A computational study on the possible role of oxygen in the oxidation of methionine and dimethylsulfide initiated by OH radicals

Computational and Theoretical Chemistry

Volumn 1009, Issue , 2013, Pages 24-29

  Xipsiti, Chara ^a   Nicolaides, Athanassios V ^a  

^a UNIVERSITY OF CYPRUS   (Cyprus)

Author keywords

CCSD(T); Dimethyl sulfide oxidation; G3(MP2) B3LYP; Mechanism; Methionine oxidation; Thermochemistry

Indexed keywords

EID: 84873157628     PISSN: 2210271X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.comptc.2012.12.020     Document Type: Article

References (61)

1. Levine R.L., Mosoni L., Berlett B.S., Stadtman E.R. Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. USA 1996, 93:15036-15040.
2. Stadtman E.R., Moskovitz J., Berlett B.S., Levine R.L. Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol. Cell. Biochem. 2002, 234(235):3-9.
3. Schöneich C. Redox processes of methionine relevant to β-amyloid oxidation and Alzheimer's disease. Arch. Biochem. Biophys. 2002, 397:370-376.
4. Butterfield D.A., Kanski J. Methionine residue 35 is critical for the oxidative stress and neurotoxicproperties of Alzheimer's amyloid β-peptide 1-42. Peptides 2002, 23:1299-1309.
5. Butterfield D.A., Bush A.I. Alzheimer's amyloid β-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol. Aging 2004, 25:563-568.
6. Butterfield D.A., Kimball B. The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity. Biochim. Biophys Acta. 2005, 1703:149-156.
7. Butterfield D.A., Galvan V., Lange M.B., Tang H., Sowell R.A., Spilman P., Fombonne J., Gorostiza O., Zhang J., Sultana R., Bredesen D.E. In vivo oxidative stress in brain of Alzheimer disease transgenic mice. requirement for methionine 35 in amyloid β-peptide of APP. Free Radical Biol. Med. 2010, 48:136-144.
8. Maiti P., Lomakin A., Benedek G.B., Bitan G. Despite its role in assembly methionine 35 is not necessary for amyloid β-protein toxicity. J. Neurochem. 2010, 113:1252-1262.
9. Moskovitz J., Maiti P., Lopes D.H.J., Oien D.B., Attar A., Liu T., Mittal S., Hayes J., Bitan G. Induction of methionine-sulfoxide reductases protects neurons from amyloid β-protein insults in vitro and in vivo. Biochemistry 2011, 50:10687-10697.
10. Schöneich C. Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease. Biochim. Biophys. Act. 2005, 1703:111-119.
11. Ciccotosto G.D., Barnham K.J., Cherny R.A., Masters C.L., Bush A.I., Curtain C.C., Cappai R., Tew D. Methionine oxidation: implications for the mechanism of toxicity of the β-amyloid peptide from Alzheimer's disease. Lett. Pept. Sci. 2003, 10:413-417.
12. Hou L., Kang I., Marchant R.E., Zagorski M.G. Methionine 35 oxidation reduces fibril assembly of the amyloid Aβ-(1-42) peptide of Alzheimer's disease. J. Biol. Chem. 2002, 277:40173-40176.
13. 35 in neurotoxic β-amyloid peptide. A molecular modeling study. Chem. Res. Toxicol. 2002, 15:408-418.
14. Schöneich C., Pogocki D., Hug G.L., Bobrowski K. Free radical reactions of methionine in peptides: mechanisms relevant to β-amyloid oxidation and Alzheimer's disease. J. Am. Chem. Soc. 2003, 125:13700-13713.
15. Barnham K.J., Ciccotosto G.D., Tickler A.K., Ali F.E., Smith D.G., Williamson N.A., Lam Y.H., Carrington D., Tew D., Kocak G., Volitakis I., Separovic F., Barrow C.J., Wade J.D., Masters C.L., Cherny R.A., Curtain C.C., Bush A.I., Cappai R. Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 2003, 278:42959-42965.
