, 78 , 161-169. https://doi.org/10.1016/j.niox.2018.03.014
    41. Kimberly J. Nelson, Arden Perkins, Amanda E.D. Van Swearingen, Steven Hartman, Andrew E. Brereton, Derek Parsonage, Freddie R. Salsbury, P. Andrew Karplus, Leslie B. Poole. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxidants & Redox Signaling 2018, 28 (7) , 521-536. https://doi.org/10.1089/ars.2016.6922
    42. Aníbal M. Reyes, Brandán Pedre, María Inés De Armas, Maria-Armineh Tossounian, Rafael Radi, Joris Messens, Madia Trujillo. Chemistry and Redox Biology of Mycothiol. Antioxidants & Redox Signaling 2018, 28 (6) , 487-504. https://doi.org/10.1089/ars.2017.7074
    43. Bruno Manta, Mariana Bonilla, Lucía Fiestas, Mattia Sturlese, Gustavo Salinas, Massimo Bellanda, Marcelo A. Comini. Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions. Antioxidants & Redox Signaling 2018, 28 (6) , 463-486. https://doi.org/10.1089/ars.2017.7133
    44. Yogesh Mishra, Michael Hall, Roland Locmelis, Kwangho Nam, Christopher A. G. Söderberg, Patrik Storm, Neha Chaurasia, Lal Chand Rai, Stefan Jansson, Wolfgang P. Schröder, Uwe H. Sauer. Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. Scientific Reports 2017, 7 (1) https://doi.org/10.1038/s41598-017-17044-3
    45. Paula Arbildi, Lucía Turell, Verónica López, Beatriz Alvarez, Verónica Fernández. Mechanistic insights into EgGST1, a Mu class glutathione S-transferase from the cestode parasite Echinococcus granulosus. Archives of Biochemistry and Biophysics 2017, 633 , 15-22. https://doi.org/10.1016/j.abb.2017.08.014
    46. Jenner Bonanata, Lucía Turell, Laura Antmann, Gerardo Ferrer-Sueta, Santiago Botasini, Eduardo Méndez, Beatriz Alvarez, E. Laura Coitiño. The thiol of human serum albumin: Acidity, microenvironment and mechanistic insights on its oxidation to sulfenic acid. Free Radical Biology and Medicine 2017, 108 , 952-962. https://doi.org/10.1016/j.freeradbiomed.2017.04.021
    47. Jean‐Philippe R. Chauvin, Derek A. Pratt. On the Reactions of Thiols, Sulfenic Acids, and Sulfinic Acids with Hydrogen Peroxide. Angewandte Chemie International Edition 2017, 56 (22) , 6255-6259. https://doi.org/10.1002/anie.201610402
    48. Jean‐Philippe R. Chauvin, Derek A. Pratt. On the Reactions of Thiols, Sulfenic Acids, and Sulfinic Acids with Hydrogen Peroxide. Angewandte Chemie 2017, 129 (22) , 6351-6355. https://doi.org/10.1002/ange.201610402
    49. Ernesto Cuevasanta, Matías N. Möller, Beatriz Alvarez. Biological chemistry of hydrogen sulfide and persulfides. Archives of Biochemistry and Biophysics 2017, 617 , 9-25. https://doi.org/10.1016/j.abb.2016.09.018
    50. Thiago G. P. Alegria, Diogo A. Meireles, José R. R. Cussiol, Martín Hugo, Madia Trujillo, Marcos Antonio de Oliveira, Sayuri Miyamoto, Raphael F. Queiroz, Napoleão Fonseca Valadares, Richard C. Garratt, Rafael Radi, Paolo Di Mascio, Ohara Augusto, Luis E. S. Netto. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite. Proceedings of the National Academy of Sciences 2017, 114 (2) https://doi.org/10.1073/pnas.1619659114
    51. Lucía Turell, Darío A. Vitturi, E. Laura Coitiño, Lourdes Lebrato, Matías N. Möller, Camila Sagasti, Sonia R. Salvatore, Steven R. Woodcock, Beatriz Alvarez, Francisco J. Schopfer. The Chemical Basis of Thiol Addition to Nitro-conjugated Linoleic Acid, a Protective Cell-signaling Lipid. Journal of Biological Chemistry 2017, 292 (4) , 1145-1159. https://doi.org/10.1074/jbc.M116.756288
    52. Carlos A. Tairum, Melina Cardoso Santos, Carlos A. Breyer, R. Ryan Geyer, Cecilia J. Nieves, Stephanie Portillo-Ledesma, Gerardo Ferrer-Sueta, José Carlos Toledo, Marcos H. Toyama, Ohara Augusto, Luis E. S. Netto, Marcos A. de Oliveira. Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms. Scientific Reports 2016, 6 (1) https://doi.org/10.1038/srep33133
    53. Arden Perkins, Derek Parsonage, Kimberly J. Nelson, O. Maduka Ogba, Paul Ha-Yeon Cheong, Leslie B. Poole, P. Andrew Karplus. Peroxiredoxin Catalysis at Atomic Resolution. Structure 2016, 24 (10) , 1668-1678. https://doi.org/10.1016/j.str.2016.07.012
    54. Madia Trujillo, Beatriz Alvarez, Rafael Radi. One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates. Free Radical Research 2016, 50 (2) , 150-171. https://doi.org/10.3109/10715762.2015.1089988
    55. Lía Randall, Bruno Manta, Kimberly J. Nelson, Javier Santos, Leslie B. Poole, Ana Denicola. Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form. Archives of Biochemistry and Biophysics 2016, 590 , 101-108. https://doi.org/10.1016/j.abb.2015.11.032
    56. Brandán Pedre, Laura A. H. van Bergen, Anna Palló, Leonardo A. Rosado, Veronica Tamu Dufe, Inge Van Molle, Khadija Wahni, Huriye Erdogan, Mercedes Alonso, Frank De Proft, Joris Messens. The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE. Chemical Communications 2016, 52 (67) , 10293-10296. https://doi.org/10.1039/C6CC02645A
    57. Bernard Knoops, Vasiliki Argyropoulou, Sarah Becker, Laura Ferté, Oksana Kuznetsova. Multiple Roles of Peroxiredoxins in Inflammation. Molecules and Cells 2016, 39 (1) , 60-64. https://doi.org/10.14348/molcells.2016.2341
    58. Ernesto Cuevasanta, Mike Lange, Jenner Bonanata, E. Laura Coitiño, Gerardo Ferrer-Sueta, Milos R. Filipovic, Beatriz Alvarez. Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide. Journal of Biological Chemistry 2015, 290 (45) , 26866-26880. https://doi.org/10.1074/jbc.M115.672816
    59. Arden Perkins, Kimberly J. Nelson, Derek Parsonage, Leslie B. Poole, P. Andrew Karplus. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends in Biochemical Sciences 2015, 40 (8) , 435-445. https://doi.org/10.1016/j.tibs.2015.05.001
    Download PDF

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect