메뉴 건너뛰기




Volumn 60, Issue 1, 2008, Pages 41-56

Protein self-modification by heme-generated reactive species

Author keywords

Crosslinking reactions; Heme generated reactive species; Hemoglobin; Myoglobin; Neuroglobin; Oxidation reactions; Protein self modification

Indexed keywords

CATECHOL; CYSTINE; FLUOROQUINONE; GLOBIN; HEMOGLOBIN; HEMOPROTEIN; HISTIDINE; HYDROGEN PEROXIDE; MYOGLOBIN; NEUROGLOBIN; QUINONE DERIVATIVE; REACTIVE NITROGEN SPECIES; UNCLASSIFIED DRUG; 4 FLUOROCATECHOL; 4-FLUOROCATECHOL; CATECHOL DERIVATIVE; DOPAMINE; NERVE PROTEIN; NITRITE; NITROGEN DIOXIDE;

EID: 42949126008     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.10     Document Type: Review
Times cited : (9)

References (117)
  • 3
    • 0000805517 scopus 로고
    • On the function and mechanism of action of peroxidise
    • Dunford, H. B., and Stillmann, J. S. (1976) On the function and mechanism of action of peroxidise. Coord. Chem. Rev. 19, 187-251.
    • (1976) Coord. Chem. Rev. , vol.19 , pp. 187-251
    • Dunford, H.B.1    Stillmann, J.S.2
  • 4
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada, S., Palmer, R. M. J., and Higgs, E. A. (1991) Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 6
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller, S., and Babcock, G. T. (1996) Heme/copper terminal oxidases. Chem. Rev. 96, 2889-2907.
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 8
    • 0000170196 scopus 로고
    • Everse, J., Everse, K. E., and Grisham, M. B., eds. CRC Press, Boca Raton, FL
    • Bosshard, H. R., Anni, H., and Yonetani, T. (1991) In Peroxidases in Chemistry and Biology, Vol. 2 (Everse, J., Everse, K. E., and Grisham, M. B., eds.). p. 51, CRC Press, Boca Raton, FL.
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 51
    • Bosshard, H.R.1    Anni, H.2    Yonetani, T.3
  • 10
    • 18944387200 scopus 로고    scopus 로고
    • The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding
    • DOI 10.1002/cbic.200400291
    • Worrall, J. A. R., Diederix, R. E. M., Prudèncio, M., Lowe, C. E., Ciofi-Baffoni, S., Ubbink, M., and Canters, G. W. (2005) The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding. ChemBioChem 6, 747-758. (Pubitemid 40873779)
    • (2005) ChemBioChem , vol.6 , Issue.4 , pp. 747-758
    • Worrall, J.A.R.1    Diederix, R.E.M.2    Prudencio, M.3    Lowe, C.E.4    Ciofi-Baffoni, S.5    Ubbink, M.6    Canters, G.W.7
  • 11
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c-type cytochromes
    • DOI 10.1021/bi0260841
    • Diederix, R. E. M., Ubbink, M., and Canters, G. W. (2002) Peroxidase activity as a tool for studying the folding of c-type cytochromes. Biochemistry 41, 13067-13077. (Pubitemid 35215792)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 13067-13077
    • Diederix, R.E.M.1    Ubbink, M.2    Canters, G.W.3
  • 12
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c-oxidase and myoglobin
    • Brunori, M. (2001) Nitric oxide, cytochrome-c-oxidase and myoglobin. Trends Biochem. Sci. 26, 21-23.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 21-23
    • Brunori, M.1
  • 13
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • Brunori, M. (2001) Nitric oxide moves myoglobin centre stage. Trends Biochem. Sci. 26, 209-210.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 209-210
    • Brunori, M.1
  • 14
    • 0033046163 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin
    • Herold, S. (1999) Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin. FEBS Lett. 443, 81-84.
    • (1999) FEBS Lett. , vol.443 , pp. 81-84
    • Herold, S.1
  • 15
    • 0035916922 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the NO-mediated oxidation of oxymyoglobin and oxyhemoglobin
    • DOI 10.1021/bi002407m
    • Herold, S., Exner, M., and Nauser, T. (2001) Kinetic and mechanistic studies of the NO-mediated oxidation of oxymyoglobin and oxyhemoglobin. Biochemistry 40, 3385-3395. (Pubitemid 32221642)
    • (2001) Biochemistry , vol.40 , Issue.11 , pp. 3385-3395
    • Herold, S.1    Exner, M.2    Nauser, T.3
  • 17
    • 0036525946 scopus 로고    scopus 로고
    • Nitric oxide and myoglobins
    • Møller, J. K., and Skibsted, L. J. (2002) Nitric oxide and myoglobins. Chem. Rev. 102, 1167-1178.
    • (2002) Chem. Rev. , vol.102 , pp. 1167-1178
    • Møller, J.K.1    Skibsted, L.J.2
  • 18
    • 0037470250 scopus 로고    scopus 로고
    • Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide. Mechanistic studies of the S-nitrosothiol formation under different mixing conditions
    • Herold, S., and Röck, G. (2003) Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide. Mechanistic studies of the S-nitrosothiol formation under different mixing conditions. J. Biol. Chem. 278, 6623-6634.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6623-6634
    • Herold, S.1    Röck, G.2
  • 19
    • 0035830832 scopus 로고    scopus 로고
    • Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (S) nitrosation dependence on the absence or presence of oxygen
    • Witting, P. K., Douglas, D. J., and Mauk, A. G. (2001) Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (S) nitrosation dependence on the absence or presence of oxygen. J. Biol. Chem. 276, 3991-3998.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3991-3998
    • Witting, P.K.1    Douglas, D.J.2    Mauk, A.G.3
  • 20
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • DOI 10.1038/380221a0
    • Jia, L., Bonaventura, C., Bonaventura, C., and Stamler, J. S. (1996) S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380, 221-226. (Pubitemid 26090643)
    • (1996) Nature , vol.380 , Issue.6571 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 21
    • 1642588213 scopus 로고    scopus 로고
    • S-Nitrosohemoglobin: A biochemical perspective
    • Zhuang, Y., and Hogg, N. (2004) S-Nitrosohemoglobin: A biochemical perspective. Free Radic. Biol. Med. 36, 947-958.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 947-958
    • Zhuang, Y.1    Hogg, N.2
  • 22
    • 1242293624 scopus 로고    scopus 로고
    • Nitrotyrosine, dityrosine and nitrotryptophan formation from metmyoglobin, hydrogen peroxide and nitrite
    • Herold, S. (2004) Nitrotyrosine, dityrosine and nitrotryptophan formation from metmyoglobin, hydrogen peroxide and nitrite. Free Radic. Biol. Med. 36, 565-579.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 565-579
    • Herold, S.1
  • 23
    • 2442450674 scopus 로고    scopus 로고
    • Myoglobin catalyzed exogenous and endogenous tyrosine nitration by nitrite and hydrogen peroxide
    • Nicolis, S., Monzani, E., Roncone, R., Gianelli, L., and Casella, L. (2004) Myoglobin catalyzed exogenous and endogenous tyrosine nitration by nitrite and hydrogen peroxide. Chem. Eur. J. 10, 2281-2290.
    • (2004) Chem. Eur. J. , vol.10 , pp. 2281-2290
    • Nicolis, S.1    Monzani, E.2    Roncone, R.3    Gianelli, L.4    Casella, L.5
  • 26
    • 4143091664 scopus 로고    scopus 로고
    • Nitrite increases the enantioselectivity of sulfoxidation catalyzed by myoglobin derivatives in the presence of hydrogen peroxide
    • DOI 10.1016/j.tet.2004.06.097, PII S0040402004010154
    • Pironti, V., Nicolis, S., Monzani, E., Colonna, S., and Casella, L. (2004) Nitrite increases the enantioselectivity of sulfoxidation catalyzed by myoglobin derivatives in the presence of hydrogen peroxide. Tetrahedron 60, 8153-8160. (Pubitemid 39094331)
    • (2004) Tetrahedron , vol.60 , Issue.37 , pp. 8153-8160
