722
Views
57
CrossRef citations to date
0
Altmetric
Review Article

Thiyl radicals and induction of protein degradation

Pages 143-149 | Received 07 Jun 2015, Accepted 21 Jul 2015, Published online: 11 Sep 2015

References

  • Davies KJ. Protein damage and degradation by oxygen radicals. I. General aspects. J Biol Chem 1987;262:9895–9901.
  • Davies KJ, Delsignore ME, Lin SW. Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J Biol Chem 1987;262:9902–9907.
  • Davies KJ, Delsignore ME. Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. J Biol Chem 1987;262:9908–9913.
  • Davies KJ, Goldberg AL. Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells. J Biol Chem 1987;262:8227–8234.
  • Stadtman ER. Protein oxidation and aging. Science 1992;257:1220–1224.
  • Stadtman ER, Oliver CN, Levine RL, Fucci L, Rivett AJ. Implication of protein oxidation in protein turnover, aging, and oxygen toxicity. Basic Life Sci 1988;49:331–339.
  • Amici A, Levine RL, Tsai L, Stadtman ER. Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. J Biol Chem 1989;264:3341–3346.
  • Davies MJ. The oxidative environment and protein damage. Biochim Biophys Acta 2005;1703:93–109.
  • Neuzil J, Gebicki JM, Stocker R. Radical-induced chain oxidation of proteins and its inhibition by chain-breaking antioxidants. Biochem J 1993;293 (Pt 3):601–606.
  • Garcia-Santamarina S, Boronat S, Hidalgo E. Reversible cysteine oxidation in hydrogen peroxide sensing and signal transduction. Biochemistry 2014;53:2560–2580.
  • Winterbourn CC, Hampton MB. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 2008;45: 549–561.
  • Jones DP. Radical-free biology of oxidative stress. Am J Physiol Cell Physiol 2008;295:C849–C868.
  • Schöneich C. Mechanisms of protein damage induced by cysteine thiyl radical formation. Chem Res Toxicol 2008; 21:1175–1179.
  • Akhlaq MS, Schuchmann HP, von Sonntag C. The reverse of the ‘repair’ reaction of thiols: H-abstraction at carbon by thiyl radicals. Int J Radiat Biol Relat Stud Phys Chem Med 1987;51:91–102.
  • Karoui H, Hogg N, Frejaville C, Tordo P, Kalyanaraman B. Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. ESR-spin trapping and oxygen uptake studies. J Biol Chem 1996;271:6000–6009.
  • Sevilla MD, Becker D, Yan M. The formation and structure of the sulfoxyl radicals RSO(.), RSOO(.), RSO2(.), and RSO2OO(.) from the reaction of cysteine, glutathione and penicillamine thiyl radicals with molecular oxygen. Int J Radiat Biol 1990;57:65–81.
  • Zhang X, Zhang N, Schuchmann H-P, von Sonntag C. Pulse radiolysis of 2-mercaptoethanol in oxygenated aqueous solution. Generation and reactions of the thiylperoxyl radical. J Phys Chem 1994;98:6541–6547.
  • Bonifacic M, Asmus KD. Adduct Formation and Absolute Rate Constants in the Displacement Reaction of Thiyl Radicals with Disulfides. J Phys Chem 1984;88:6286–6290.
  • Winterbourn CC. Are free radicals involved in thiol-based redox signaling? Free Radic Biol Med 2015;80:164–170.
  • Nauser T, Koppenol WH, Schöneich C. Protein thiyl radical reactions and product formation: a kinetic simulation. Free Radic Biol Med 2015;80:158–163.
  • Maples KR, Kennedy CH, Jordan SJ, Mason RP. In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides. Arch Biochem Biophys 1990;277: 402–409.
  • Venters HD, Jr., Bonilla LE, Jensen T, Garner HP, Bordayo EZ, Najarian MM, et al. Heme from Alzheimer's brain inhibits muscarinic receptor binding via thiyl radical generation. Brain research 1997;764:93–100.
  • Svistunenko DA. Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view. Biochim Biophys Acta 2005;1707:127–155.
  • Meneghini R. Iron homeostasis, oxidative stress, and DNA damage. Free Radic Biol Med 1997;23:783–92.
  • Schrag M, Mueller C, Zabel M, Crofton A, Kirsch WM, Ghribi O, et al. Oxidative stress in blood in Alzheimer's disease and mild cognitive impairment: a meta-analysis. Neurobiol Dis 2013;59:100–110.
  • Chen P, Chakraborty S, Mukhopadhyay S, Lee E, Paoliello MM, Bowman AB, et al. Manganese Homeostasis in the Nervous System. J Neurochem 2015; May 16. doi: 10.1111/jnc.13170. [Epub ahead of print]
  • Chen P, Parmalee N, Aschner M. Genetic factors and manganese-induced neurotoxicity. Front Genet 2014;5:265.
