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Volumn 316-318, Issue , 2012, Pages 133-139

Gas-phase reactivity of sulfur-based radical ions of cysteine derivatives and small peptides

Author keywords

Cysteine radical anions; Cysteine radical cations; Ion molecule reactions; Radical rearrangement

Indexed keywords


EID: 84860537492     PISSN: 13873806     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijms.2011.12.001     Document Type: Article
Times cited : (26)

References (70)
  • 1
    • 0032558387 scopus 로고    scopus 로고
    • Superoxide produced in the heme pocket of the β-chain of hemoglobin reacts with the β-93 cysteine to produce a thiyl radical
    • DOI 10.1021/bi980941c
    • C. Balagopalakrishna, O. Abugo, J. Horsky, P. Manoharan, E. Nagababu, and J. Rifkind Superoxide produced in the heme pocket of the B-chain of hemoglobin reacts with the B-93 cysteine to produce a thiyl radical Biochemistry 37 1998 13194 13202 (Pubitemid 28449563)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13194-13202
    • Balagopalakrishna, C.1    Abugo, O.O.2    Horsky, J.3    Manoharan, P.T.4    Nagababu, E.5    Rifkind, J.M.6
  • 2
    • 0037131403 scopus 로고    scopus 로고
    • X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage
    • DOI 10.1074/jbc.M205821200
    • A. Becker, and W. Kabsch X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA: how the enzyme uses the Cys 418 thiyl radical for pyruvate cleavage J. Biol. Chem. 277 2002 40036 40042 (Pubitemid 35190993)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 40036-40042
    • Becker, A.1    Kabsch, W.2
  • 3
    • 0015501033 scopus 로고
    • Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase
    • A. Ehrenberg, and P. Reichard Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase J. Biol. Chem. 247 1972 3485 3488
    • (1972) J. Biol. Chem. , vol.247 , pp. 3485-3488
    • Ehrenberg, A.1    Reichard, P.2
  • 4
    • 79952607624 scopus 로고    scopus 로고
    • The stability of Cα peptide radicals: Why glycyl radical enzymes?
    • J. Hioe, G. Savasci, H. Brand, and H. Zipse The stability of Cα peptide radicals: why glycyl radical enzymes? Chem. Eur. J. 17 2011 3781 3789
    • (2011) Chem. Eur. J. , vol.17 , pp. 3781-3789
    • Hioe, J.1    Savasci, G.2    Brand, H.3    Zipse, H.4
  • 5
    • 79953053845 scopus 로고    scopus 로고
    • Structural basis for recutive radical formation and electron recycling in (R)-2-hydroxyisocaproyl-CoA dehydratase
    • S. Knauer, W. Buckel, and H. Dobbek Structural basis for recutive radical formation and electron recycling in (R)-2-hydroxyisocaproyl-CoA dehydratase J. Am. Chem. Soc. 133 2011 4342 4347
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4342-4347
    • Knauer, S.1    Buckel, W.2    Dobbek, H.3
  • 7
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • S. Licht, G. Gerfen, and J. Stubbe Thiyl radicals in ribonucleotide reductases Science 271 1996 477 481 (Pubitemid 26044465)
    • (1996) Science , vol.271 , Issue.5248 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 8
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • D. Logan, J. Andersson, B.-M. Sjoberg, and P. Nordlund A glycyl radical site in the crystal structure of a class III ribonucleotide reductase Science 283 1999 1499 1504
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.1    Andersson, J.2    Sjoberg, B.-M.3    Nordlund, P.4
  • 9
    • 49449089311 scopus 로고    scopus 로고
    • Peptide cysteine thiyl radicals abstract hydrogen atoms from surrounding amino acids: The photolysis of a cystine containing model peptide
    • O. Mozziconacci, V. Sharov, T. Williams, B. Kerwin, and C. Schoneich Peptide cysteine thiyl radicals abstract hydrogen atoms from surrounding amino acids: the photolysis of a cystine containing model peptide J. Phys. Chem. B 112 2008 9250 9257
