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Volumn 24, Issue 2, 1998, Pages 269-279

Heme protein radicals: Formation, fate, and biological consequences

Author keywords

Electron paramagnetic resonance; Electron tunneling; Hemoglobin; Hydrogen peroxide; Myoglobin; Myoglobin radicals; Oxoferryl; Protein radicals; Tyrosyl radicals

Indexed keywords

HEMOPROTEIN; MYOGLOBIN;

EID: 0031984429     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00226-8     Document Type: Article
Times cited : (128)

References (62)
  • 1
    • 0021041598 scopus 로고
    • Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxiy-5, 8, 11, 13-eicosatetraenoic acid
    • Walters F. P., Kennedy F. G., Jones D. P. Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxiy-5, 8, 11, 13-eicosatetraenoic acid. FEBS Lett. 163:1983;292-296.
    • (1983) FEBS Lett. , vol.163 , pp. 292-296
    • Walters, F.P.1    Kennedy, F.G.2    Jones, D.P.3
  • 2
    • 0344972032 scopus 로고
    • Role of ferryl myoglobin in lipid peroxidation and its reduction to met- Or oxymyoglobin by glutathione, quinones, quinone thioether derivatives, and ascorbate
    • Vigo-Pelfrey Boca Raton, FL: CRC Press
    • Galaris D., Buffinton G., Hochstein P., Cadenas E. Role of ferryl myoglobin in lipid peroxidation and its reduction to met- or oxymyoglobin by glutathione, quinones, quinone thioether derivatives, and ascorbate. Vigo-Pelfrey. Membrane lipid oxidation. 1:1990;269 CRC Press, Boca Raton, FL.
    • (1990) Membrane Lipid Oxidation , vol.1 , pp. 269
    • Galaris, D.1    Buffinton, G.2    Hochstein, P.3    Cadenas, E.4
  • 3
    • 0025616146 scopus 로고
    • Detection of ferryl myoglobin in the isolated ischemic rat heart
    • Arduini A., Eddy L., Hochstein P. Detection of ferryl myoglobin in the isolated ischemic rat heart. Free Radic. Biol. Med. 9:1990;511-513.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 511-513
    • Arduini, A.1    Eddy, L.2    Hochstein, P.3
  • 4
    • 0001202803 scopus 로고
    • The reaction between metmyoglobin and hydrogen peroxide
    • George P., Irvine D. H. The reaction between metmyoglobin and hydrogen peroxide. Biochem. J. 52:1952;511-517.
    • (1952) Biochem. J. , vol.52 , pp. 511-517
    • George, P.1    Irvine, D.H.2
  • 6
    • 0028360918 scopus 로고
    • Ferrylmyoglobin: Formation and chemical reactivity toward electron-donating compounds
    • Giulivi C., Cadenas E. Ferrylmyoglobin: Formation and chemical reactivity toward electron-donating compounds. Methods Enzymol. 233:1994;189-202.
    • (1994) Methods Enzymol. , vol.233 , pp. 189-202
    • Giulivi, C.1    Cadenas, E.2
  • 7
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • King N. K., Winfield M. E. The mechanism of metmyoglobin oxidation. J. Biol. Chem. 238:1963;1520-1528.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1520-1528
    • King, N.K.1    Winfield, M.E.2
  • 9
    • 0024309382 scopus 로고
    • Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link
    • Catalano C. E., Choe Y. S., Ortiz de Montellano P. R. Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link. J. Biol. Chem. 264:1989;10534-10537.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10534-10537
    • Catalano, C.E.1    Choe, Y.S.2    Ortiz De Montellano, P.R.3
  • 10
    • 0027509149 scopus 로고
    • The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and β-methylstyrene by recombinant sperm whale myoglobin
    • Rao S. I., Wilks A., Ortiz de Montellano P. R. The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and β-methylstyrene by recombinant sperm whale myoglobin. J. Biol. Chem. 268:1993;803-809.
    • (1993) J. Biol. Chem. , vol.268 , pp. 803-809
    • Rao, S.I.1    Wilks, A.2    Ortiz De Montellano, P.R.3
  • 11
    • 0028284759 scopus 로고
    • Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates
    • Kelman D. J., DeGray J. A., Mason R. P. Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. J. Biol. Chem. 269:1994;7458-7463.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7458-7463
    • Kelman, D.J.1    Degray, J.A.2    Mason, R.P.3
  • 14
    • 0029028275 scopus 로고
    • Self-peroxidation of metmyoglobin results in the formation of an oxygen-reactive tryptophan-centered radical
    • Gunther M. R., Kelman D. J., Corbett J. T., Mason R. P. Self-peroxidation of metmyoglobin results in the formation of an oxygen-reactive tryptophan-centered radical. J. Biol. Chem. 270:1995;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
  • 15
    • 0024400292 scopus 로고
    • Influence of interior packing and hydrophobicity on the stability of a protein
    • Sandberg W., Terwilliger T. Influence of interior packing and hydrophobicity on the stability of a protein. Science. 245:1989;54-57.