  • Petruk AA, Bartesaghi S, Trujillo M, Estrin DA, Murgida D, Kalyanaraman B, et al. Molecular basis of intramolecular electron transfer in proteins during radical-mediated oxidations: computer simulation studies in model tyrosine-cysteine peptides in solution. Arch Biochem Biophys 2012;525:82–91.
  • Pietraforte D, Minetti M. Direct ESR detection or peroxynitrite-induced tyrosine-centred protein radicals in human blood plasma. Biochem J 1997;325 (Pt 3):675–684.
  • Grierson L, Hildenbrand K, Bothe E. Intramolecular transformation reaction of the glutathione thiyl radical into a non-sulphur-centred radical: a pulse-radiolysis and EPR study. Int J Radiat Biol 1992;62:265–277.
  • Chen Y, Barkley MD. Toward understanding tryptophan fluorescence in proteins. Biochemistry 1998;37:9976–9982.
  • Hildenbrand K, Schulte-Frohlinde D. Time-resolved EPR studies on the reaction rates of peroxyl radicals of poly(acrylic acid) and of calf thymus DNA with glutathione. Re-examination of a rate constant for DNA. Int J Radiat Biol 1997;71: 377–385.
  • Jones CM, Lawrence A, Wardman P, Burkitt MJ. Kinetics of superoxide scavenging by glutathione: an evaluation of its role in the removal of mitochondrial superoxide. Biochem Soc Trans 2003;31:1337–1339.
  • Jones CM, Lawrence A, Wardman P, Burkitt MJ. Electron paramagnetic resonance spin trapping investigation into the kinetics of glutathione oxidation by the superoxide radical: re-evaluation of the rate constant. Free Radic Biol Med 2002;32:982–990.
  • Kang PT, Chen CL, Chen YR. Increased mitochondrial prooxidant activity mediates up-regulation of Complex I S-glutathionylation via protein thiyl radical in the murine heart of eNOS(-/-). Free Radic Biol Med 2015;79:56–68.
  • Kang PT, Zhang L, Chen CL, Chen J, Green KB, Chen YR. Protein thiyl radical mediates S-glutathionylation of complex I. Free Radic Biol Med 2012;53:962–973.
  • Chen CA, Lin CH, Druhan LJ, Wang TY, Chen YR, Zweier JL. Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling. J Biol Chem 2011;286:29098–29107.
  • Zweier JL, Chen CA, Druhan LJ. S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide/reactive oxygen species-mediated signaling. Antioxidants & redox signaling 2011;14: 1769–1775.
  • Ford E, Hughes MN, Wardman P. Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological pH. Free Radic Biol Med 2002;32:1314–1323.
  • Augusto O, Bonini MG, Amanso AM, Linares E, Santos CC, De Menezes SL. Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology. Free Radic Biol Med 2002;32:841–859.
  • Davis MF, Vigil D, Campbell SL. Regulation of Ras proteins by reactive nitrogen species. Free Radic Biol Med 2011;51: 565–575.
  • Davis MF, Zhou L, Ehrenshaft M, Ranguelova K, Gunawardena HP, Chen X, et al. Detection of Ras GTPase protein radicals through immuno-spin trapping. Free Radic Biol Med 2012;53:1339–1345.
  • Mitchell L, Hobbs GA, Aghajanian A, Campbell SL. Redox regulation of Ras and Rho GTPases: mechanism and function. Antioxidants & Redox Signaling 2013;18:250–258.
  • Raines KW, Bonini MG, Campbell SL. Nitric oxide cell signaling: S-nitrosation of Ras superfamily GTPases. Cardiovasc Res 2007;75:229–239.
  • Jourd'heuil D, Jourd'heuil FL, Feelisch M. Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism. J Biol Chem 2003;278:15720–15726.
  • Bosworth CA, Toledo JC, Jr., Zmijewski JW, Li Q, Lancaster JR, Jr. Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide. Proc Natl Acad Sci U S A 2009;106: 4671–4676.
  • Hobbs GA, Mitchell LE, Arrington ME, Gunawardena HP, DeCristo MJ, Loeser RF, et al. Redox regulation of Rac1 by thiol oxidation. Free Radic Biol Med 2015;79:237–250.
  • Pryor WA, Gojon G, Church DF. Relative Rate Constants for Hydrogen Atom Abstraction by the Cyclohexanethiyl and Benzenethiyl Radicals. J Org Chem 1978;43:793–800.