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9250-9257
    • Mozziconacci, O.1    Sharov, V.2    Williams, T.3    Kerwin, B.4    Schoneich, C.5
  • 10
    • 57449084574 scopus 로고    scopus 로고
    • 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
    • T. Nauser, G. Casi, W. Koppenol, and C. Schoneich 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 112 2008 15034 15044
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15034-15044
    • Nauser, T.1    Casi, G.2    Koppenol, W.3    Schoneich, C.4
  • 11
    • 0033566661 scopus 로고    scopus 로고
    • 12-dependent enzyme provides new mechanistic insights
    • DOI 10.1016/S0969-2126(99)80116-6
    • R. Reitzer, K. Gruber, G. Jogl, U. Wagner, H. Bothe, W. Buckel, and C. Kratky Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights Structure 7 1999 891 902 (Pubitemid 29372511)
    • (1999) Structure , vol.7 , Issue.8 , pp. 891-902
    • Reitzer, R.1    Gruber, K.2    Jogl, G.3    Wagner, U.G.4    Bothe, H.5    Buckel, W.6    Kratky, C.7
  • 12
    • 0024473758 scopus 로고
    • 191 as the free-radical site in cytochrome c peroxidase compound ES
    • M. Sivaraja, D. Goodin, M. Smith, and B. Hoffman Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES Science 245 1989 738 740 (Pubitemid 19214005)
    • (1989) Science , vol.245 , Issue.4919 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 13
    • 0142062498 scopus 로고    scopus 로고
    • Radicals with a controlled lifestyle
    • J. Stubbe Radicals with a controlled lifestyle Chem. Commun. 2003 2511 2513 (Pubitemid 37296958)
    • (2003) Chemical Communications , Issue.20 , pp. 2511-2513
    • Stubbe, J.1
  • 14
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • J. Stubbe, and W.A. Van der Donk Protein radicals in enzyme catalysis Chem. Rev. 98 1998 705 762 (Pubitemid 128631440)
    • (1998) Chemical Reviews , vol.98 , Issue.2 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 15
    • 0030474520 scopus 로고    scopus 로고
    • Protein and peptide alkoxyl radicals can give rise to C-terminal decarboxylation and backbone cleavage
    • DOI 10.1006/abbi.1996.0545
    • M. Davies Protein and peptide alkoxyl radicals can give rise to C-terminal decarboxylation and backbone cleavage Arch. Biochem. Biophys. 336 1996 163 172 (Pubitemid 26423763)
    • (1996) Archives of Biochemistry and Biophysics , vol.336 , Issue.1 , pp. 163-172
    • Davies, M.J.1
  • 16
    • 78650750400 scopus 로고    scopus 로고
    • Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
    • M. Davies Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention J. Clin. Biochem. Nutr. 48 2011 8 19
    • (2011) J. Clin. Biochem. Nutr. , vol.48 , pp. 8-19
    • Davies, M.1
  • 18
    • 0033712060 scopus 로고    scopus 로고
    • β-Scission of C-3 β-carbon alkoxyl radicals on peptides and proteins: A novel pathway which results in the formation of a α-carbon radicals and the loss of amino acid side chains
    • H. Headlam, A. Mortimer, C. Easton, and M. Davies β-Scission of C-3 β-carbon alkoxyl radicals on peptides and proteins: a novel pathway which results in the formation of a α-carbon radicals and the loss of amino acid side chains Chem. Res. Toxicol. 13 2000 1087 1095
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 1087-1095
    • Headlam, H.1    Mortimer, A.2    Easton, C.3    Davies, M.4
  • 19
    • 0034600281 scopus 로고    scopus 로고
    • Influence of β-sheet structure on the susceptibility of proteins to backbone oxidative damage: Preference for (α)c-centered radical formation at glycine residues of antiparallel β-sheets
    • DOI 10.1021/ja9939688
    • A. Rauk, and D. Armstrong Influence of β-sheet on the susceptibility of proteins to backbone oxidative damage: preference for αC-centered radical formation at glycine residues of antiparallel β-sheets J. Am. Chem. Soc. 122 2000 4185 4192 (Pubitemid 30304853)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.17 , pp. 4185-4192