    • (1989) Science , vol.245 , pp. 54-57
    • Sandberg, W.1    Terwilliger, T.2
  • 16
    • 0024473758 scopus 로고
    • Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compund ES
    • Sivaraja M., Goodin D. B., Smith M., Hoffman B. M. Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compund ES. Science. 245:1989;738-740.
    • (1989) Science , vol.245 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 17
    • 0024295374 scopus 로고
    • Trp-191 → Phe, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation
    • Mauro J. M., Fishel L. A., Hazzard J. T., Meyer T. E., Tollin G., Cusanovich M. A., Kraut J. Trp-191 → Phe, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation. Biochemistry. 27:1990;6243-6256.
    • (1990) Biochemistry , vol.27 , pp. 6243-6256
    • Mauro, J.M.1    Fishel, L.A.2    Hazzard, J.T.3    Meyer, T.E.4    Tollin, G.5    Cusanovich, M.A.6    Kraut, J.7
  • 18
    • 0025891116 scopus 로고
    • Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance
    • Fishel L. A., Farnum M. F., Mauro J. M., Miller M. A., Kraut J., Liu Y. J., Tan X. L., Scholes C. P. Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance. Biochemistry. 30:1991;1986-1996.
    • (1991) Biochemistry , vol.30 , pp. 1986-1996
    • Fishel, L.A.1    Farnum, M.F.2    Mauro, J.M.3    Miller, M.A.4    Kraut, J.5    Liu, Y.J.6    Tan, X.L.7    Scholes, C.P.8
  • 19
    • 0025881572 scopus 로고
    • Importance of a conserved hydrogen-bonding network in cytochromes c to their redox potentials and stabilities
    • Caffrey M., Daldal F., Holden H. M., Cusanovich M. A. Importance of a conserved hydrogen-bonding network in cytochromes c to their redox potentials and stabilities. Biochemistry. 30:1991;4119-4125.
    • (1991) Biochemistry , vol.30 , pp. 4119-4125
    • Caffrey, M.1    Daldal, F.2    Holden, H.M.3    Cusanovich, M.A.4
  • 20
    • 0024058721 scopus 로고
    • Protein dynamics and reaction rates: Mode-specific chemistry in large molecules?
    • Bialek W., Onuchic J. N. Protein dynamics and reaction rates: Mode-specific chemistry in large molecules? Proc. Natl. Acad. Sci. USA. 85:1988;5908-5912.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5908-5912
    • Bialek, W.1    Onuchic, J.N.2
  • 21
    • 0014314347 scopus 로고
    • Temperature effects on the formation and reactions of free radicals in gamma-irradiated dry enzymes
    • Stratton K. Temperature effects on the formation and reactions of free radicals in gamma-irradiated dry enzymes. Radiat. Res. 35:1968;182-201.
    • (1968) Radiat. Res. , vol.35 , pp. 182-201
    • Stratton, K.1
  • 22
    • 0011129346 scopus 로고
    • Chemical catalysis
    • San Francisco: W. H. Freeman
    • Fersht A. Chemical catalysis. Enzyme structure and mechanism. 1989;47-97 W. H. Freeman, San Francisco.
