메뉴 건너뛰기




Volumn 9, Issue 1, 1996, Pages 318-325

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

Author keywords

[No Author keywords available]

Indexed keywords

5,5 DIMETHYL 1 PYRROLINE 1 OXIDE; CUMENE HYDROPEROXIDE; CYTOCHROME P450; FREE RADICAL; PROPANE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0030068523     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx9501501     Document Type: Article
Times cited : (57)

References (47)
  • 1
    • 0015839164 scopus 로고
    • Microsomal electron transport. I. Reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase and cytochrome P450 as electron carriers in microsomal NADPH-peroxidase activity
    • Hrycay, E. G., and O'Brien, P. J. (1973) Microsomal electron transport. I. Reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase and cytochrome P450 as electron carriers in microsomal NADPH-peroxidase activity. Arch. Biochem Biophys. 157, 7-22.
    • (1973) Arch. Biochem Biophys. , vol.157 , pp. 7-22
    • Hrycay, E.G.1    O'Brien, P.J.2
  • 2
    • 0015868089 scopus 로고
    • Microsomal-catalyzed hydroperoxide-dependent C-oxidation of amines
    • Kadlubar, F. F., Morton, K. C., and Ziegler, D. M. (1973) Microsomal-catalyzed hydroperoxide-dependent C-oxidation of amines. Biochem. Biophys. Res. Commun. 54, 1255-1261
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 1255-1261
    • Kadlubar, F.F.1    Morton, K.C.2    Ziegler, D.M.3
  • 3
    • 0017113579 scopus 로고
    • Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P450
    • Nordblom, G. D., White, R. E., and Coon, M. J. (1976) Studies on hydroperoxide-dependent substrate hydroxylation by purified liver microsomal cytochrome P450 Arch. Biochem. Biophys 175, 524-533.
    • (1976) Arch. Biochem. Biophys , vol.175 , pp. 524-533
    • Nordblom, G.D.1    White, R.E.2    Coon, M.J.3
  • 4
    • 0019274781 scopus 로고
    • Radical mechanism of aminopyrine oxidation by cumene hydroperoxide catalyzed by purified liver microsomal cytochrome P450
    • Griffin, B. W., Marth, C., Yasukochi, Y., and Masters, B. S. S. (1980) Radical mechanism of aminopyrine oxidation by cumene hydroperoxide catalyzed by purified liver microsomal cytochrome P450. Arch. Biochem Biophys. 205, 543-553.
    • (1980) Arch. Biochem Biophys. , vol.205 , pp. 543-553
    • Griffin, B.W.1    Marth, C.2    Yasukochi, Y.3    Masters, B.S.S.4
  • 5
    • 9044249768 scopus 로고
    • Catalytic activity and stereospecificity of phenobarbital-inducible and 5,6-benzoflavone-inducible isozymes of liver microsomal cytochrome P450 in the oxygenation of benzo[α]pyrene and trans-7,8-dihydroxy-7,8-dihydrobenzo[α]pyrene
    • (Coon, M. J., Conney, A. H., Estabrook, R. W., Gelboin, H. V., Gillette, J. R., and O'Brien, P. J. Eds.) Academic Press, Inc., New York
    • Vatsis, K. P., Deutsch, J., Gelboin, H. V., and Coon, M. J. (1980) Catalytic activity and stereospecificity of phenobarbital-inducible and 5,6-benzoflavone-inducible isozymes of liver microsomal cytochrome P450 in the oxygenation of benzo[α]pyrene and trans-7,8-dihydroxy-7,8-dihydrobenzo[α]pyrene. In Microsomes, Drug Oxidations, and Chemical Carcinogenesis (Coon, M. J., Conney, A. H., Estabrook, R. W., Gelboin, H. V., Gillette, J. R., and O'Brien, P. J. Eds.) Vol. II, pp 1065-1080, Academic Press, Inc., New York.