    • Rauk, A.1    Armstrong, D.A.2
  • 20
    • 0032475395 scopus 로고    scopus 로고
    • 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
    • DOI 10.1021/ja9807789
    • A. Rauk, D. Yu, and D. Armstrong Oxidative damage to and by cysteine proteins: an ab initio study of the radical structures, CH, SH, and CC bond dissociation energies, and transition structures for H abstraction by thiyl radicals J. Am. Chem. Soc. 120 1998 8848 8855 (Pubitemid 28442923)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.34 , pp. 8848-8855
    • Rauk, A.1    Yu, D.2    Armstrong, D.A.3
  • 21
    • 47049096866 scopus 로고    scopus 로고
    • Mechanisms of protein damage induced by cysteine thiyl radical formation
    • DOI 10.1021/tx800005u
    • C. Schoneich Mechanisms of protein damage induced by cysteine thiyl radical formation Chem. Res. Toxicol. 21 2008 1175 1179 (Pubitemid 351967380)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.6 , pp. 1175-1179
    • Schoneich, C.1
  • 22
    • 69149104334 scopus 로고    scopus 로고
    • Radical cations of amino acids and peptides: Structures and stabilities
    • A. Hopkinson Radical cations of amino acids and peptides: structures and stabilities Mass Spectrom. Rev. 28 2009 655 671
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 655-671
    • Hopkinson, A.1
  • 24
    • 0346114246 scopus 로고
    • Detection identification of short-lived free radicals by an electron spin resonance trapping technique
    • E.G. Janzen, B.J. Blackburn, and Detection Identification of short-lived free radicals by an electron spin resonance trapping technique J. Am. Chem. Soc. 90 1968 5909 5910
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 5909-5910
    • Janzen, E.G.1    Blackburn, B.J.2
  • 26
    • 46749131482 scopus 로고    scopus 로고
    • Dependence of product formation from decomposition of nitroso-dithiols on the degree of nitrosation. Evidence that dinitroso-dithiothreitol acts solely as an nitric oxide releasing compound
    • DOI 10.1039/b801583j
    • S. Liebskind, H.G. Korth, H. de Groot, and M. Kirsch Dependence of product formation from decomposition of nitroso-dithiols on the degree of nitrosation. Evidence that dinitroso-dithioreitol acts solely as an nitric oxide releasing compound Org. Biomol. Chem. 6 2008 2560 2573 (Pubitemid 351950586)
    • (2008) Organic and Biomolecular Chemistry , vol.6 , Issue.14 , pp. 2560-2573
    • Liebeskind, S.1    Korth, H.-G.2    De Groot, H.3    Kirsch, M.4
  • 28
    • 36348964192 scopus 로고    scopus 로고
    • Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport
    • DOI 10.1161/CIRCRESAHA.107.155879
    • J. Sun, M. Morgan, R.F. Shen, C. Steenbergen, and E. Murphy Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport Circ. Res. 101 2007 1155 1163 (Pubitemid 350146442)
    • (2007) Circulation Research , vol.101 , Issue.11 , pp. 1155-1163
    • Sun, J.1    Morgan, M.2    Shen, R.-F.3    Steenbergen, C.4    Murphy, E.5
  • 29
    • 1842785867 scopus 로고    scopus 로고
    • EPR spin trapping of protein radicals
    • DOI 10.1016/j.freeradbiomed.2003.12.013, PII S089158490300861X
    • M.J. Davies, and C.L. Hawkins EPR spin trapping of protein radicals Free Radic. Biol. Med. 36 2004 1072 1086 (Pubitemid 38479861)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.9 , pp. 1072-1086
    • Davies, M.J.1    Hawkins, C.L.2
  • 31
    • 80052316735 scopus 로고    scopus 로고
    • Assessments of thiyl radicals in biosystems: Difficulties and new applications
    • D.A. Stoyanovsky, A. Maeda, J.L. Atkins, and V.E. Kagan Assessments of thiyl radicals in biosystems: difficulties and new applications Anal. Chem. 2011
    • (2011) Anal. Chem.