    • (1989) Enzyme Structure and Mechanism , pp. 47-97
    • Fersht, A.1
  • 24
    • 0027093430 scopus 로고
    • The interaction of trolox-C, a water-soluble vitamin E analog, with ferrylmyoglobin: Reduction of the oxoferryl moiety
    • Giulivi C., Romero F. J., Cadenas E. The interaction of trolox-C, a water-soluble vitamin E analog, with ferrylmyoglobin: Reduction of the oxoferryl moiety. Arch. Biochem. Biophys. 299:1992;302-312.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 302-312
    • Giulivi, C.1    Romero, F.J.2    Cadenas, E.3
  • 25
    • 0005955494 scopus 로고
    • ESR spin trapping study on the oxidizing species formed in the reaction of the ferrous iron with hydrogen peroxide
    • Yamazaki I., Piette L. H. ESR spin trapping study on the oxidizing species formed in the reaction of the ferrous iron with hydrogen peroxide. J. Am. Chem. Soc. 113:1991;7588-7593.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7588-7593
    • Yamazaki, I.1    Piette, L.H.2
  • 26
    • 0025785533 scopus 로고
    • Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase
    • Osawa Y., Korzekwa K. Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase. Proc. Natl. Acad. Sci. USA. 88:1991;7081-7085.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7081-7085
    • Osawa, Y.1    Korzekwa, K.2
  • 27
    • 0027275824 scopus 로고
    • Inhibition of the protein radical reactions of ferrylmyoglobin by the water-soluble analog of vitamin E, trolox C
    • Giulivi C., Cadenas E. Inhibition of the protein radical reactions of ferrylmyoglobin by the water-soluble analog of vitamin E, trolox C. Arch. Biochem. Biophys. 303:1993;152-158.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 152-158
    • Giulivi, C.1    Cadenas, E.2
  • 28
    • 77956897161 scopus 로고
    • Cytochrome c peroxidase
    • Boyer P.D. Orlando, FL: Academic Press
    • Yonetani T. Cytochrome c peroxidase. Boyer P. D. The enzymes. 13:1976;345-361 Academic Press, Orlando, FL.
    • (1976) The Enzymes , vol.13 , pp. 345-361
    • Yonetani, T.1
  • 29
    • 0026063955 scopus 로고
    • Identification of a globin free radical in equine myoglobin treated with peroxides
    • Davies M. J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta. 1077:1991;86-90.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 86-90
    • Davies, M.J.1
  • 30
    • 0027366718 scopus 로고
    • Detection and reaction of the globin radical in hemoglobin
    • McArthur K. M., Davies M. J. Detection and reaction of the globin radical in hemoglobin. Biochim. Biophys. Acta. 1202:1993;173-181.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 173-181
    • McArthur, K.M.1    Davies, M.J.2
  • 31
    • 0020025575 scopus 로고
    • Structure of the tyrosyl radical in bacteriophage T4-induced ribonucleotide reductase
    • Sahlin M., Gräsland A., Ehrenberg A., Sjöberg B. M. Structure of the tyrosyl radical in bacteriophage T4-induced ribonucleotide reductase. J. Biol. Chem. 257:1982;366-372.
    • (1982) J. Biol. Chem. , vol.257 , pp. 366-372
    • Sahlin, M.1    Gräsland, A.2    Ehrenberg, A.3    Sjöberg, B.M.4
  • 32
    • 0024788454 scopus 로고
    • Electron spin resonance spectrum of Tyr-151 free-radical formed in reactions of sperm whale metmyoglobin with ethyl hydroperoxide and potassium irridate
    • Miki H., Harada K., Yamazaki I., Tamura M., Watanabe H. Electron spin resonance spectrum of Tyr-151 free-radical formed in reactions of sperm whale metmyoglobin with ethyl hydroperoxide and potassium irridate. Arch. Biochem. Biophys. 275:1989;354-362.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 354-362
    • Miki, H.1    Harada, K.2    Yamazaki, I.3    Tamura, M.4    Watanabe, H.5
  • 33
    • 0016616098 scopus 로고
    • Electron spin resonance study on peroxidase- And oxidase-reactions of horseradish peroxidase and methemoglobin
    • Shiga T., Imaizumi K. Electron spin resonance study on peroxidase- and oxidase-reactions of horseradish peroxidase and methemoglobin. Arch. Biochem. Biophys. 167:1975;469-479.
    • (1975) Arch. Biochem. Biophys. , vol.167 , pp. 469-479
    • Shiga, T.1    Imaizumi, K.2
  • 34
    • 0000743530 scopus 로고
    • A possible structure for the higher oxidation state of metmyoglobin. 55
    • George P., Irvine D. H. A possible structure for the higher oxidation state of metmyoglobin. 55. Biochem. J. 60:1955;596-604.
    • (1955) Biochem. J. , vol.60 , pp. 596-604
    • George, P.1    Irvine, D.H.2
  • 35
    • 0017407172 scopus 로고
    • Evaluation of the horseradish peroxidase-scopoletin method for the measurements of hydrogen peroxide formation in biological systems
    • Boveris A., Martino E., Stoppani A. O. M. Evaluation of the horseradish peroxidase-scopoletin method for the measurements of hydrogen peroxide formation in biological systems. Anal. Biochem. 80:1977;145-158.
