메뉴 건너뛰기




Volumn 49, Issue 3, 2010, Pages 437-446

Metabolic stability of superoxide and hydroxyl radical adducts of a cyclic nitrone toward rat liver microsomes and cytosol: A stopped-flow ESR spectroscopy study

Author keywords

Cyclic nitrones; Cytochromes P450; EPR spectroscopy; ESR spectroscopy; Hydroxyl radical; Spin trapping; Superoxide

Indexed keywords

ASCORBIC ACID; CYTOCHROME P450; GLUTATHIONE; HEMOPROTEIN; HORSERADISH PEROXIDASE; HYDROPEROXIDE; HYDROXYL RADICAL; METHEMOGLOBIN; NITRONE; SUPEROXIDE; 5-TERT-BUTOXYCARBONYL 5-METHYL-1-PYRROLINE N-OXIDE; AMINE OXIDE; HYDROGEN PEROXIDE; NITROGEN OXIDE; NITRONES; SPIN LABELING;

EID: 77954143678     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.04.035     Document Type: Article
Times cited : (23)

References (60)
  • 3
    • 73949132618 scopus 로고    scopus 로고
    • Oxidative stress in malignant progression: the role of clusterin, a sensitive cellular biosensor of free radicals
    • Trougakos I.P., Gonos E.S. Oxidative stress in malignant progression: the role of clusterin, a sensitive cellular biosensor of free radicals. Adv. Cancer Res. 2009, 104:171-210.
    • (2009) Adv. Cancer Res. , vol.104 , pp. 171-210
    • Trougakos, I.P.1    Gonos, E.S.2
  • 4
    • 62549102431 scopus 로고    scopus 로고
    • Reactive oxygen species: destroyers or messengers?
    • Bartosz G. Reactive oxygen species: destroyers or messengers?. Biochem. Pharmacol. 2009, 77:1303-1315.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1303-1315
    • Bartosz, G.1
  • 5
    • 0029815291 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective stratagem against oxidative injury
    • Cairo G., Castrusini E., Minotti G., Bernelli-Zazzera A. Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective stratagem against oxidative injury. FASEB J. 1996, 10:1326-1335.
    • (1996) FASEB J. , vol.10 , pp. 1326-1335
    • Cairo, G.1    Castrusini, E.2    Minotti, G.3    Bernelli-Zazzera, A.4
  • 6
    • 0030752458 scopus 로고    scopus 로고
    • Redox modulation of iron regulatory proteins by peroxynitrite
    • Bouton C., Hirling H., Drapier J.C. Redox modulation of iron regulatory proteins by peroxynitrite. J. Biol. Chem. 1997, 272:19969-19975.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19969-19975
    • Bouton, C.1    Hirling, H.2    Drapier, J.C.3
  • 7
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • Pryor W.A., Squadrito G.L. The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide. Am. J. Physiol. 1995, 268:L699-L722.
    • (1995) Am. J. Physiol. , vol.268
    • Pryor, W.A.1    Squadrito, G.L.2
  • 8
    • 0034281968 scopus 로고    scopus 로고
    • Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques
    • Barbacanne M.A., Souchard J.P., Darblade B., Iliou J.P., Nepveu F., Pipy B., Bayard F., Arnal J.F. Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques. Free Radic. Biol. Med. 2000, 29:388-396.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 388-396
    • Barbacanne, M.A.1    Souchard, J.P.2    Darblade, B.3    Iliou, J.P.4    Nepveu, F.5    Pipy, B.6    Bayard, F.7    Arnal, J.F.8
  • 9
    • 33646828379 scopus 로고    scopus 로고
    • Use of spectroscopic probes for detection of reactive oxygen species
    • Bartosz G. Use of spectroscopic probes for detection of reactive oxygen species. Clin. Chim. Acta 2006, 368:53-76.
    • (2006) Clin. Chim. Acta , vol.368 , pp. 53-76
    • Bartosz, G.1
  • 10
    • 49249083962 scopus 로고    scopus 로고
    • Real-time amperometric analysis of reactive oxygen and nitrogen species released by single immunostimulated macrophages
    • Amatore C., Arbault S., Bouton C., Drapier J.C., Ghandour H., Koh A.C.W. Real-time amperometric analysis of reactive oxygen and nitrogen species released by single immunostimulated macrophages. Chembiochem 2008, 9:1472-1480.