    • (1980) Microsomes, Drug Oxidations, and Chemical Carcinogenesis , vol.2 , pp. 1065-1080
    • Vatsis, K.P.1    Deutsch, J.2    Gelboin, H.V.3    Coon, M.J.4
  • 6
    • 0018817225 scopus 로고
    • Oxygen activation by cytochrome P450
    • White, R. E., and Coon, M. J. (1980) Oxygen activation by cytochrome P450. Annu. Rev. Biochem. 49, 315-356.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 315-356
    • White, R.E.1    Coon, M.J.2
  • 7
    • 33847799949 scopus 로고
    • Aliphatic hydroxylation via oxygen rebound oxygen transfer catalyzed by iron
    • Groves, J. T., and MeClusky, G. A. (1976) Aliphatic hydroxylation via oxygen rebound oxygen transfer catalyzed by iron. J. Am. Chem. Soc. 98, 859-861.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 859-861
    • Groves, J.T.1    Meclusky, G.A.2
  • 8
    • 9044221834 scopus 로고
    • Evaluation of homolytic and heterolytic mechanisms of peroxide oxygen-oxygen bond cleavage by cytochrome P450
    • (Nozaki, M., Yamamoto, S., Ishimura, T., Coon, M. J., Ernster, L., and Estabrook, R W., Eds.) Academic Press, Inc., New York
    • Coon, M. J., and Blake, R. C., II (1982) Evaluation of homolytic and heterolytic mechanisms of peroxide oxygen-oxygen bond cleavage by cytochrome P450. In Oxygenases and Oxygen Metabolism (Nozaki, M., Yamamoto, S., Ishimura, T., Coon, M. J., Ernster, L., and Estabrook, R W., Eds.) pp 485-495, Academic Press, Inc., New York.
    • (1982) Oxygenases and Oxygen Metabolism , pp. 485-495
    • Coon, M.J.1    Blake II, R.C.2
  • 9
    • 0022994793 scopus 로고
    • The mechanism of cumene hydroperoxide-dependent lipid peroxidation: The function of cytochrome P450
    • Weiss, R. K., and Estabrook, R. W. (1986) The mechanism of cumene hydroperoxide-dependent lipid peroxidation: The function of cytochrome P450. Arch. Biochem. Biophys. 251, 348-360.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 348-360
    • Weiss, R.K.1    Estabrook, R.W.2
  • 10
    • 0022220110 scopus 로고
    • Interaction of cytochrome P450 with a hydroperoxide derived from butylated hydroxytoluene: Mechanism of isomerization
    • Thompson, J. A., and Wand, M. D. (1985) Interaction of cytochrome P450 with a hydroperoxide derived from butylated hydroxytoluene: Mechanism of isomerization. J. Biol. Chem. 260, 10637-10644.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10637-10644
    • Thompson, J.A.1    Wand, M.D.2
  • 11
    • 0023137251 scopus 로고
    • Hydrocarbon formation in the reductive cleavage of hydroperoxides by cytochrome P450
    • Vaz, A. D. N., and Coon, M. J. (1987) Hydrocarbon formation in the reductive cleavage of hydroperoxides by cytochrome P450. Proc. Natl. Acad. Sci. U.S.A. 84, 1172-1176.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 1172-1176
    • Vaz, A.D.N.1    Coon, M.J.2
  • 12
    • 0024999291 scopus 로고
    • Reductive cleavage of hydroperoxides by cytochrome P450
    • Vaz, A. D. N., and Coon, M. J. (1990) Reductive cleavage of hydroperoxides by cytochrome P450 Methods Enzymol. 186, 278-282.
