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Volumn 80, Issue , 2015, Pages 158-163

Protein thiyl radical reactions and product formation: A kinetic simulation

Author keywords

Carbon centered radicals; D Amino acids; Free radicals; Glutathione; Hydrogen atom transfer; Thiyl radicals

Indexed keywords

ASCORBIC ACID; GLUTATHIONE; OXYGEN; PROTEIN THIYL RADICAL; RADICAL; UNCLASSIFIED DRUG; AMINO ACID; DISULFIDE; FREE RADICAL; HYDROGEN; PROTEIN; THIOL DERIVATIVE;

EID: 84923920135     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.12.006     Document Type: Review
Times cited : (45)

References (63)
  • 1
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45 2008 549 561
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 2
    • 84924119180 scopus 로고    scopus 로고
    • Are free radicals involved in thiol-based redox signaling?
    • Sep 30. [Epub ahead of print]
    • C.C. Winterbourn Are free radicals involved in thiol-based redox signaling? Free Radic. Biol. Med. 2014 Sep 30. pii: S0891-5849(14)00408-0. http://dx.doi.org/10.1016/j.freeradbiomed.2014.08.017. [Epub ahead of print]
    • (2014) Free Radic. Biol. Med.
    • Winterbourn, C.C.1
  • 3
    • 84899636261 scopus 로고    scopus 로고
    • Reversible cysteine oxidation in hydrogen peroxide sensing and signal transduction
    • S. Garcia-Santamarina, S. Boronat, and E. Hidalgo Reversible cysteine oxidation in hydrogen peroxide sensing and signal transduction Biochemistry 53 2014 2560 2580
    • (2014) Biochemistry , vol.53 , pp. 2560-2580
    • Garcia-Santamarina, S.1    Boronat, S.2    Hidalgo, E.3
  • 4
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • D.P. Jones Radical-free biology of oxidative stress, Am. J Physiol. Cell Physiol. 295 2008 C849 C868
    • (2008) Am. J Physiol. Cell Physiol. , vol.295 , pp. C849-C868
    • Jones, D.P.1
  • 5
    • 47049096866 scopus 로고    scopus 로고
    • Mechanisms of protein damage induced by cysteine thiyl radical formation
    • C. Schöneich Mechanisms of protein damage induced by cysteine thiyl radical formation Chem. Res. Toxicol. 21 2008 1175 1179
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1175-1179
    • Schöneich, C.1
  • 7
    • 0029939154 scopus 로고    scopus 로고
    • Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite: ESR-spin trapping and oxygen uptake studies
    • H. Karoui, N. Hogg, C. Frejaville, P. Tordo, and B. Kalyanaraman 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. 271 1996 6000 6009
    • (1996) J. Biol. Chem. , vol.271 , pp. 6000-6009
    • Karoui, H.1    Hogg, N.2    Frejaville, C.3    Tordo, P.4    Kalyanaraman, B.5
  • 8
    • 0025099316 scopus 로고
    • 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
    • M.D. Sevilla, D. Becker, and M. Yan 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. 57 1990 65 81
    • (1990) Int. J. Radiat. Biol. , vol.57 , pp. 65-81
    • Sevilla, M.D.1    Becker, D.2    Yan, M.3
  • 9
    • 33751158782 scopus 로고
    • Pulse radiolysis of 2-mercaptoethanol in oxygenated aqueous solution: Generation and reactions of the thiylperoxyl radical
    • X. Zhang, N. Zhang, H.-P. Schuchmann, and C. von Sonntag Pulse radiolysis of 2-mercaptoethanol in oxygenated aqueous solution: generation and reactions of the thiylperoxyl radical J. Phys. Chem. 98 1994 6541 6547
    • (1994) J. Phys. Chem. , vol.98 , pp. 6541-6547
    • Zhang, X.1    Zhang, N.2    Schuchmann, H.-P.3    Von Sonntag, C.4
  • 10
    • 0012217954 scopus 로고
    • Adduct formation and absolute rate constants in the displacement reaction of thiyl radicals with disulfides
    • M. Bonifacic, and K.D. Asmus Adduct formation and absolute rate constants in the displacement reaction of thiyl radicals with disulfides J. Phys. Chem. 88 1984 6286 6290
    • (1984) J. Phys. Chem. , vol.88 , pp. 6286-6290