    • (2008) Chembiochem , vol.9 , pp. 1472-1480
    • Amatore, C.1    Arbault, S.2    Bouton, C.3    Drapier, J.C.4    Ghandour, H.5    Koh, A.C.W.6
  • 11
    • 42149158251 scopus 로고    scopus 로고
    • Spin trapping of oxygen free radicals in chemical and biological systems: new traps, radicals and possibilities
    • Bacic G., Spasojevic I., Secerov B., Mojovic M. Spin trapping of oxygen free radicals in chemical and biological systems: new traps, radicals and possibilities. Spectrochim. Acta A 2008, 69:1354-1366.
    • (2008) Spectrochim. Acta A , vol.69 , pp. 1354-1366
    • Bacic, G.1    Spasojevic, I.2    Secerov, B.3    Mojovic, M.4
  • 12
    • 0032903261 scopus 로고    scopus 로고
    • Issues pertinent to the in vivo in situ spin trapping of free radicals
    • Pou S., Halpern H.J., Tsai P., Rosen G.M. Issues pertinent to the in vivo in situ spin trapping of free radicals. Acc. Chem. Res. 1999, 32:155-161.
    • (1999) Acc. Chem. Res. , vol.32 , pp. 155-161
    • Pou, S.1    Halpern, H.J.2    Tsai, P.3    Rosen, G.M.4
  • 13
    • 0035884737 scopus 로고    scopus 로고
    • Measurement of oxidative stress by EPR radical-probe technique
    • Valgimigli L., Pedulli G.F., Paolini M. Measurement of oxidative stress by EPR radical-probe technique. Free Radic. Biol. Med. 2001, 31:708-716.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 708-716
    • Valgimigli, L.1    Pedulli, G.F.2    Paolini, M.3
  • 14
    • 2442619131 scopus 로고    scopus 로고
    • Detection of reactive oxygen and nitrogen species by EPR spin trapping
    • Villamena F.A., Zweier J.L. Detection of reactive oxygen and nitrogen species by EPR spin trapping. Antioxid. Redox Signal. 2004, 6:619-629.
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 619-629
    • Villamena, F.A.1    Zweier, J.L.2
  • 16
    • 0017815770 scopus 로고
    • Considerations in the spin trapping of superoxide and hydroxyl radical in aqueous systems using 5, 5-dimethyl-1-pyrroline-1-oxide
    • Buettner G.R., Oberley L.W. Considerations in the spin trapping of superoxide and hydroxyl radical in aqueous systems using 5, 5-dimethyl-1-pyrroline-1-oxide. Biochem. Biophys. Res. Commun. 1978, 83:69-74.
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 69-74
    • Buettner, G.R.1    Oberley, L.W.2
  • 17
    • 0018992113 scopus 로고
    • Spin trapping of superoxide and hydroxyl radical: practical aspects
    • Finkelstein E., Rosen E., Rauckman E.J. Spin trapping of superoxide and hydroxyl radical: practical aspects. Arch. Biochem. Biophys. 1980, 200:1-16.
    • (1980) Arch. Biochem. Biophys. , vol.200 , pp. 1-16
    • Finkelstein, E.1    Rosen, E.2    Rauckman, E.J.3
  • 19
    • 0027711846 scopus 로고
    • The spin trapping of superoxide and hydroxyl free radicals with DMPO (5, 5-dimethylpyrroline-N-oxide): more about iron
    • Buettner G.R. The spin trapping of superoxide and hydroxyl free radicals with DMPO (5, 5-dimethylpyrroline-N-oxide): more about iron. Free Radic. Res. Commun. 1993, 19:S79-S87.
    • (1993) Free Radic. Res. Commun. , vol.19
    • Buettner, G.R.1
  • 20
    • 0029013876 scopus 로고
    • 5-(Diethoxyphosphoryl)-5-methyl-1-pyrroline N-oxide: a new efficient phosphorylated nitrone for the in vitro and in vivo spin trapping of oxygen-centered radicals
    • Frejaville C., Karoui H., Tuccio B., Le Moigne F., Culcasi M., Pietri S., Lauricella R., Tordo P. 5-(Diethoxyphosphoryl)-5-methyl-1-pyrroline N-oxide: a new efficient phosphorylated nitrone for the in vitro and in vivo spin trapping of oxygen-centered radicals. J. Med. Chem. 1995, 38:258-265.