    • (1990) Methods Enzymol. , vol.186 , pp. 278-282
    • Vaz, A.D.N.1    Coon, M.J.2
  • 14
    • 0028181731 scopus 로고
    • 319 mutations of cytochrome P450 1A2 remarkably enhance homolytic O-O cleavage of alkyl hydroperoxides: An optical absorption spectral study
    • 319 mutations of cytochrome P450 1A2 remarkably enhance homolytic O-O cleavage of alkyl hydroperoxides: An optical absorption spectral study. J. Biol. Chem. 269, 13296-13304.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13296-13304
    • Shimizu, T.1    Murakami, Y.2    Hatano, M.3
  • 15
    • 0001707019 scopus 로고
    • Homolytic and heterolytic oxygen-oxygen bond scissions accompanying oxygen transfer to iron(III) porphyrins by percarboxylic acids and hydroperoxides. A mechanistic criterion for peroxidase and cytochrome P450
    • Lee, W. A., and Bruice, T. C. (1985) Homolytic and heterolytic oxygen-oxygen bond scissions accompanying oxygen transfer to iron(III) porphyrins by percarboxylic acids and hydroperoxides. A mechanistic criterion for peroxidase and cytochrome P450. J. Am. Chem. Soc. 107, 513-514.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 513-514
    • Lee, W.A.1    Bruice, T.C.2
  • 16
    • 0024457086 scopus 로고
    • Mechanistic aspects of cytochrome P450-hydroperoxide interactions: Substituent effects on degradative pathways
    • Thompson, J. A., and Yumibe, N. P. (1989) Mechanistic aspects of cytochrome P450-hydroperoxide interactions: Substituent effects on degradative pathways. Drug Metab. Rev. 20, 365-378.
    • (1989) Drug Metab. Rev. , vol.20 , pp. 365-378
    • Thompson, J.A.1    Yumibe, N.P.2
  • 17
    • 0028920062 scopus 로고
    • Interactions of peroxyquinols with cytochromes P450 2B1, 3A1, and 3A5: Influence of the apoprotein on heterolytic versus homolytic O-O bond cleavage
    • Correia , M. A., Yao, K., Allentoff, A. J., Wrighton, S. A., and Thompson, J. A. (1995) Interactions of peroxyquinols with cytochromes P450 2B1, 3A1, and 3A5: Influence of the apoprotein on heterolytic versus homolytic O-O bond cleavage. Arch. Biochem. Biophys. 317, 471-478.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 471-478
    • Correia, M.A.1    Yao, K.2    Allentoff, A.J.3    Wrighton, S.A.4    Thompson, J.A.5
  • 18
    • 0019890232 scopus 로고
    • Skin tumor-promoting activity of benzoyl peroxide, a widely used free radical-generating compound
    • Slaga, T. J., Klein-Szanto, A. J. P., Triplett, L. L., Yotti, L. P., and Trosko, J. E. (1981) Skin tumor-promoting activity of benzoyl peroxide, a widely used free radical-generating compound. Science 213, 1023-1025.
    • (1981) Science , vol.213 , pp. 1023-1025
    • Slaga, T.J.1    Klein-Szanto, A.J.P.2    Triplett, L.L.3    Yotti, L.P.4    Trosko, J.E.5
  • 19
    • 0023645563 scopus 로고
    • Generation of free radicals from organic hydroperoxide tumor promoters in isolated mouse keratinocytes: Formation of alkyl and alkoxyl radicals from tert-butyl hydroperoxide and cumene hydroperoxide
    • Taffe, B. G., Takahashi, N., Kensler, T. W., and Mason, R. P. (1987) Generation of free radicals from organic hydroperoxide tumor promoters in isolated mouse keratinocytes: Formation of alkyl and alkoxyl radicals from tert-butyl hydroperoxide and cumene hydroperoxide J. Biol. Chem 262, 12143-12149.
    • (1987) J. Biol. Chem , vol.262 , pp. 12143-12149
    • Taffe, B.G.1    Takahashi, N.2    Kensler, T.W.3    Mason, R.P.4
  • 20
    • 0026547659 scopus 로고
    • Detection of radicals produced by reaction of hydroperoxides with rat liver microsomal fractions
    • Greenley, T. L., and Davies, M. J. (1992) Detection of radicals produced by reaction of hydroperoxides with rat liver microsomal fractions. Biochim. Biophys. Acta 1116, 192-203.