    • Bonifacic, M.1    Asmus, K.D.2
  • 11
    • 0038182543 scopus 로고    scopus 로고
    • Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide: Evidence for a free radical mechanism
    • D. Jourd'heuil, F.L. Jourd'heuil, and M. Feelisch Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide: evidence for a free radical mechanism J. Biol. Chem. 278 2003 15720 15726
    • (2003) J. Biol. Chem. , vol.278 , pp. 15720-15726
    • Jourd'heuil, D.1    Jourd'heuil, F.L.2    Feelisch, M.3
  • 12
    • 63849086054 scopus 로고    scopus 로고
    • Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide
    • C.A. Bosworth, J.C. Toledo Jr., J.W. Zmijewski, Q. Li, and J.R. Lancaster Jr. Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide Proc. Natl. Acad. Sci. USA 106 2009 4671 4676
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4671-4676
    • Bosworth, C.A.1    Toledo, J.C.2    Zmijewski, J.W.3    Li, Q.4    Lancaster, J.R.5
  • 14
    • 79959956903 scopus 로고    scopus 로고
    • Regulation of Ras proteins by reactive nitrogen species
    • M.F. Davis, D. Vigil, and S.L. Campbell Regulation of Ras proteins by reactive nitrogen species Free Radic. Biol. Med. 51 2011 565 575
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 565-575
    • Davis, M.F.1    Vigil, D.2    Campbell, S.L.3
  • 17
    • 34250778409 scopus 로고    scopus 로고
    • Nitric oxide cell signaling: S-nitrosation of Ras superfamily GTPases
    • K.W. Raines, M.G. Bonini, and S.L. Campbell Nitric oxide cell signaling: S-nitrosation of Ras superfamily GTPases Cardiovasc. Res. 75 2007 229 239
    • (2007) Cardiovasc. Res. , vol.75 , pp. 229-239
    • Raines, K.W.1    Bonini, M.G.2    Campbell, S.L.3
  • 18
    • 0025259891 scopus 로고
    • In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides
    • K.R. Maples, C.H. Kennedy, S.J. Jordan, and R.P. Mason In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides Arch. Biochem. Biophys. 277 1990 402 409
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 402-409
    • Maples, K.R.1    Kennedy, C.H.2    Jordan, S.J.3    Mason, R.P.4
  • 20
    • 0030857377 scopus 로고    scopus 로고
    • Iron homeostasis, oxidative stress, and DNA damage
    • R. Meneghini Iron homeostasis, oxidative stress, and DNA damage Free Radic. Biol. Med. 23 1997 783 792
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 783-792
    • Meneghini, R.1
  • 22
    • 84864288909 scopus 로고    scopus 로고
    • Molecular basis of intramolecular electron transfer in proteins during radical-mediated oxidations: Computer simulation studies in model tyrosine-cysteine peptides in solution
    • A.A. Petruk, S. Bartesaghi, M. Trujillo, D.A. Estrin, D. Murgida, B. Kalyanaraman, M.A. Marti, and R. Radi 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. 525 2012 82 91
    • (2012) Arch. Biochem. Biophys. , vol.525 , pp. 82-91
    • Petruk, A.A.1    Bartesaghi, S.2    Trujillo, M.3    Estrin, D.A.4    Murgida, D.5    Kalyanaraman, B.6    Marti, M.A.7    Radi, R.8
  • 23
    • 0030814598 scopus 로고    scopus 로고
    • Direct ESR detection or peroxynitrite-induced tyrosine-centred protein radicals in human blood plasma
    • D. Pietraforte, and M. Minetti Direct ESR detection or peroxynitrite-induced tyrosine-centred protein radicals in human blood plasma Biochem. J. 325 1997 675 684
    • (1997) Biochem. J. , vol.325 , pp. 675-684
    • Pietraforte, D.1    Minetti, M.2
  • 24
    • 0031770008 scopus 로고    scopus 로고
    • On the influence of secondary structure on the alpha-C-H bond dissociation energy of proline residues in proteins: A theoretical study
    • D.A. Block, D. Yu, D.A. Armstrong, and A. Rauk 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. 76 1998 1042 1049
    • (1998) Can. J. Chem. , vol.76 , pp. 1042-1049