    • Stoyanovsky, D.A.1    Maeda, A.2    Atkins, J.L.3    Kagan, V.E.4
  • 33
    • 78651414181 scopus 로고
    • Mass spectrometric studies on amino acid and peptide derivatives
    • C.O. Andersson Mass spectrometric studies on amino acid and peptide derivatives Acta Chem. Scand. 12 1958 1353
    • (1958) Acta Chem. Scand. , vol.12 , pp. 1353
    • Andersson, C.O.1
  • 35
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • R.A. Zubarev, N.L. Kelleher, and F.W. McLafferty Electron capture dissociation of multiply charged protein cations. A nonergodic process J. Am. Chem. Soc. 120 1998 3265 3266
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 38
    • 17844369494 scopus 로고    scopus 로고
    • Formation of cationic peptide radicals by gas-phase redox reactions with trivalent chromium, manganese, iron, and cobalt complexes
    • DOI 10.1021/ja043088f
    • C.K. Barlow, W.D. McFadyen, and R.A.J. O'Hair Formation of cationic peptide radicals by gas-phase redox reactions with trivalent chromium, manganese, iron, and cobalt complexes J. Am. Chem. Soc. 127 2005 6109 6115 (Pubitemid 40584827)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.16 , pp. 6109-6115
    • Barlow, C.K.1    McFadyen, D.W.D.2    O'Hair, R.A.J.3
  • 39
    • 24744432499 scopus 로고    scopus 로고
    • Bioconjugates for tunable peptide fragmentation: Free radical initiated peptide sequencing (FRIPS)
    • DOI 10.1021/ja052042z
    • R. Hodyss, H.A. Cox, and J.L. Beauchamp Bioconjugates for tunable peptide fragmentation: free radical initiated peptide sequencing (FRIPS) J. Am. Chem. Soc. 127 2005 12436 12437 (Pubitemid 41292131)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.36 , pp. 12436-12437
    • Hodyss, R.1    Cox, H.A.2    Beauchamp, J.L.3
  • 41
    • 33747094043 scopus 로고    scopus 로고
    • N-Terminal amino acid side-chain cleavage of chemically modified peptides in the gas phase: A mass spectrometry technique for N-terminus identification
    • DOI 10.1016/j.bmc.2006.05.060, PII S0968089606004342, Tetrahedron Prize for Creativity in Organic Chemistry 2005: B. Giese
    • A. Chacon, D.S. Masterson, H. Yin, D.C. Liebler, and N.A. Porter N-terminal amino acid side-chain cleavage of chemically modified peptides in the gas phase: a mass spectrometry technique for N-terminus identification Bioorg. Med. Chem. 14 2006 6213 6222 (Pubitemid 44224084)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.18 , pp. 6213-6222
    • Chacon, A.1    Masterson, D.S.2    Yin, H.3    Liebler, D.C.4    Porter, N.A.5
  • 43
    • 33751323198 scopus 로고    scopus 로고
    • Electrospray Tandem Mass Spectrometry Analysis of S- and N-Nitrosopeptides: Facile Loss of NO and Radical-Induced Fragmentation
    • DOI 10.1016/j.jasms.2006.07.026, PII S1044030506007112
    • G. Hao, and S.S. Gross Electrospray tandem mass spectrometry analysis of S- and N-nitrosopeptides: facile loss of NO and radical-induced fragmentation J. Am. Soc. Mass Spectrom. 17 2006 1725 1730 (Pubitemid 44809955)
    • (2006) Journal of the American Society for Mass Spectrometry , vol.17 , Issue.12 , pp. 1725-1730
    • Hao, G.1    Gross, S.S.2
  • 44
    • 65549138010 scopus 로고    scopus 로고
    • Gas-phase fragmentation of long-lived cysteine radical cations formed via NO loss from protonated S-nitrosocysteine
    • V. Ryzhov, A. Lam, and R.A.J. O'Hair Gas-phase fragmentation of long-lived cysteine radical cations formed via NO loss from protonated S-nitrosocysteine J. Am. Soc. Mass Spectrom. 20 2009 985 995
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 985-995
    • Ryzhov, V.1    Lam, A.2    O'Hair, R.A.J.3
  • 46
    • 78651425110 scopus 로고    scopus 로고
    • Mobile protons vs. mobile radicals: Gas-phase unimolecular chemistry of radical cations of cysteine-containing peptides
    • A. Lam, V. Ryzhov, and R.A.J. O'Hair Mobile protons vs. mobile radicals: gas-phase unimolecular chemistry of radical cations of cysteine-containing peptides J. Am. Soc. Mass Spectrom. 21 2010 1296 1312
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1296-1312
    • Lam, A.1    Ryzhov, V.2    O'Hair, R.A.J.3
  • 47
    • 80054007258 scopus 로고    scopus 로고
    • Glutathione radical cation in the gas phase; Generation, structure and fragmentation
    • 10.1039/C1OB05968H
    • J. Zhao, K.W.M. Siu, and A.C. Hopkinson Glutathione radical cation in the gas phase; generation, structure and fragmentation Org. Biomol. Chem. 2011 10.1039/C1OB05968H
    • (2011) Org. Biomol. Chem.