  • Pryor WA, Gojon G, Stanley JP. Hydrogen abstraction by thiyl radicals. J Am Chem Soc 1973;95:945–946.
  • Dang HS, Roberts BP, Sekhon J, Smits TM. Deoxygenation of carbohydrates by thiol-catalysed radical-chain redox rearrangement of the derived benzylidene acetals. Org Biomol Chem 2003;1:1330–1341.
  • Dang HS, Roberts BP, Tocher DA. Thiol-catalysed radical-chain redox rearrangement reactions of benzylidene acetals derived from terpenoid diols. Org Biomol Chem 2003;1: 4073–4084.
  • Nauser T, Pelling J, Schöneich C. Thiyl radical reaction with amino acid side chains: rate constants for hydrogen transfer and relevance for posttranslational protein modification. Chem Res Toxicol 2004;17:1323–1328.
  • Nauser T, Schöneich C. Thiyl radicals abstract hydrogen atoms from the (alpha)C-H bonds in model peptides: absolute rate constants and effect of amino acid structure. J Am Chem Soc 2003;125:2042–2043.
  • Nauser T, Casi G, Koppenol WH, Schöneich C. Reversible intramolecular hydrogen transfer between cysteine thiyl radicals and glycine and alanine in model peptides: absolute rate constants derived from pulse radiolysis and laser flash photolysis. J Phys Chem B 2008;112:15034–15044.
  • Marino SM, Gladyshev VN. Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces. J Mol Biol 2010;404:902–916.
  • Biaglow JE, Ayene IS, Tuttle SW, Koch CJ, Donahue J, Mieyal JJ. Role of vicinal protein thiols in radiation and cytotoxic responses. Radiat Res 2006;165:307–317.
  • Chatterjee A. Reduced glutathione: a radioprotector or a modulator of DNA-repair activity? Nutrients 2013;5: 525–42.
  • Svoboda P, Harms-Ringdahl M. Protection or sensitization by thiols or ascorbate in irradiated solutions of DNA or deoxyguanosine. Radiat Res 1999;151:605–616.
  • Mozziconacci O, Sharov V, Williams TD, Kerwin BA, Schöneich C. Peptide cysteine thiyl radicals abstract hydrogen atoms from surrounding amino acids: the photolysis of a cystine containing model peptide. J Phys Chem B 2008;112: 9250–9257.
  • Mozziconacci O, Kerwin BA, Schöneich C. Reversible hydrogen transfer between cysteine thiyl radical and glycine and alanine in model peptides: covalent H/D exchange, radical-radical reactions, and L− to D-Ala conversion. J Phys Chem B 2010;114:6751–6762.
  • Hofstetter D, Nauser T, Koppenol WH. Hydrogen exchange equilibria in glutathione radicals: rate constants. Chem Res Toxicol 2010;23:1596–1600.
  • Mozziconacci O, Williams TD, Schöneich C. Intramolecular hydrogen transfer reactions of thiyl radicals from glutathione: formation of carbon-centered radical at Glu, Cys, and Gly. Chem Res Toxicol 2012;25:1842–1861.
  • Hofstetter D, Thalmann B, Nauser T, Koppenol WH. Hydrogen exchange equilibria in thiols. Chem Res Toxicol 2012;25: 1862–1867.
  • Zhao R, Lind J, Merenyi G, Eriksen TE. Significance of the intramolecular transformation of glutathione thiyl radicals to alpha-aminoalkyl radicals. Thermochemical and biological implications. J Chem Soc Perk T 2 1997:569–574.
  • Zhao R, Lind J, Merenyi G, Eriksen TE. Kinetics of One-Electron Oxidation of Thiols and Hydrogen Abstraction by Thiyl Radicals from Alpha-Amino C-H Bonds. J Am Chem Soc 1994;116:12010–12015.
  • Nauser T, Koppenol WH, Schöneich C. Reversible hydrogen transfer reactions in thiyl radicals from cysteine and related molecules: absolute kinetics and equilibrium constants determined by pulse radiolysis. J Phys Chem B 2012;116:5329–5341.
  • Wei Y, Mathies G, Yokoyama K, Chen J, Griffin RG, Stubbe J. A chemically competent thiosulfuranyl radical on the Escherichia coli class III ribonucleotide reductase. J Am Chem Soc 2014;136:9001–13.
  • Fossey J, Sorba J. HO and HS substituent effect on alkyl radicals: an ab-initio molecular orbital study. J Mol Struct 1989;186:305–319.
  • Naumov S, Von Sonntag C. UV/Vis absorption spectra of alkyl-, vinyl-, aryl- and thioperoxyl radicals and some related radicals in aqueous solution. J Phys Org Chem 2005;18:586–594.