    • Block, D.A.1    Yu, D.2    Armstrong, D.A.3    Rauk, A.4
  • 25
    • 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
    • A. Rauk, D. Yu, and D.A. Armstrong 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. 120 1998 8848 8855
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8848-8855
    • Rauk, A.1    Yu, D.2    Armstrong, D.A.3
  • 26
    • 0031042252 scopus 로고    scopus 로고
    • 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
    • A. Rauk, D. Yu, and D.A. Armstrong 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. 119 1997 208 217
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 208-217
    • Rauk, A.1    Yu, D.2    Armstrong, D.A.3
  • 27
    • 0141680315 scopus 로고    scopus 로고
    • H-atom abstraction by thiyl radicals from peptides and cyclic dipeptides: A theoretical study of reaction rates
    • D.L. Reid, D.A. Armstrong, A. Rauk, and C. von Sonntag H-atom abstraction by thiyl radicals from peptides and cyclic dipeptides: a theoretical study of reaction rates Phys. Chem. Chem. Phys. 5 2003 3994 3999
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 3994-3999
    • Reid, D.L.1    Armstrong, D.A.2    Rauk, A.3    Von Sonntag, C.4
  • 28
    • 0037467060 scopus 로고    scopus 로고
    • Thiyl radicals abstract hydrogen atoms from the (alpha)C-H bonds in model peptides: Absolute rate constants and effect of amino acid structure
    • T. Nauser, and C. Schöneich 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. 125 2003 2042 2043
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2042-2043
    • Nauser, T.1    Schöneich, C.2
  • 29
    • 6344249017 scopus 로고    scopus 로고
    • Thiyl radical reaction with amino acid side chains: Rate constants for hydrogen transfer and relevance for posttranslational protein modification
    • T. Nauser, J. Pelling, and C. Schöneich Thiyl radical reaction with amino acid side chains: rate constants for hydrogen transfer and relevance for posttranslational protein modification Chem. Res. Toxicol. 17 2004 1323 1328
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1323-1328
    • Nauser, T.1    Pelling, J.2    Schöneich, C.3
  • 30
    • 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.H. Koppenol, and C. Schöneich 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.H.3    Schöneich, C.4
  • 31
    • 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.D. Williams, B.A. Kerwin, and C. Schöneich 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.D.3    Kerwin, B.A.4    Schöneich, C.5
  • 32
    • 77952505171 scopus 로고    scopus 로고
    • 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
    • O. Mozziconacci, B.A. Kerwin, and C. Schöneich 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 114 2010 6751 6762
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6751-6762
    • Mozziconacci, O.1    Kerwin, B.A.2    Schöneich, C.3
  • 33
    • 77958092906 scopus 로고    scopus 로고
    • Hydrogen exchange equilibria in glutathione radicals: Rate constants
    • D. Hofstetter, T. Nauser, and W.H. Koppenol Hydrogen exchange equilibria in glutathione radicals: rate constants Chem. Res. Toxicol. 23 2010 1596 1600
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1596-1600
    • Hofstetter, D.1    Nauser, T.2    Koppenol, W.H.3
  • 34
    • 84866433551 scopus 로고    scopus 로고
    • Intramolecular hydrogen transfer reactions of thiyl radicals from glutathione: Formation of carbon-centered radical at Glu, Cys, and Gly
    • O. Mozziconacci, T.D. Williams, and C. Schöneich Intramolecular hydrogen transfer reactions of thiyl radicals from glutathione: formation of carbon-centered radical at Glu, Cys, and Gly Chem. Res. Toxicol. 25 2012 1842 1861
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 1842-1861
    • Mozziconacci, O.1    Williams, T.D.2    Schöneich, C.3