    • (1992) Biochim. Biophys. Acta , vol.1116 , pp. 192-203
    • Greenley, T.L.1    Davies, M.J.2
  • 21
    • 0027159382 scopus 로고
    • Radical production from peroxide and peracid tumour promoters: EPR spin trapping studies
    • Greenley, T. L., and Davies, M. J. (1993) Radical production from peroxide and peracid tumour promoters: EPR spin trapping studies. Biochim. Biophys. Acta 1157, 23-31.
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 23-31
    • Greenley, T.L.1    Davies, M.J.2
  • 22
    • 0024970407 scopus 로고
    • Peroxyl, alkoxyl, and carbon-centered radical formation from organic hydroperoxides by chloroperoxidase
    • Chamulitrat, W., Takahashi, N., and Mason, R. P. (1989) Peroxyl, alkoxyl, and carbon-centered radical formation from organic hydroperoxides by chloroperoxidase. J. Biol. Chem. 264, 7889-7899.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7889-7899
    • Chamulitrat, W.1    Takahashi, N.2    Mason, R.P.3
  • 23
    • 0023858329 scopus 로고
    • Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with heme-proteins by electron spin resonance spectroscopy
    • Davies, M. J. (1988) Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with heme-proteins by electron spin resonance spectroscopy. Biochim. Biophys. Acta 964, 28-35.
    • (1988) Biochim. Biophys. Acta , vol.964 , pp. 28-35
    • Davies, M.J.1
  • 24
    • 0029010656 scopus 로고
    • Mechanism of radical production from the reaction of cytochrome c with organic hydroperoxides: An ESR spin trapping investigation
    • Barr, D. P., and Mason, R. P. (1995) Mechanism of radical production from the reaction of cytochrome c with organic hydroperoxides: An ESR spin trapping investigation. J. Biol. Chem. 270, 12709-12716.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12709-12716
    • Barr, D.P.1    Mason, R.P.2
  • 25
    • 0025059537 scopus 로고
    • A simple and rapid method for the purification of cytochrome P450 (form LM4)
    • Alterman, M. A., and Dowgii, A. I. (1990) A simple and rapid method for the purification of cytochrome P450 (form LM4). Biomed. Chromatogr. 4, 221-222.
    • (1990) Biomed. Chromatogr. , vol.4 , pp. 221-222
    • Alterman, M.A.1    Dowgii, A.I.2
  • 26
    • 0028358220 scopus 로고
    • Expression of modified human cytochrome P450 1A2 in Escherichia coli: Stabilization, purification, spectral characterization, and catalytic activities of the enzyme
    • Sandhu, P., Guo, Z., Baba, T., Martin, M. V., Tukey, R. H., and Guengerich, F. P. (1994) Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme. Arch. Biochem. Biophys. 309, 168-177.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 168-177
    • Sandhu, P.1    Guo, Z.2    Baba, T.3    Martin, M.V.4    Tukey, R.H.5    Guengerich, F.P.6
  • 27
    • 0000290799 scopus 로고
    • Determination of organic peroxides by physical, chemical, and colorimetric methods
    • (Swern, D., Ed.) Wiley Interscience, New York
    • Mair, R. D., and Hall, R. T. (1971) Determination of organic peroxides by physical, chemical, and colorimetric methods. In Organic Peroxides (Swern, D., Ed.) pp 535-635, Wiley Interscience, New York.
    • (1971) Organic Peroxides , pp. 535-635
    • Mair, R.D.1    Hall, R.T.2
  • 28
    • 0028455102 scopus 로고
    • Simulation of multiple isotropic spin-trap EPR spectra
    • Duling, D. R. (1994) Simulation of multiple isotropic spin-trap EPR spectra. J. Magn. Reson. 104B, 105-110.