    • (1995) J. Med. Chem. , vol.38 , pp. 258-265
    • Frejaville, C.1    Karoui, H.2    Tuccio, B.3    Le Moigne, F.4    Culcasi, M.5    Pietri, S.6    Lauricella, R.7    Tordo, P.8
  • 21
    • 0031148677 scopus 로고    scopus 로고
    • Quantitative measurement of superoxide generation using the spin trap 5-(diethoxyphosphoryl)-5-methyl-1-pyrroline-N-oxide
    • Roubaud V., Sankarapandi S., Kuppusamy P., Tordo P., Zweier J.L. Quantitative measurement of superoxide generation using the spin trap 5-(diethoxyphosphoryl)-5-methyl-1-pyrroline-N-oxide. Anal. Biochem. 1997, 247:404-411.
    • (1997) Anal. Biochem. , vol.247 , pp. 404-411
    • Roubaud, V.1    Sankarapandi, S.2    Kuppusamy, P.3    Tordo, P.4    Zweier, J.L.5
  • 22
    • 0000945821 scopus 로고    scopus 로고
    • Evaluation of DEPMPO as a spin trapping agent in biological systems
    • Liu K.J., Miyake M., Panz T., Swartz H. Evaluation of DEPMPO as a spin trapping agent in biological systems. Free Radic. Biol. Med. 1999, 26:714-721.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 714-721
    • Liu, K.J.1    Miyake, M.2    Panz, T.3    Swartz, H.4
  • 23
    • 0035451497 scopus 로고    scopus 로고
    • Synthesis and biochemical applications of a solid cyclic nitrone spin trap: a relatively superior trap for detecting superoxide anions and glutathiyl radicals
    • Zhao H., Joseph J., Zhang H., Karoui H., Kalyanaraman B. Synthesis and biochemical applications of a solid cyclic nitrone spin trap: a relatively superior trap for detecting superoxide anions and glutathiyl radicals. Free Radic. Biol. Med. 2001, 31:599-606.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 599-606
    • Zhao, H.1    Joseph, J.2    Zhang, H.3    Karoui, H.4    Kalyanaraman, B.5
  • 24
    • 0036019831 scopus 로고    scopus 로고
    • Superoxide radical trapping and spin adduct decay of 5-tert-butoxycarbonyl-5-methyl-1-pyrroline N-oxide (BocMPO): kinetics and theoretical analysis
    • Villamena F.A., Zweier J.L. Superoxide radical trapping and spin adduct decay of 5-tert-butoxycarbonyl-5-methyl-1-pyrroline N-oxide (BocMPO): kinetics and theoretical analysis. J. Chem. Soc., Perkin Trans. 2002, 2:1340-1344.
    • (2002) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1340-1344
    • Villamena, F.A.1    Zweier, J.L.2
  • 25
    • 24144499158 scopus 로고    scopus 로고
    • Is there stereoselectivity in spin trapping superoxide by 5-tert-butoxycarbonyl-5-methyl-1-pyrroline N-oxide?
    • Tsai P., Marra J.M., Pou S., Bowman M.K., Rosen G.M. Is there stereoselectivity in spin trapping superoxide by 5-tert-butoxycarbonyl-5-methyl-1-pyrroline N-oxide?. J. Org. Chem. 2005, 70:7093-7097.
    • (2005) J. Org. Chem. , vol.70 , pp. 7093-7097
    • Tsai, P.1    Marra, J.M.2    Pou, S.3    Bowman, M.K.4    Rosen, G.M.5
  • 27
    • 0029858929 scopus 로고    scopus 로고
    • Degradation of DMPO adducts from hydroxyl and 1-hydroxyethyl radicals by rat liver microsomes
    • Reinke L.A., Moore D.R., McCay P.B. Degradation of DMPO adducts from hydroxyl and 1-hydroxyethyl radicals by rat liver microsomes. Free Radic. Res. 1996, 25:467-474.
    • (1996) Free Radic. Res. , vol.25 , pp. 467-474
    • Reinke, L.A.1    Moore, D.R.2    McCay, P.B.3
  • 28
    • 0017597954 scopus 로고
    • Formation and reduction of a nitroxide radical by liver microsomes
    • Rosen G.M., Rauckman E.J. Formation and reduction of a nitroxide radical by liver microsomes. Biochem. Pharmacol. 1977, 26:675-678.