    • (1977) Anal. Biochem. , vol.80 , pp. 145-158
    • Boveris, A.1    Martino, E.2    Stoppani, A.O.M.3
  • 37
    • 0022273861 scopus 로고
    • Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface
    • Ortiz de Montellano P. R., Catalano C. E. Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface. J. Biol. Chem. 260:1985;9265-9271.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9265-9271
    • Ortiz De Montellano, P.R.1    Catalano, C.E.2
  • 38
    • 0027414020 scopus 로고
    • Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome
    • Giulivi C., Davies K. J. A. Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome. J. Biol. Chem. 268:1993;8752-8759.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8752-8759
    • Giulivi, C.1    Davies, K.J.A.2
  • 39
    • 0025201423 scopus 로고
    • A novel antioxidant role for hemoglobin
    • Giulivi C., Davies K. J. A. A novel antioxidant role for hemoglobin. J. Biol. Chem. 265:1990;19453-19460.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19453-19460
    • Giulivi, C.1    Davies, K.J.A.2
  • 40
    • 0000110144 scopus 로고
    • Free-radical combination reactions involving phenoxyl radicals
    • Jonsson M., Lind J., Reitbergen T., Eriksen T. E. Free-radical combination reactions involving phenoxyl radicals. J. Phys. Chem. 97:1993;11278-11282.
    • (1993) J. Phys. Chem. , vol.97 , pp. 11278-11282
    • Jonsson, M.1    Lind, J.2    Reitbergen, T.3    Eriksen, T.E.4
  • 41
    • 0022297759 scopus 로고
    • Energetics of interconversion reactions of oxyradicals
    • Koppenol W. H., Butler J. Energetics of interconversion reactions of oxyradicals. Adv. Free Radic. Biol. Med. 1:1985;91-131.
    • (1985) Adv. Free Radic. Biol. Med. , vol.1 , pp. 91-131
    • Koppenol, W.H.1    Butler, J.2
  • 42
    • 0022552272 scopus 로고
    • X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes
    • Chance M., Powers L., Kumar C., Chance B. X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes. Biochemistry. 25:1986;1259-1265.
    • (1986) Biochemistry , vol.25 , pp. 1259-1265
    • Chance, M.1    Powers, L.2    Kumar, C.3    Chance, B.4
  • 43
    • 0001250805 scopus 로고
    • Influence of nitrogen base ligation and hydrogen bonding on the rate constants for oxygen transferfrom percarboxylic acids and alkyl hydroperoxides to (meso-tetraphenylporphinato)manganese (III) chloride
    • Yuan L-C., Bruice T. C. Influence of nitrogen base ligation and hydrogen bonding on the rate constants for oxygen transferfrom percarboxylic acids and alkyl hydroperoxides to (meso-tetraphenylporphinato)manganese (III) chloride. J. Am. Chem. Soc. 108:1986;1643-1650.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1643-1650
    • Yuan, L-C.1    Bruice, T.C.2
  • 44
    • 0024595597 scopus 로고
    • Oxidation of dimethylsulphoxide to formaldehyde by oxyhaemoglobin and oxyleghaemoglobin in the presence of hydrogen peroxide is not mediated by "free" hydroxyl radicals
    • Puppo A., Halliwell B. Oxidation of dimethylsulphoxide to formaldehyde by oxyhaemoglobin and oxyleghaemoglobin in the presence of hydrogen peroxide is not mediated by "free" hydroxyl radicals. Free Radic. Res. Communn. 5:1989;277-281.
    • (1989) Free Radic. Res. Communn. , vol.5 , pp. 277-281
    • Puppo, A.1    Halliwell, B.2
  • 45
    • 0023693165 scopus 로고
    • The generation of ferryl or hydroxyl radicals during interaction of hemoproteins with hydrogen peroxide
    • Harel S., Kanner J. The generation of ferryl or hydroxyl radicals during interaction of hemoproteins with hydrogen peroxide. Free Radic. Res. Commun. 5:1988;21-33.
    • (1988) Free Radic. Res. Commun. , vol.5 , pp. 21-33
    • Harel, S.1    Kanner, J.2
  • 46
    • 0023897833 scopus 로고
    • Formation of hydroxyl radicals in biological systems. Does myoglobin stimulate hydroxyl radical formation from hydrogen peroxide?
    • Puppo A., Halliwell B. Formation of hydroxyl radicals in biological systems. Does myoglobin stimulate hydroxyl radical formation from hydrogen peroxide? Free Radic. Res. Commun. 4:1988;415-422.
    • (1988) Free Radic. Res. Commun. , vol.4 , pp. 415-422
    • Puppo, A.1    Halliwell, B.2
  • 47
    • 0344541032 scopus 로고
    • Autooxidation of L-ascorbic acid and imidazole nucleus. II. The decomposition products of imidazole derivatives
    • Imanaga Y. Autooxidation of L-ascorbic acid and imidazole nucleus. II. The decomposition products of imidazole derivatives. J. Biochem. (Tokyo). 42:1955;669-676.