  • Morris M, Chan B, Radom L. Heteroatomic deprotonation of substituted methanes and methyl radicals: theoretical insights into structure, stability, and thermochemistry. J Phys Chem A 2012;116:12381–12387.
  • Asmus KD, Henglein A, Wigger A, Beck G. Pulsradiolytische Versuche zur elektrolytischen Dissoziation von aliphatischen Alkoholradikalen. Berichte der Bunsengesellschaft für Physikalische Chemie 1966;70:756–758.
  • Simic M, Neta P, Hayon E. Pulse radiolysis study of alcohols in aqueous solution. J Phys Chem 1969;73:3794–3800.
  • Mozziconacci O, Kerwin BA, Schöneich C. Photolysis of an intrachain peptide disulfide bond: primary and secondary processes, formation of H2S, and hydrogen transfer reactions. J Phys Chem B 2010;114:3668–3688.
  • Mozziconacci O, Kerwin BA, Schöneich C. Reversible hydrogen transfer reactions of cysteine thiyl radicals in peptides: the of cysteine into dehydroalanine and alanine, and of alanine into dehydroalanine. J Phys Chem B 2011;115:12287–12305.
  • Mozziconacci O, Haywood J, Gorman EM, Munson E, Schöneich C. Photolysis of recombinant human insulin in the solid state: formation of a dithiohemiacetal product at the C-terminal disulfide bond. Pharm Res 2012;29:121–133.
  • Dae-Kyung K, Jeong J, Drake SK, Wehr NB, Rouault TA, Levine RL. Iron regulatory protein 2 as iron sensor. J Biol Chem 2003;278:14857–14864.
  • Jeong J, Rouault TA, Levine RL. Identification of a heme-sensing domain in iron regulatory protein 2. J Biol Chem 2004;279:45450–45454.
  • Garrison WM. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem Rev 1987;87:381–398.
  • Block DA, Yu D, Armstrong DA, Rauk A. On the influence of secondary structure on the alpha-C-H bond dissociation energy of proline residues in proteins: a theoretical study. Can J Chem 1998;76:1042–1049.
  • Rauk A, Yu D, Armstrong DA. Oxidative damage to and by cysteine in proteins: An ab initio study of the radical structures, C-H, S-H, and C-C bond dissociation energies, and transition structures for H abstraction by thiyl radicals. J Am Chem Soc 1998;120:8848–8855.
  • Rauk A, Yu D, Armstrong DA. Toward site specificity of oxidative damage in proteins: C-H and C-C bond dissociation energies and reduction potentials of the radicals of alanine, serine, and threonine residues - An ab initio study. J Am Chem Soc 1997;119:208–217.
  • Reid DL, Armstrong DA, Rauk A, von Sonntag C. H-atom abstraction by thiyl radicals from peptides and cyclic dipeptides. A theoretical study of reaction rates. Phys Chem Chem Phys 2003;5:3994–3999.
  • Mozziconacci O, Williams TD, Kerwin BA, Schöneich C. Reversible intramolecular hydrogen transfer between protein cysteine thiyl radicals and alpha C-H bonds in insulin: control of selectivity by secondary structure. J Phys Chem B 2008;112:15921–15932.
  • Hogan MC. Phosphorescence quenching method for measurement of intracellular PO2 in isolated skeletal muscle fibers. J Appl Physiol (1985) 1999;86:720–724.
  • Richardson RS, Newcomer SC, Noyszewski EA. Skeletal muscle intracellular PO(2) assessed by myoglobin desaturation: response to graded exercise. J Appl Physiol (1985) 2001;91:2679–2685.
  • Carreau A, El Hafny-Rahbi B, Matejuk A, Grillon C, Kieda C. Why is the partial oxygen pressure of human tissues a crucial parameter? Small molecules and hypoxia. J Cell Mol Med 2011;15:1239–1253.
  • Strambini G, Cioni P. The effect of protein structure on oxygen quenching of phosphorescence. J Am Chem Soc 1999;121: 8337–8344.
  • Mozziconacci O, Schöneich C. Sequence-specific formation of D-amino acids in a monoclonal antibody during light exposure. Molecular pharmaceutics 2014;11:4291–4297.
  • Routaboul L, Vanthuyne N, Gastaldi S, Gil G, Bertrand M. Highly efficient photochemically induced thiyl radical- mediated racemization of aliphatic amines at 30 degrees C. J Org Chem 2008;73:364–368.
  • Chen Y, Chen C, Zhang L, Green-Church KB, Zweier JL. Superoxide generation from mitochondrial NADH dehydrogenase induces self-inactivation with specific protein radical formation. J Biol Chem 2005;280:37339–37348.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.