    • (1977) Biochem. Pharmacol. , vol.26 , pp. 675-678
    • Rosen, G.M.1    Rauckman, E.J.2
  • 29
    • 0023107397 scopus 로고
    • Nonenzymatic bioreduction in rat liver and kidney of nitroxyl spin labels, potential contrast agents in magnetic resonance imaging
    • Eriksson U.G., Brasch R.C., Tozer T.N. Nonenzymatic bioreduction in rat liver and kidney of nitroxyl spin labels, potential contrast agents in magnetic resonance imaging. Drug Metab. Dispos. 1987, 15:155-160.
    • (1987) Drug Metab. Dispos. , vol.15 , pp. 155-160
    • Eriksson, U.G.1    Brasch, R.C.2    Tozer, T.N.3
  • 30
    • 0024604606 scopus 로고
    • Metabolism of aqueous soluble nitroxides in hepatocytes: effects of cell integrity, oxygen, and structure of nitroxides
    • Iannone A., Hu H.P., Tomasi A., Vannini V., Swartz H.M. Metabolism of aqueous soluble nitroxides in hepatocytes: effects of cell integrity, oxygen, and structure of nitroxides. Biochim. Biophys. Acta 1989, 99:90-96.
    • (1989) Biochim. Biophys. Acta , vol.99 , pp. 90-96
    • Iannone, A.1    Hu, H.P.2    Tomasi, A.3    Vannini, V.4    Swartz, H.M.5
  • 31
  • 32
    • 0025294771 scopus 로고
    • Metabolism of nitroxide spin labels in subcellular fraction of rat liver. I. Reduction by microsomes
    • Iannone A., Tomasi A., Vannini V., Swartz H.M. Metabolism of nitroxide spin labels in subcellular fraction of rat liver. I. Reduction by microsomes. Biochim. Biophys. Acta 1990, 1034:285-289.
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 285-289
    • Iannone, A.1    Tomasi, A.2    Vannini, V.3    Swartz, H.M.4
  • 33
    • 0025368277 scopus 로고
    • Metabolism of nitroxide spin labels in subcellular fractions of rat liver. II. Reduction in the cytosol
    • Iannone A., Tomasi A., Vannini V., Swartz H.M. Metabolism of nitroxide spin labels in subcellular fractions of rat liver. II. Reduction in the cytosol. Biochim. Biophys. Acta 1990, 1034:290-293.
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 290-293
    • Iannone, A.1    Tomasi, A.2    Vannini, V.3    Swartz, H.M.4
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 1964, 239:2379-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 38
    • 0016107350 scopus 로고
    • A rapid micromethod for the determination of ascorbic acid in plasma and tissues
    • Zannoni V., Lynch M., Goldstein S., Sato P. A rapid micromethod for the determination of ascorbic acid in plasma and tissues. Biochem. Med. 1974, 11:41-48.
    • (1974) Biochem. Med. , vol.11 , pp. 41-48
    • Zannoni, V.1    Lynch, M.2    Goldstein, S.3    Sato, P.4
  • 39
    • 0022517319 scopus 로고
    • Decrease of hepatic mitochondrial glutathione and mitochondrial injury induced by 1, 2-dibromoethane in the rat in vivo: effect of diethylmaleate pretreatment
    • Botti B., Bini A., Calligaro A., Meletti E., Tomasi A., Vannini V. Decrease of hepatic mitochondrial glutathione and mitochondrial injury induced by 1, 2-dibromoethane in the rat in vivo: effect of diethylmaleate pretreatment. Toxicol. Appl. Pharmacol. 1986, 83:494-505.
    • (1986) Toxicol. Appl. Pharmacol. , vol.83 , pp. 494-505
    • Botti, B.1    Bini, A.2    Calligaro, A.3    Meletti, E.4    Tomasi, A.5    Vannini, V.6
  • 40
    • 67650481933 scopus 로고    scopus 로고
    • Kinetic investigation of reaction of ascorbate and hydroxyl radical adduct of DPMO (5, 5-dimethyl-1-pyrroline N-oxide) studied by stopped-flow ESR
    • Sakurai Y., Sanuki H., Komatsu-Watanabe R., Ideguchi T., Yanagi N., Kawai K., Kanaori K., Tajima K. Kinetic investigation of reaction of ascorbate and hydroxyl radical adduct of DPMO (5, 5-dimethyl-1-pyrroline N-oxide) studied by stopped-flow ESR. Chem. Lett. 2008, 37:1270-1271.