16. Glaser C.B., Yamin G., Uversky V.N., Fink A.L. Methionine oxidation, α-synuclein and Parkinson's disease. Biochim. Biophys. Acta. 2005, 1703:157-169.
17. Butterfield D.A., Drake J., Pocernich C., Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide. Trends Mol. Med. 2001, 7:548-554.
18. Varadarajan S., Kanski J., Aksenova M., Lauderback C., Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for alzheimer¢s Aβ(1-42) and Aβ(25-35). J. Am. Chem. Soc. 2001, 123:5625-5631.
19. Hensley K., Carney J.M., Mattson M.P., Aksenova M., Harrus M., Wu J.F., Floyd R.A., Butterfield D.A. A model for 3-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc. Nati. Acad. Sci. USA 1994, 91:3270-3274.
20. Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. Review: Alzheimer's Amyloid β-peptide-associated free radical oxidative stress and neurotoxicity. J. Struct. Biol. 2000, 130:184-208.
21. Lauderback C.M., Kanski J., Hackett J.M., Maeda N., Kindy M.S., Butterfield D.A. Apolipoprotein E modulates Alzheimer's Aβ(1-42)-induced oxidative damage to synaptosomes in an allele-specific manner. Brain Res. 2002, 924:90-97.
22. Hayes C.S., Aguiar B.I., Martinez L.C., Setlow P. In vitro and in vivo oxidation of methionine residues in small, acid-soluble spore proteins from bacillus species. J. Bacteriol. 1998, 180:2694-2700.
23. Uversky V.N., Yamina G., Souillac P.O., Goers J., Glaserd C.B., Finka A.L. Methionine oxidation inhibits firillation of human α-synuclein in vitro. FEBS Lett. 2002, 517:239-244.
24. Voct W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Fr. Rad. Biol. Med. 1995, 18:93-105.
25. Kantorow M., Hawse J.R., Cowell T.L., Benhamed S., Pizarro G.O., Reddy V.N., Hejtmancik J.F. Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. Proc. Natl. Acad. Sci. USA 2004, 101:9654.
26. Marino T., Soriano-Correa C., Russo N. Oxidation mechanism of methionine by ho center dot radical: a theoretical study. J. Phys. Chem. B 2012, 116:5349-5354.
27. Barata-Vallejo S., Ferreri C., Postigo A., Chatgilialoglu C. Radiation chemical studies of methionine in aqueous solution: understanding the role of molecular oxygen. Chem. Res. Toxicol. 2010, 23:258-263.
28. OH-induced oxidation of enkephalins. J. Phys. Chem. B 2012, 116:12460-12472.
29. Schöneich C., Zhao F., Madden K.P., Bobrowski K. Side chain fragmentation of N-terminal threonine or serine residue induced through intramolecular proton transfer to hydroxy sulfuranyl radical formed at neighboring methionine in dipeptides. J. Am. Chem. Soc. 1994, 116:4641-4652.
30. Schöneich C., Pogocki D., Wisniowski P., Hug G.L., Bobrowski K. Intramolecular sulfuroxygen bond formation in radical cations of N-acetylmethionine amide. J. Am. Chem. Soc. 2000, 122:10224-10225.
31. Brunelle P., Schöneich C., Rauk A. One-electron oxidation of methionine peptides - stability of the three-electron SN(amide) bond. Can. J. Chem. 2006, 84:893-904.
32. Ji W.F., Li Z.L., Shen L., Kong D.X., Zhang H.Y. Density functional theory methods as powerful tools to elucidate amino acid oxidation mechanisms. A case study on methionine model peptide. J. Phys. Chem. B 2007, 111:485-489.