    • (1994) J. Magn. Reson. , vol.104 B , pp. 105-110
    • Duling, D.R.1
  • 29
    • 0020479617 scopus 로고
    • The catalytic mechanism of cytochrome P450: Spin-trapping evidence for one electron substrate oxidation
    • Augusto, O., Beilan, H. S., and Ortiz de Montellano, P. R. (1982) The catalytic mechanism of cytochrome P450: Spin-trapping evidence for one electron substrate oxidation. J. Biol. Chem. 257, 11288-11295.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11288-11295
    • Augusto, O.1    Beilan, H.S.2    Ortiz De Montellano, P.R.3
  • 30
    • 0020563447 scopus 로고
    • NADH and NADPH inhibit lipid peroxidation promoted by hydroperoxides in rat liver microsomes
    • Cavallini, L., Valente, M., and Bindoli, A. (1983) NADH and NADPH inhibit lipid peroxidation promoted by hydroperoxides in rat liver microsomes. Biochim. Biophys Acta 752, 339-345.
    • (1983) Biochim. Biophys Acta , vol.752 , pp. 339-345
    • Cavallini, L.1    Valente, M.2    Bindoli, A.3
  • 31
    • 0001896864 scopus 로고
    • Peroxy radicals
    • Ingold, K. U. (1969) Peroxy radicals. Acc. Chem. Res. 2, 1-9.
    • (1969) Acc. Chem. Res. , vol.2 , pp. 1-9
    • Ingold, K.U.1
  • 32
    • 0026754737 scopus 로고
    • When are metal ion-dependent hydroxyl and alkoxyl radical adducts of 5,5-dimethyl-1-pyrroline N-oxide artifacts?
    • Hanna, P. M., Chamulitrat, W., and Mason, R. P. (1992) When are metal ion-dependent hydroxyl and alkoxyl radical adducts of 5,5-dimethyl-1-pyrroline N-oxide artifacts? Arch. Biochem. Biophys. 296, 640-644.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 640-644
    • Hanna, P.M.1    Chamulitrat, W.2    Mason, R.P.3
  • 33
    • 0021833801 scopus 로고
    • Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P450 heme
    • Schaefer, W. H., Harris, T. M., and Guengerich, F. P. (1985) Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P450 heme. Biochemistry 24, 3254-3263.
    • (1985) Biochemistry , vol.24 , pp. 3254-3263
    • Schaefer, W.H.1    Harris, T.M.2    Guengerich, F.P.3
  • 34
    • 0022535486 scopus 로고
    • Covalent binding to apoprotein is a major fate of heme in a variety of reactions in which cytochrome P450 is destroyed
    • Guengerich, F. P. (1986) Covalent binding to apoprotein is a major fate of heme in a variety of reactions in which cytochrome P450 is destroyed. Biochem. Biophys. Res. Commun. 138, 193-198.
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 193-198
    • Guengerich, F.P.1
  • 35
    • 0027530606 scopus 로고
    • Cumene hydroperoxide-mediated inactivation of cytochrome P450 2B1. Identification of an active site heme-modified peptide
    • Yao, K., Falick, A. M., Patel, N., and Correia, M. A. (1993) Cumene hydroperoxide-mediated inactivation of cytochrome P450 2B1. Identification of an active site heme-modified peptide. J. Biol. Chem. 268, 59-65.
    • (1993) J. Biol. Chem. , vol.268 , pp. 59-65
    • Yao, K.1    Falick, A.M.2    Patel, N.3    Correia, M.A.4
  • 36
    • 0028099510 scopus 로고
    • Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions
    • Karuzina, I. I., and Archakov, A. I. (1994) Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions. Free Radicals Biol. Med. 17, 557-567.
    • (1994) Free Radicals Biol. Med. , vol.17 , pp. 557-567
    • Karuzina, I.I.1    Archakov, A.I.2
  • 38
    • 33947471406 scopus 로고
    • The photooxidation of 2,2′ -azoisobutane at 25 °C
    • Thomas, S. S., and Calvert, J. G. (1962) The photooxidation of 2,2′ -azoisobutane at 25 °C. J. Am. Chem. Soc. 84, 4207-4212.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 4207-4212
    • Thomas, S.S.1    Calvert, J.G.2
  • 39
    • 0007758844 scopus 로고
    • Deuterium-isotope effects m the autoxidation of aralkyl hydrocarbons. Mechanism of the interaction of peroxy radicals
    • Russell, G. A. (1957) Deuterium-isotope effects m the autoxidation of aralkyl hydrocarbons. Mechanism of the interaction of peroxy radicals. J. Am. Chem. Soc. 79, 3871-3877.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 3871-3877
    • Russell, G.A.1
  • 40
    • 0040168541 scopus 로고
    • Ultraviolet photochemistry of acetatopentaamminecobalt(III) in aqueous solution
    • Kantrowitz, E. R., Hoffman, M. Z., and Endicott, J. F. (1971) Ultraviolet photochemistry of acetatopentaamminecobalt(III) in aqueous solution. J. Phys. Chem. 75, 1914-1920.