    • (1955) J. Biochem. (Tokyo) , vol.42 , pp. 669-676
    • Imanaga, Y.1
  • 48
    • 37049062411 scopus 로고
    • Photolysis of L-histidine
    • Johns R. B., Jaskewycz T. Photolysis of L-histidine. Nature. 206:1965;1149.
    • (1965) Nature , vol.206 , pp. 1149
    • Johns, R.B.1    Jaskewycz, T.2
  • 49
    • 0014640056 scopus 로고
    • Sensitized photooxidation of histidine and its derivatives. products and mechanism of the reaction
    • Tomita M., Irie M., Ukita T. Sensitized photooxidation of histidine and its derivatives. products and mechanism of the reaction. Biochemistry. 8:1969;5149-5160.
    • (1969) Biochemistry , vol.8 , pp. 5149-5160
    • Tomita, M.1    Irie, M.2    Ukita, T.3
  • 50
    • 0025095792 scopus 로고
    • Site-specific oxidation of angiotensin I by copper (II) and L-ascorbate: Conversion of histidine residues to 2-imidazolones
    • Uchida K., Kawakishi S. Site-specific oxidation of angiotensin I by copper (II) and L-ascorbate: Conversion of histidine residues to 2-imidazolones. Arch. Biochem. Biophys. 283:1990;20-26.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 20-26
    • Uchida, K.1    Kawakishi, S.2
  • 51
    • 0021701864 scopus 로고
    • The repair of oxidized amino acids by antioxidants
    • Hoey B. M., Butler J. The repair of oxidized amino acids by antioxidants. Biochim. Biophys. Acta. 791:1984;212-218.
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 212-218
    • Hoey, B.M.1    Butler, J.2
  • 52
    • 0344265271 scopus 로고
    • Reduction potential determination of some biochemically important free radicals: Pulse-radiolysis and electrochemical methods
    • Faraggi M., Klapper M. H. Reduction potential determination of some biochemically important free radicals: Pulse-radiolysis and electrochemical methods. J. Chim. Phys. Phys.-Chim. Biol. 90:1993;711-744.
    • (1993) J. Chim. Phys. Phys.-Chim. Biol. , vol.90 , pp. 711-744
    • Faraggi, M.1    Klapper, M.H.2
  • 54
    • 0019891910 scopus 로고
    • Ultraviolet difference spectroscopy of myoglobin: Assignment of pK values of tyrosyl phenolic groups and the stability of the ferryl derivatives
    • Uyeda M., Peisach J. Ultraviolet difference spectroscopy of myoglobin: Assignment of pK values of tyrosyl phenolic groups and the stability of the ferryl derivatives. Biochemistry. 20:1981;2028-2035.
    • (1981) Biochemistry , vol.20 , pp. 2028-2035
    • Uyeda, M.1    Peisach, J.2
  • 55
    • 0028245961 scopus 로고
    • Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin
    • Giulivi C., Pacifici R. E., Davies K. J. A. Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin. Arch. Biochem. Biophys. 311:1994;329-341.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 329-341
    • Giulivi, C.1    Pacifici, R.E.2    Davies, K.J.A.3
  • 56
    • 0344972024 scopus 로고    scopus 로고
    • Giulivi C.; Davies, K. J. A., unpublished results
    • Giulivi, C.; Davies, K. J. A., unpublished results.
  • 57
    • 0028033328 scopus 로고
    • Characterization of the tyrosyl radicals in ovine prostaglandin-H synthase-1 by Isotope replacement and site-directed mutagenesis
    • Tsai A., Hsi L., Kulmacz R. J., Palmer G., Smith W. L. Characterization of the tyrosyl radicals in ovine prostaglandin-H synthase-1 by Isotope replacement and site-directed mutagenesis. J. Biol. Chem. 269:1994;5085-5091.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5085-5091
    • Tsai, A.1    Hsi, L.2    Kulmacz, R.J.3    Palmer, G.4    Smith, W.L.5
  • 60
    • 0024378007 scopus 로고
    • Protein-radical involvement in bological catalysis?
    • Stubbe J. A. Protein-radical involvement in bological catalysis? Annu. Rev. Biochem. 58:1989;257-285.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 257-285
    • Stubbe, J.A.1
  • 61
    • 0029294618 scopus 로고
    • A Radical approach to enzyme catalysis
    • Marsh E. N. A Radical approach to enzyme catalysis. Bioessays. 17:1995;431-441.
    • (1995) Bioessays , vol.17 , pp. 431-441
    • Marsh, E.N.1


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