  • 36
    • 0026761957 scopus 로고
    • Intramolecular transformation reaction of the glutathione thiyl radical into a non-sulphur-centred radical: A pulse-radiolysis and EPR study
    • L. Grierson, K. Hildenbrand, and E. Bothe Intramolecular transformation reaction of the glutathione thiyl radical into a non-sulphur-centred radical: a pulse-radiolysis and EPR study Int. J. Radiat. Biol. 62 1992 265 277
    • (1992) Int. J. Radiat. Biol. , vol.62 , pp. 265-277
    • Grierson, L.1    Hildenbrand, K.2    Bothe, E.3
  • 37
    • 0001712481 scopus 로고    scopus 로고
    • Significance of the intramolecular transformation of glutathione thiyl radicals to alpha-aminoalkyl radicals: Thermochemical and biological implications
    • R. Zhao, J. Lind, G. Merenyi, and T.E. Eriksen Significance of the intramolecular transformation of glutathione thiyl radicals to alpha-aminoalkyl radicals: thermochemical and biological implications J. Chem. Soc. Perkins Trans. 2 1997 569 574
    • (1997) J. Chem. Soc. Perkins Trans. , vol.2 , pp. 569-574
    • Zhao, R.1    Lind, J.2    Merenyi, G.3    Eriksen, T.E.4
  • 38
    • 0001434308 scopus 로고
    • Kinetics of one-electron oxidation of thiols and hydrogen abstraction by thiyl radicals from alpha-amino C-H bonds
    • R. Zhao, J. Lind, G. Merenyi, and T.E. Eriksen Kinetics of one-electron oxidation of thiols and hydrogen abstraction by thiyl radicals from alpha-amino C-H bonds J. Am. Chem. Soc. 116 1994 12010 12015
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 12010-12015
    • Zhao, R.1    Lind, J.2    Merenyi, G.3    Eriksen, T.E.4
  • 39
    • 84861076397 scopus 로고    scopus 로고
    • Reversible hydrogen transfer reactions in thiyl radicals from cysteine and related molecules: Absolute kinetics and equilibrium constants determined by pulse radiolysis
    • T. Nauser, W.H. Koppenol, and C. Schöneich 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 116 2012 5329 5341
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5329-5341
    • Nauser, T.1    Koppenol, W.H.2    Schöneich, C.3
  • 40
    • 0000302143 scopus 로고
    • Reaction-mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • W.M. Garrison Reaction-mechanisms in the radiolysis of peptides, polypeptides, and proteins Chem. Rev. 87 1987 381 398
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 41
    • 0032978537 scopus 로고    scopus 로고
    • 2 in isolated skeletal muscle fibers
    • 2 in isolated skeletal muscle fibers J. Appl. Physiol. 86 1999 720 724
    • (1999) J. Appl. Physiol. , vol.86 , pp. 720-724
    • Hogan, M.C.1
  • 42
    • 0035190320 scopus 로고    scopus 로고
    • Skeletal muscle intracellular PO(2) assessed by myoglobin desaturation: Response to graded exercise
    • R.S. Richardson, S.C. Newcomer, and E.A. Noyszewski Skeletal muscle intracellular PO(2) assessed by myoglobin desaturation: response to graded exercise J. Appl. Physiol. 91 2001 2679 2685
    • (2001) J. Appl. Physiol. , vol.91 , pp. 2679-2685
    • Richardson, R.S.1    Newcomer, S.C.2    Noyszewski, E.A.3
  • 43
    • 79957635293 scopus 로고    scopus 로고
    • Why is the partial oxygen pressure of human tissues a crucial parameter? Small molecules and hypoxia
    • A. Carreau, B. El Hafny-Rahbi, A. Matejuk, C. Grillon, and C. Kieda Why is the partial oxygen pressure of human tissues a crucial parameter? Small molecules and hypoxia J. Cell. Mol. Med. 15 2011 1239 1253
    • (2011) J. Cell. Mol. Med. , vol.15 , pp. 1239-1253
    • Carreau, A.1    El Hafny-Rahbi, B.2    Matejuk, A.3    Grillon, C.4    Kieda, C.5
  • 44
    • 0033568619 scopus 로고    scopus 로고
    • The effect of protein structure on oxygen quenching of phosphorescence
    • G. Strambini, and P. Cioni The effect of protein structure on oxygen quenching of phosphorescence J. Am. Chem. Soc. 121 1999 8337 8344