    • Zhao, J.1    Siu, K.W.M.2    Hopkinson, A.C.3
  • 48
    • 45749143632 scopus 로고    scopus 로고
    • Are the radical centers in peptide radical cations mobile? The generation, tautomerism, and dissociation of isomeric α-carbon-centered triglycine radical cations in the gas phase
    • DOI 10.1021/ja801108j
    • I.K. Chu, J. Zhao, M. Xu, S.O. Siu, A.C. Hopkinson, and K.W.M. Siu Are the radical centers in peptide radical cations mobile? The generation, tautomerism, and dissociation of isomeric α-carbon-centered triglycine radical cations in the gas phase J. Am. Chem. Soc. 130 2008 7862 7872 (Pubitemid 351875061)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.25 , pp. 7862-7872
    • Chu, I.K.1    Zhao, J.2    Xu, M.3    Shiu, O.S.4    Hopkinson, A.C.5    Siu, K.W.M.6
  • 49
    • 0032237966 scopus 로고    scopus 로고
    • Estimation of effective ion temperatures in a quadrupole ion trap
    • S. Gronert Estimation of effective ion temperatures in a quadrupole ion trap J. Am. Soc. Mass Spectrom. 9 1998 845 848
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 845-848
    • Gronert, S.1
  • 50
    • 72449129957 scopus 로고    scopus 로고
    • Gas-phase reactivity of protonated 2-, 3-, and 4-dehydropyridine radicals toward organic reagents
    • A. Adeuya, J.M. Price, B.J. Jankiewicz, J.J. Nash, and H.I. Kenttamaa Gas-phase reactivity of protonated 2-, 3-, and 4-dehydropyridine radicals toward organic reagents J. Phys. Chem. A 113 2009 13663 13674
    • (2009) J. Phys. Chem. A , vol.113 , pp. 13663-13674
    • Adeuya, A.1    Price, J.M.2    Jankiewicz, B.J.3    Nash, J.J.4    Kenttamaa, H.I.5
  • 52
    • 77956877676 scopus 로고    scopus 로고
    • Reactions of an aromatic σ,σ-biradical with amino acids and dipeptides in the gas phase
    • M. Fu, S. Li, E. Archibold, M. Yurkovich, J. Nash, and H. Kenttamaa Reactions of an aromatic σ,σ-biradical with amino acids and dipeptides in the gas phase J. Am. Soc. Mass Spectrom. 21 2010 1737 1752
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1737-1752
    • Fu, M.1    Li, S.2    Archibold, E.3    Yurkovich, M.4    Nash, J.5    Kenttamaa, H.6
  • 55
    • 84989036188 scopus 로고
    • Long lived distonic radical cations
    • H.I. Kenttamaa Long lived distonic radical cations Org. Mass Spectrom. 29 1994 1 10
    • (1994) Org. Mass Spectrom. , vol.29 , pp. 1-10
    • Kenttamaa, H.I.1
  • 56
    • 0001766175 scopus 로고
    • Ion-molecule reactions of distonic radical cations
    • K.M. Stirk, L.K.M. Kiminkinen, and H.I. Kenttamaa Ion-molecule reactions of distonic radical cations Chem. Rev. 92 1992 1649 1665
    • (1992) Chem. Rev. , vol.92 , pp. 1649-1665
    • Stirk, K.M.1    Kiminkinen, L.K.M.2    Kenttamaa, H.I.3
  • 57
    • 0035917356 scopus 로고    scopus 로고
    • Polarity of the transition state controls the reactivity of related charged phenyl radicals toward atom and group donors
    • DOI 10.1021/jo001634r
    • S. Tichey, K. Thoen, J. Price, J. Ferra, C. Petucci, and H. Kenttamaa Polarity of the transition state controls the reactivity of related charged phenyl radicals toward atom and group donors J. Org. Chem. 66 2001 2726 2733 (Pubitemid 32867692)
    • (2001) Journal of Organic Chemistry , vol.66 , Issue.8 , pp. 2726-2733
    • Tichy, S.E.1    Thoen, K.K.2    Price, J.M.3    Ferra Jr., J.J.4    Petucci, C.J.5    Kenttamaa, H.I.6
  • 58
    • 80755142776 scopus 로고    scopus 로고
    • Structure reactivity of the N-acetyl-cysteine radical cation and anion: Does radical migration occur?