33. Bobrowski K., Hug G.L., Pogocki D., Marciniak B., Schöneich C. Sulfur radical cationpeptide bond complex in the one-electron oxidation of S-Methylglutathione. J. Am. Chem. Soc. 2007, 129:9236-9245.
34. Bobrowski K., Hug G.L., Pogocki D., Marciniak B., Schöneich C. Stabilization of sulfide radical cations through complexation with the peptide bond: mechanisms relevant to oxidation of proteins containing multiple methionine residues. J. Phys. Chem. B. 2007, 111:9608-9620.
35. Fourré I., Bergès J., Houée-Levin C. Structural and topological studies of methionine radical cations in dipeptides: electron sharing in two-center three-electron bonds. J. Phys. Chem. A 2010, 114:7359-7368.
36. Huang M.L., Rauk A. Reactions of one-electron-oxidized methionine with oxygen: an ab initio study. J. Phys. Chem. A. 2004, 108:6222-6230.
37. Rauk A., Armstrong D.A., Fairlie D.P. Is oxidative damage by β-Amyloid and prion peptides mediated by hydrogen atom transfer from glycine α-Carbon to methionine sulfur within β-sheets?. J. Am. Chem. Soc. 2000, 122:9761-9767.
38. Gu M., Turecek F. The elusive dimethylhydroxysulfuranyl radical. An intermediate or a transition state?. J. Am. Chem. Soc. 1992, 114:7146-7151.
39. Michael L. Computational study of addition and abstraction reactions between OH radical and dimethyl sulfide. A difficult case. J. Phys. Chem. 1993, 97:10971-10976.
40. Tureček F. The dimethyl sulfide-hydroxyl radical reaction. An ab initio study. J. Phys. Chem. 1994, 98:3701-3706.
41. 2 by ab initio and density functional theory. J. Mol. Struc. 2001, 543:167-175.
42. Williams M.B., Campuzano-Jost P., Cossairt B.M., Hynes A.J. Experimental and theoretical studies of the reaction of the oh radical with alkyl sulfides: 1. Direct observations of the formation of the OH-DMS adduct-pressure dependence of the forward rate of addition and development of a predictive expression at low temperature. J. Phys. Chem. A 2007, 111:89-104.
43. 2 reaction. J. Phys. Chem. 1996, 100:14694-14702.
44. Turnipseed A.A., Barone S.B., Ravishankara A.R. Reaction of OH with dimethyl sulfide. 2. Products and mechanisms. J. Phys. Chem. 1996, 100:14703-14713.
45. OH scavenging reaction by OH. Its relevance in DMSO formation. Comp. Theor. Chem. 2011, 965:249-258.
46. Frisch M.J., Trucks G.W., Schlegel H.B., Scuseria G.E., Robb M.A., Cheeseman J.R., Montgomery J.A., Vreven T., Kudin K.N., Burant J.C., Millam J.M., Iyengar S.S., Tomasi J., Barone V., Mennucci B., Cossi M., Scalmani G., Rega N., Petersson G.A., Nakatsuji H., Hada M., Ehara M., Toyota K., Fukuda R., Hasegawa J., Ishida M., Nakajima T., Honda Y., Kitao O., Nakai H., Klene M., Li X., Knox J.E., Hratchian H.P., Cross J.B., Adamo C., Jaramillo J., Gomperts R., Stratmann R.E., Yazyev O., Austin A.J., Cammi R., Pomelli C., Ochterski J.W., Ayala P.Y., Morokuma K., Voth G.A., Salvador P., Dannenberg J.J., Zakrzewski V.G., Dapprich S., Daniels A.D., Strain M.C., Farkas O., Malick D.K., Rabuck A.D., Raghavachari K., Foresman J.B., Ortiz J.V., Cui Q., Baboul A.G., Clifford S., Cioslowski J., Stefanov B.B., Liu G., Liashenko A., Piskorz P., Komaromi I., Martin R.L., Fox D.J., Keith T., Al-Laham M.A., Peng C.Y., Nanayakkara A., Challacombe M., Gill M.W., Johnson B., Chen W., Wong M.W., Gonzalez C., Pople J.A. Gaussian03, Revision C.2 2005, Gaussian, Inc., Wallingford, CT.