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8337-8344
    • Strambini, G.1    Cioni, P.2
  • 45
    • 84908432562 scopus 로고    scopus 로고
    • Carbon-centered radicals add reversibly to histidine - Implications
    • T. Nauser, and A. Carreras Carbon-centered radicals add reversibly to histidine - implications Chem. Commun. (Cambridge) 50 2014 14349 14351
    • (2014) Chem. Commun. (Cambridge) , vol.50 , pp. 14349-14351
    • Nauser, T.1    Carreras, A.2
  • 47
    • 80054904377 scopus 로고    scopus 로고
    • Reversible hydrogen transfer reactions of cysteine thiyl radicals in peptides: The conversion of cysteine into dehydroalanine and alanine, and of alanine into dehydroalanine
    • O. Mozziconacci, B.A. Kerwin, and C. Schöneich Reversible hydrogen transfer reactions of cysteine thiyl radicals in peptides: the conversion of cysteine into dehydroalanine and alanine, and of alanine into dehydroalanine J. Phys. Chem. B 115 2011 12287 12305
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12287-12305
    • Mozziconacci, O.1    Kerwin, B.A.2    Schöneich, C.3
  • 48
    • 58149151045 scopus 로고    scopus 로고
    • Reversible intramolecular hydrogen transfer between protein cysteine thiyl radicals and alpha C-H bonds in insulin: Control of selectivity by secondary structure
    • O. Mozziconacci, T.D. Williams, B.A. Kerwin, and C. Schöneich 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 112 2008 15921 15932
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15921-15932
    • Mozziconacci, O.1    Williams, T.D.2    Kerwin, B.A.3    Schöneich, C.4
  • 49
    • 84860596640 scopus 로고    scopus 로고
    • Photolysis of recombinant human insulin in the solid state: Formation of a dithiohemiacetal product at the C-terminal disulfide bond
    • O. Mozziconacci, J. Haywood, E.M. Gorman, E. Munson, and C. Schöneich Photolysis of recombinant human insulin in the solid state: formation of a dithiohemiacetal product at the C-terminal disulfide bond Pharm. Res. 29 2012 121 133
    • (2012) Pharm. Res. , vol.29 , pp. 121-133
    • Mozziconacci, O.1    Haywood, J.2    Gorman, E.M.3    Munson, E.4    Schöneich, C.5
  • 50
    • 84876458314 scopus 로고    scopus 로고
    • The photolysis of disulfide bonds in IgG1 and IgG2 leads to selective intramolecular hydrogen transfer reactions of cysteine thiyl radicals, probed by covalent H/D exchange and RPLC-MS/MS analysis
    • S. Zhou, O. Mozziconacci, B.A. Kerwin, and C. Schöneich The photolysis of disulfide bonds in IgG1 and IgG2 leads to selective intramolecular hydrogen transfer reactions of cysteine thiyl radicals, probed by covalent H/D exchange and RPLC-MS/MS analysis Pharm. Res. 30 2013 1291 1299
    • (2013) Pharm. Res. , vol.30 , pp. 1291-1299
    • Zhou, S.1    Mozziconacci, O.2    Kerwin, B.A.3    Schöneich, C.4
  • 51
    • 84923905764 scopus 로고    scopus 로고
    • Sequence-specific formation of D-amino acids in a monoclonal antibody during light exposure
    • O. Mozziconacci, and C. Schöneich Sequence-specific formation of D-amino acids in a monoclonal antibody during light exposure Mol. Pharm. 11 2014 4291 4297
    • (2014) Mol. Pharm. , vol.11 , pp. 4291-4297
    • Mozziconacci, O.1    Schöneich, C.2
  • 52
    • 34548829834 scopus 로고
    • Radical-cations as reference chromogens in kinetic-studies of one-electron transfer-reactions - Pulse-radiolysis studies of 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate)
    • B.S. Wolfenden, and R.L. Willson Radical-cations as reference chromogens in kinetic-studies of one-electron transfer-reactions - pulse-radiolysis studies of 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) J. Chem. Soc. Perkins Trans. 2 1982 805 812
    • (1982) J. Chem. Soc. Perkins Trans. , vol.2 , pp. 805-812