    • (1971) J. Phys. Chem. , vol.75 , pp. 1914-1920
    • Kantrowitz, E.R.1    Hoffman, M.Z.2    Endicott, J.F.3
  • 41
    • 0025652977 scopus 로고
    • Detection of myoglobin-derived radicals on reaction of metmyoglobin with hydrogen peroxide and other peroxidic compounds
    • Davies, M. J. (1990) Detection of myoglobin-derived radicals on reaction of metmyoglobin with hydrogen peroxide and other peroxidic compounds. Free Radical Res. Commun. 10, 361-370.
    • (1990) Free Radical Res. Commun. , vol.10 , pp. 361-370
    • Davies, M.J.1
  • 42
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • Gunther, M. R., Kelman, D. J., Corbett., J. T., and Mason, R. P. (1995) Self-peroxidation of metmyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. J. Biol Chem. 270, 16075-16081.
    • (1995) J. Biol Chem. , vol.270 , pp. 16075-16081
    • Gunther, M.R.1    Kelman, D.J.2    Corbett, J.T.3    Mason, R.P.4
  • 43
    • 0021099828 scopus 로고
    • Functional differences between peroxidase compound I and the cytochrome P450 reactive oxygen intermediate
    • McCarthy, M. B., and White, R. E., (1983) Functional differences between peroxidase compound I and the cytochrome P450 reactive oxygen intermediate. J. Biol. Chem. 258, 9153-9158.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9153-9158
    • McCarthy, M.B.1    White, R.E.2
  • 44
    • 0021100138 scopus 로고
    • Competing modes of peroxyacid flux through cytochrome P450
    • McCarthy, M. B., and White, R. E. (1983) Competing modes of peroxyacid flux through cytochrome P450. J. Biol. Chem. 258, 11610-11616.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11610-11616
    • McCarthy, M.B.1    White, R.E.2
  • 45
    • 84995049049 scopus 로고
    • Radical processes in lipids. A laser photolysis study of t-butoxy radical reactivity toward fatty acids
    • Small, R. D., Jr., Scaiano, J. C., and Patterson, L K. (1979) Radical processes in lipids. A laser photolysis study of t-butoxy radical reactivity toward fatty acids. Photochem. Photobiol. 29, 49-51.
    • (1979) Photochem. Photobiol. , vol.29 , pp. 49-51
    • Small Jr., R.D.1    Scaiano, J.C.2    Patterson, L.K.3
  • 46
    • 0019321958 scopus 로고
    • Evidence for a homolytic mechanism of peroxide oxygen-oxygen bond cleavage during substrate hdroxylation by cytochrome P450
    • White R. E., Sligar, S. G., and Coon, M. J. (1980) Evidence for a homolytic mechanism of peroxide oxygen-oxygen bond cleavage during substrate hdroxylation by cytochrome P450. J. Biol. Chem. 255, 11108-11111.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11108-11111
    • White, R.E.1    Sligar, S.G.2    Coon, M.J.3
  • 47
    • 0025938290 scopus 로고
    • Peroxyl free radicals: Biological reactive intermediates produced during lipid oxidation
    • Marnett, L. J. (1990) Peroxyl free radicals: Biological reactive intermediates produced during lipid oxidation. Adv. Exp. Med. Biol. 283, 65-70.
    • (1990) Adv. Exp. Med. Biol. , vol.283 , pp. 65-70
    • Marnett, L.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.