    • (2008) Chem. Lett. , vol.37 , pp. 1270-1271
    • Sakurai, Y.1    Sanuki, H.2    Komatsu-Watanabe, R.3    Ideguchi, T.4    Yanagi, N.5    Kawai, K.6    Kanaori, K.7    Tajima, K.8
  • 41
    • 0030558710 scopus 로고    scopus 로고
    • Automatic computer simulations of ESR spectra
    • Rockenbauer A., Korecz L. Automatic computer simulations of ESR spectra. Appl. Magn. Reson. 1996, 10:29-43.
    • (1996) Appl. Magn. Reson. , vol.10 , pp. 29-43
    • Rockenbauer, A.1    Korecz, L.2
  • 42
    • 0003631066 scopus 로고    scopus 로고
    • Kluwer Academic/Plenum, New York, P.R. Ortiz de Montellano (Ed.)
    • Cytochrome P450. Structure, mechanism and biochemistry 2005, Kluwer Academic/Plenum, New York. third ed. P.R. Ortiz de Montellano (Ed.).
    • (2005) Cytochrome P450. Structure, mechanism and biochemistry
  • 45
    • 0021262955 scopus 로고
    • Oxidation of nitroxide radicals by reaction of hemoglobin with hydrogen peroxide
    • Yamaguchi T., Nakano T., Kimoto E. Oxidation of nitroxide radicals by reaction of hemoglobin with hydrogen peroxide. Biochem. Biophys. Res. Commun. 1984, 120:534-539.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 534-539
    • Yamaguchi, T.1    Nakano, T.2    Kimoto, E.3
  • 46
    • 67449097663 scopus 로고    scopus 로고
    • Spin scavenging analysis of myoglobin protein-centered radicals using stable nitroxide radicals: characterization of oxoammonium cation-induced modifications
    • Lardinois O.M., Maltby D.A., Medzihradszky K.F., Ortiz de Montellano P.R., Tomer R.P., Mason K.B., Deterding L.J. Spin scavenging analysis of myoglobin protein-centered radicals using stable nitroxide radicals: characterization of oxoammonium cation-induced modifications. Chem. Res. Toxicol. 2009, 22:1034-1049.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1034-1049
    • Lardinois, O.M.1    Maltby, D.A.2    Medzihradszky, K.F.3    Ortiz de Montellano, P.R.4    Tomer, R.P.5    Mason, K.B.6    Deterding, L.J.7
  • 48
    • 0029957646 scopus 로고    scopus 로고
    • Stimulation by nitroxides of catalase-like activity of hemeproteins. Kinetics and mechanism
    • Krishna M.C., Samuni A., Taira J., Goldstein S., Mitchell J.B., Russo A. Stimulation by nitroxides of catalase-like activity of hemeproteins. Kinetics and mechanism. J. Biol. Chem. 1996, 271:26018-26025.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26018-26025
    • Krishna, M.C.1    Samuni, A.2    Taira, J.3    Goldstein, S.4    Mitchell, J.B.5    Russo, A.6
  • 49
    • 0027351798 scopus 로고
    • The effects of myoglobin and apomyoglobin on the formation and stability of the hydroxyl radical adduct of 5, 5-dimethyl-1-pyrroline-N-oxide
    • Yang W.D., DeBono D., Symons M.C. The effects of myoglobin and apomyoglobin on the formation and stability of the hydroxyl radical adduct of 5, 5-dimethyl-1-pyrroline-N-oxide. Free Radic. Res. Commun. 1993, 18:99-106.
    • (1993) Free Radic. Res. Commun. , vol.18 , pp. 99-106
    • Yang, W.D.1    DeBono, D.2    Symons, M.C.3
  • 51
    • 0000166417 scopus 로고
    • Detection of superoxide generated by endothelial cells
    • Rosen G.M., Freeman B.A. Detection of superoxide generated by endothelial cells. Proc. Natl Acad. Sci. U. S. A. 1984, 81:7269-7273.