    • Wolfenden, B.S.1    Willson, R.L.2
  • 53
    • 0001065226 scopus 로고    scopus 로고
    • Rate constant determination for the reaction of hydroxyl and glutathione thiyl radicals with glutathione in aqueous solution
    • S.P. Mezyk Rate constant determination for the reaction of hydroxyl and glutathione thiyl radicals with glutathione in aqueous solution J. Phys. Chem. 100 1996 8861 8866
    • (1996) J. Phys. Chem. , vol.100 , pp. 8861-8866
    • Mezyk, S.P.1
  • 55
    • 0027390329 scopus 로고
    • Superoxide as an intracellular radical sink
    • C.C. Winterbourn Superoxide as an intracellular radical sink Free Radic. Biol. Med. 14 1993 85 90
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 85-90
    • Winterbourn, C.C.1
  • 56
    • 0025572691 scopus 로고
    • •- radical induced cleavage of disulfide bonds in proteins: A gamma-ray and pulse radiolysis mechanistic investigation
    • •- radical induced cleavage of disulfide bonds in proteins: a gamma-ray and pulse radiolysis mechanistic investigation Biochemistry 29 1990 10978 10989
    • (1990) Biochemistry , vol.29 , pp. 10978-10989
    • Favaudon, V.1    Tourbez, H.2    Houée-Levin, C.3    Lhoste, J.M.4
  • 57
    • 0030134581 scopus 로고    scopus 로고
    • LINAC/LASER determination of the absolute rate constant for thiyl and hydroxyl radical reaction with sulfhydryls in aqueous solution: Mercaptoethanol, cysteamine, and N-acetyl-L-cysteine
    • S.P. Mezyk LINAC/LASER determination of the absolute rate constant for thiyl and hydroxyl radical reaction with sulfhydryls in aqueous solution: mercaptoethanol, cysteamine, and N-acetyl-L-cysteine J. Phys. Chem. 100 1996 8295 8301
    • (1996) J. Phys. Chem. , vol.100 , pp. 8295-8301
    • Mezyk, S.P.1
  • 58
    • 84970583204 scopus 로고
    • Outer-sphere electron-transfer reactions of ascorbate anions
    • N.H. Williams, and J.K. Yandell Outer-sphere electron-transfer reactions of ascorbate anions Aust. J. Chem. 35 1982 1133 1144
    • (1982) Aust. J. Chem. , vol.35 , pp. 1133-1144
    • Williams, N.H.1    Yandell, J.K.2
  • 59
    • 34248581972 scopus 로고    scopus 로고
    • The oxidizing power of the glutathione thiyl radical as measured by its electrode potential at physiological pH
    • E. Madej, and P. Wardman The oxidizing power of the glutathione thiyl radical as measured by its electrode potential at physiological pH Arch. Biochem. Biophys. 462 2007 94 102
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 94-102
    • Madej, E.1    Wardman, P.2
  • 60
    • 77954142511 scopus 로고    scopus 로고
    • Electrode potentials of partially reduced oxygen species, from dioxygen to water
    • W.H. Koppenol, D.M. Stanbury, and P.L. Bounds Electrode potentials of partially reduced oxygen species, from dioxygen to water Free Radic. Biol. Med. 49 2010 317 322
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 317-322
    • Koppenol, W.H.1    Stanbury, D.M.2    Bounds, P.L.3
  • 61
    • 84905695327 scopus 로고    scopus 로고
    • Why selenocysteine replaces cysteine in thioredoxin reductase: A radical hypothesis
    • T. Nauser, D. Steinmann, G. Grassi, and W.H. Koppenol Why selenocysteine replaces cysteine in thioredoxin reductase: a radical hypothesis Biochemistry 53 2014 5017 5022
    • (2014) Biochemistry , vol.53 , pp. 5017-5022
    • Nauser, T.1    Steinmann, D.2    Grassi, G.3    Koppenol, W.H.4
  • 63
    • 84923905763 scopus 로고    scopus 로고
    • Gitler, C., Danon, A., editors. London: Imperial College Press
    • Winterbourn, C. C. In: Gitler, C., Danon, A., editors. Cellular Implications of Redox Signaling. London: Imperial College Press; 2003. p. 175-190.
    • (2003) Cellular Implications of Redox Signaling , pp. 175-190
    • Winterbourn, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.