47. Frisch M.J., Trucks G.W., Schlegel H.B., Scuseria G.E., Robb M.A., Cheeseman J.R., Montgomery J.A., Vreven T., Kudin K.N., Burant J.C., Millam J.M., Iyengar S.S., Tomasi J., Barone V., Mennucci B., Cossi M., Scalmani G., Rega N., Petersson G.A., Nakatsuji H., Hada M., Ehara M., Toyota K., Fukuda R., Hasegawa J., Ishida M., Nakajima T., Honda Y., Kitao O., Nakai H., Klene M., Li X., Knox J.E., Hratchian H.P., Cross J.B., Adamo C., Jaramillo J., Gomperts R., Stratmann R.E., Yazyev O., Austin A.J., Cammi R., Pomelli C., Ochterski J.W., Ayala P.Y., Morokuma K., Voth G.A., Salvador P., Dannenberg J.J., Zakrzewski V.G., Dapprich S., Daniels A.D., Strain M.C., Farkas O., Malick D.K., Rabuck A.D., Raghavachari K., Foresman J.B., Ortiz J.V., Cui Q., Baboul A.G., Clifford S., Cioslowski J., Stefanov B.B., Liu G., Liashenko A., Piskorz P., Komaromi I., Martin R.L., Fox D.J., Keith T., Al-Laham M.A., Peng C.Y., Nanayakkara A., Challacombe M., Gill P.M.W., Johnson B., Chen W., Wong M.W., Gonzalez C., Pople J.A. Gaussian09, Revision A 02 2009, Gaussian Inc., Pittsburgh, PA.
48. Baboul A.G., Curtiss L.A., Redfern P.C., Raghavachari K. Gaussian-3 theory using density functional geometries and zero-point energies. J. Chem. Phys. 1999, 110:7650-7657.
49. Nicolaides A., Rauk A., Glukhovtsev M., Radom L. J. Phys. Chem. 1996, 100:17460-17464.
50. Nicolaides A., Radom L. An evaluation of the performance of G2, G2(MP2) and G2(MP2,SVP) theories for heats of formation and heats of reaction in the case of 'large' hydrocarbons. Mol. Phys. 1996, 88:759-765.
51. Mennucci B., Tomasi J. Continuum solvation models: a new approach to the problem of solute's charge distribution and cavity boundaries. J. Chem. Phys. 1997, 106:5151-5158.
52. Fourré I., Bergè J. Structural and topological characterization of the three-electron bond: The SO radicals. J. Phys. Chem. 2004, 108:898-906.
53. Tran N.L., Colvin M.E. The prediction of biochemical acid dissociation constants using first principles quantum chemical simulation. J. Mol. Struct. (Theochem.) 2000, 532:127-137.
54. Hammerum S. Distonic radical cations in gaseous and condensed phase. Mass Spectrom. Rev. 1988, 7:123-202.
55. 2SO dimethylsulfoxide by combustion calorimetry. J. Chem. Thermodyn. 1994, 26:971-975.
56. 4] reaction. J. Phys. Chem. 1990, 94:4396-4398.
57. Espinosa-García J. New theoretical value of the enthalpy of formation of the OOH radical. Mol. Phys. 1993, 79:445-447.
58. Tureček F., Brabec L., Vondrák T., HanuŠ V., Hájíček J., Havlas Z. Sulfenic acids in the gas phase. Preparation, ionization energies and heats of formation of methane-, ethene-, and benzenesulfenic acid. Collect. Czech. Chem. Commun. 1988, 53:2140-2158.
59. Cubbage J.W., Guo Y., McCulla R.D., Jenks W.S. Thermolysis of alkyl sulfoxides and derivatives: a comparison of experiment and theory. J. Org. Chem. 2001, 66:8722-8736.
60. y (y=2,3). J. Mol. Struct.: Theochem. 2002, 581:129-138.
61. P.J. Linstrom and W.G. Mallard, Eds., NIST Chemistry WebBook, NIST Standard Reference database Number 69, June 2005, National Institute of Standards and Technology, Gaithersburg MD, 20899 (<>). http://webbook.nist.gov.