    • (1984) Proc. Natl Acad. Sci. U. S. A. , vol.81 , pp. 7269-7273
    • Rosen, G.M.1    Freeman, B.A.2
  • 52
    • 0032868198 scopus 로고    scopus 로고
    • NMR spin trapping: detection of free radical reactions using a phosphorus-containing nitrone spin trap
    • Khramtsov V., Berliner L.J., Clanton T.L. NMR spin trapping: detection of free radical reactions using a phosphorus-containing nitrone spin trap. Magn. Reson. Med. 1999, 42:228-234.
    • (1999) Magn. Reson. Med. , vol.42 , pp. 228-234
    • Khramtsov, V.1    Berliner, L.J.2    Clanton, T.L.3
  • 54
    • 2442509005 scopus 로고    scopus 로고
    • Conversion of the 2, 2, 6, 6-tetramethylpiperidine moiety to a 2, 2-dimethylpyrrolidine by cytochrome P450: evidence for a mechanism involving nitroxide radicals and heme iron
    • Yin W., Mitra K., Stearns R.A., Baillie T.A., Kumar S. Conversion of the 2, 2, 6, 6-tetramethylpiperidine moiety to a 2, 2-dimethylpyrrolidine by cytochrome P450: evidence for a mechanism involving nitroxide radicals and heme iron. Biochemistry 2004, 43:5455-5466.
    • (2004) Biochemistry , vol.43 , pp. 5455-5466
    • Yin, W.1    Mitra, K.2    Stearns, R.A.3    Baillie, T.A.4    Kumar, S.5
  • 55
    • 1942520360 scopus 로고    scopus 로고
    • Using anti-5, 5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping
    • Mason R.P. Using anti-5, 5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping. Free Radic. Biol. Med. 2004, 36:1214-1223.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1214-1223
    • Mason, R.P.1
  • 56
    • 0001591335 scopus 로고
    • Mechanistic studies on the formation of aminoxyl radicals from 5, 5-dimethyl-1-pyrroline-N-oxide in Fenton systems. Characterization of key precursors giving rise to background ESR signals
    • Makino K., Hagi A., Ide H., Murakami A. Mechanistic studies on the formation of aminoxyl radicals from 5, 5-dimethyl-1-pyrroline-N-oxide in Fenton systems. Characterization of key precursors giving rise to background ESR signals. Can. J. Chem. 1992, 70:2818-2827.
    • (1992) Can. J. Chem. , vol.70 , pp. 2818-2827
    • Makino, K.1    Hagi, A.2    Ide, H.3    Murakami, A.4
  • 57
    • 1642588204 scopus 로고    scopus 로고
    • Rapid formation of 4-hydroxy-2-nonenal, malondialdehyde, and phosphatidylcholine aldehyde from phospholipid hydroperoxide by hemoproteins
    • Hayashi T., Uchida K., Takebe G., Takahashi K. Rapid formation of 4-hydroxy-2-nonenal, malondialdehyde, and phosphatidylcholine aldehyde from phospholipid hydroperoxide by hemoproteins. Free Radic. Biol. Med. 2004, 36:1025-1033.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1025-1033
    • Hayashi, T.1    Uchida, K.2    Takebe, G.3    Takahashi, K.4
  • 58
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich F.P. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 2001, 14:611-650.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 59
    • 0030068523 scopus 로고    scopus 로고
    • Reaction of cytochrome P450 with cumene hydroperoxide: ESR spin trapping evidence for the homolytic scission of the peroxide O-O bond by ferric cytochrome P450 1A2
    • Barr D.P., Martin M.V., Guengerich F.P., Mason R.P. Reaction of cytochrome P450 with cumene hydroperoxide: ESR spin trapping evidence for the homolytic scission of the peroxide O-O bond by ferric cytochrome P450 1A2. Chem. Res. Toxicol. 1996, 9:318-325.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 318-325
    • Barr, D.P.1    Martin, M.V.2    Guengerich, F.P.3    Mason, R.P.4
  • 60
    • 25444520504 scopus 로고    scopus 로고
    • Nitric oxide release from the unimolecular decomposition of the superoxide radical anion adduct of cyclic nitrones in aqueous medium
    • Locigno E.J., Zweier J.L., Villamena F.A. Nitric oxide release from the unimolecular decomposition of the superoxide radical anion adduct of cyclic nitrones in aqueous medium. Org. Biomol. Chem. 2005, 3:3220-3227.
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 3220-3227
    • Locigno, E.J.1    Zweier, J.L.2    Villamena, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.