    • S. Osburn, G. Berden, J. Oomens, R.A.J. O'Hair, V. Ryzhov, and Structure Reactivity of the N-acetyl-cysteine radical cation and anion: does radical migration occur? J. Am. Soc. Mass Spectrom. 22 2011 1794 1803
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1794-1803
    • Osburn, S.1    Berden, G.2    Oomens, J.3    O'Hair, R.A.J.4    Ryzhov, V.5
  • 60
    • 42649132483 scopus 로고    scopus 로고
    • Coupling of ion-molecule reactions with liquid chromatography on a quadrupole ion trap mass spectrometer
    • DOI 10.1002/rcm.3494
    • Y. Pyatkivskyy, and V. Ryzhov Coupling of ion-molecule reactions to liquid chromatography on a quadrupole ion trap mass spectrometer Rapid Commun. Mass Spectrom. 22 2008 1288 1294 (Pubitemid 351600779)
    • (2008) Rapid Communications in Mass Spectrometry , vol.22 , Issue.8 , pp. 1288-1294
    • Pyatkivskyy, Y.1    Ryzhov, V.2
  • 61
    • 45849121003 scopus 로고    scopus 로고
    • Intercluster chemistry of protonated and sodiated betaine dimers upon collision induced dissociation and electron induced dissociation
    • L. Feketova, G.N. Khairallah, and R.A.J. O'Hair Intercluster chemistry of protonated and sodiated betaine dimers upon collision induced dissociation and electron induced dissociation Eur. J. Mass Spectrom. 14 2008 107 110
    • (2008) Eur. J. Mass Spectrom. , vol.14 , pp. 107-110
    • Feketova, L.1    Khairallah, G.N.2    O'Hair, R.A.J.3
  • 64
    • 0022481682 scopus 로고
    • Cyclic guanosine monophosphate as a mediator of vasodilation
    • F. Murad Cyclic guanosine monophosphate as a mediator of vasodilation J. Clin. Invest. 78 1986 1 5 (Pubitemid 16068173)
    • (1986) Journal of Clinical Investigation , vol.78 , Issue.1 , pp. 1-5
    • Murad, F.1
  • 67
    • 0001712481 scopus 로고    scopus 로고
    • Significance of the intramolecular transformation of glutathione thiyl radicals to α-aminoalkyl radicals. Thermochemical and biological implications
    • R. Zhao, J. Lind, G. Merenyi, and T.E. Ericksen Significance of the intramolecular transformation of glutathione thiyl radicals to α-aminoalkyl radicals. Thermochemical and biological implications J. Chem. Soc. Perkin Trans. 2 2 1997 569 574 (Pubitemid 127441861)
    • (1997) Journal of the Chemical Society. Perkin Transactions 2 , Issue.3 , pp. 569-574
    • Zhao, R.1    Lind, J.2    Merenyi, G.3    Eriksen, T.E.4
  • 68
    • 79955421688 scopus 로고    scopus 로고
    • Gas-phase ion-molecule reactions using regioselectively generated radical cations to model oxidative damage and probe radical sites in peptides
    • C.K. Barlow, A. Wright, C.J. Easton, and R.A.J. O'Hair Gas-phase ion-molecule reactions using regioselectively generated radical cations to model oxidative damage and probe radical sites in peptides Org. Biomol. Chem. 9 2011 3733 3745
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 3733-3745
    • Barlow, C.K.1    Wright, A.2    Easton, C.J.3    O'Hair, R.A.J.4
  • 69
    • 77249116312 scopus 로고    scopus 로고
    • Direct observation of the gas phase reaction of the cyclohexyl radical with dioxygen using a distonic radical ion approach
    • B. Kirk, D. Harman, and S. Blanksby Direct observation of the gas phase reaction of the cyclohexyl radical with dioxygen using a distonic radical ion approach J. Phys. Chem. A 114 2010 1446 1456
    • (2010) J. Phys. Chem. A , vol.114 , pp. 1446-1456
    • Kirk, B.1    Harman, D.2    Blanksby, S.3


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