    • Pironti, V.1    Nicolis, S.2    Monzani, E.3    Colonna, S.4    Casella, L.5
  • 27
    • 0033556669 scopus 로고    scopus 로고
    • Asymmetric oxidation catalyzed by myoglobin mutants
    • DOI 10.1016/S0957-4166(98)00498-4, PII S0957416698004984
    • Ozaki, S.-I., Yang, H., Matsui, T., Goto, Y., and Watanabe, Y. (1999) Asymmetric oxidation catalyzed by myoglobin mutants. Tetrahedron: Asymm. 10, 183-192. (Pubitemid 29089218)
    • (1999) Tetrahedron Asymmetry , vol.10 , Issue.1 , pp. 183-192
    • Ozaki, S.-I.1    Yang, H.-J.2    Matsui, T.3    Goto, Y.4    Watanabe, Y.5
  • 28
    • 0030001545 scopus 로고    scopus 로고
    • Conversion of myoglobin into a highly stereospecific peroxygenase by the L29H/H64L mutation
    • Ozaki, S., Matsui, T., and Watanabe, Y. (1996) Conversion of myoglobin into a highly stereospecific peroxygenase by the L29H/H64L mutation. J. Am. Chem. Soc. 118, 9784-9785.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9784-9785
    • Ozaki, S.1    Matsui, T.2    Watanabe, Y.3
  • 29
    • 0030839466 scopus 로고    scopus 로고
    • Conversion of myoglobin into a peroxygenase: A catalytic intermediate of sulfoxidation and epoxidation by the F43H/H64L mutant
    • Ozaki, S., Matsui, T., and Watanabe, Y. (1997) Conversion of myoglobin into a peroxygenase: a catalytic intermediate of sulfoxidation and epoxidation by the F43H/H64L mutant. J. Am. Chem. Soc. 119, 6666-6667.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6666-6667
    • Ozaki, S.1    Matsui, T.2    Watanabe, Y.3
  • 30
    • 0037166981 scopus 로고    scopus 로고
    • Asymmetric sulfoxidation and amine binding by H64D/V68A and H64D/V68S Mb: Mechanistic insight into the chiral discrimination step
    • Kato, S., Yang, H., Ueno, T., Ozaki, S., Philips, G. N., Fukuzumi, S. M., and Watanabe, Y. (2002) Asymmetric sulfoxidation and amine binding by H64D/V68A and H64D/V68S Mb: mechanistic insight into the chiral discrimination step. J. Am. Chem. Soc. 124, 8506-8507.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8506-8507
    • Kato, S.1    Yang, H.2    Ueno, T.3    Ozaki, S.4    Philips, G.N.5    Fukuzumi, S.M.6    Watanabe, Y.7
  • 31
    • 0035844279 scopus 로고    scopus 로고
    • 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical
    • 2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical. J. Biol. Chem. 276, 16540-16547.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16540-16547
    • Witting, P.K.1    Mauk, A.G.2
  • 32
    • 0034816211 scopus 로고    scopus 로고
    • Reaction of human myoglobin and peroxynitrite: Characterising biomarkers for myoglobin-derived oxidative stress
    • Witting, P. K., Mauk, A. G., Douglas, D. J., and Stoker, R. (2001) Reaction of human myoglobin and peroxynitrite: characterising biomarkers for myoglobin-derived oxidative stress. Biochem. Biophys. Res. Commun. 286, 352-356.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 352-356
    • Witting, P.K.1    Mauk, A.G.2    Douglas, D.J.3    Stoker, R.4
  • 33
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos, H. (1998) Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch. Biochem. Biophys. 356, 1-11.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 35
    • 0037371492 scopus 로고    scopus 로고
    • Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin
    • Herold, S., and Rehmann, F.-J. K. (2003) Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin. Free Radic. Biol. Med. 34, 531-545.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 531-545
    • Herold, S.1    Rehmann, F.-J.K.2
  • 36
    • 1542314758 scopus 로고    scopus 로고
    • Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide
    • Monzani, E., Roncone, R., Casella, L., Galliano, M., and Koppenol, W. H. (2004) Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide. Eur. J. Biochem. 271, 895-906.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 895-906
    • Monzani, E.1    Roncone, R.2    Casella, L.3    Galliano, M.4    Koppenol, W.H.5
  • 38
    • 0034839839 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin
    • Herold, S., and Rehmann, F.-J. K. (2001) Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin. J. Biol. Inorg. Chem. 6, 543-555.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 543-555
    • Herold, S.1    Rehmann, F.-J.K.2
  • 39
    • 0036801298 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species at biological heme centers: A potential mechanism of nitric oxide-dependent toxicity
    • Casella, L., Monzani, E., Roncone, R., Nicolis, S., Sala, A., and De Riso, A. (2002) Formation of reactive nitrogen species at biological heme centers: a potential mechanism of nitric oxide-dependent toxicity. Environ. Health Perspect. 110, 709-711.
    • (2002) Environ. Health Perspect. , vol.110 , pp. 709-711
    • Casella, L.1    Monzani, E.2    Roncone, R.3    Nicolis, S.4    Sala, A.5    De Riso, A.6
  • 40
    • 33646923430 scopus 로고    scopus 로고
    • Reactive nitrogen species of physiological relevance: Mechanism of formation and biological targets
    • Roncone, R., Barbieri, M., Monzani, E., and Casella, L. (2006) Reactive nitrogen species of physiological relevance: mechanism of formation and biological targets. Coord. Chem. Rev. 250, 1286-1293.
    • (2006) Coord. Chem. Rev. , vol.250 , pp. 1286-1293
    • Roncone, R.1    Barbieri, M.2    Monzani, E.3    Casella, L.4
  • 41
    • 0033559008 scopus 로고    scopus 로고
    • Cytotoxic and genotoxic potential of dopamine
    • Stokes, A. H., Hastings, T. G., and Vrana, K. E. (1999) Cytotoxic and genotoxic potential of dopamine. J. Neurosci. Res. 55, 659-665.
    • (1999) J. Neurosci. Res. , vol.55 , pp. 659-665
    • Stokes, A.H.1    Hastings, T.G.2    Vrana, K.E.3
  • 42
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the a-synuclein protofibril by a dopamine-α-synuclein adduct
    • Conway, K. A., Rochet, J.-C., Bieganski, R. M., and Lansbury, P. T. Jr. (2001) Kinetic stabilization of the a-synuclein protofibril by a dopamine-α-synuclein adduct. Science 294, 1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.-C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 43
    • 0035112815 scopus 로고    scopus 로고
    • Reaction of oxidized dopamine with endogenous cysteine residues in the human dopamine transporter
    • Whitehead, R. E., Ferrer, J. V., Javitch, J. A., and Justice, J. B. (2001) Reaction of oxidized dopamine with endogenous cysteine residues in the human dopamine transporter. J. Neurochem. 76, 1242-1251.
    • (2001) J. Neurochem. , vol.76 , pp. 1242-1251
    • Whitehead, R.E.1    Ferrer, J.V.2    Javitch, J.A.3    Justice, J.B.4
  • 44
    • 0032403510 scopus 로고    scopus 로고
    • Dopamine, in the presence of tyrosinase, covalently modifies and inactivates tyrosine hydroxylase
    • Xu, Y., Stokes, A. H., Roskoski, R., Jr., and Vrana, K. E. (1998) Dopamine, in the presence of tyrosinase, covalently modifies and inactivates tyrosine hydroxylase. J. Neurosci. Res. 54, 691-697.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 691-697
    • Xu, Y.1    Stokes, A.H.2    Roskoski Jr., R.3    Vrana, K.E.4
  • 46
    • 0033558324 scopus 로고    scopus 로고
    • Dopamine quinone formation and protein modification associated with the striatal neurotoxicity of methamphetamine: Evidence against a role for extracellular dopamine
    • LaVoie, M. J., and Hastings, T. G. (1999) Dopamine quinone formation and protein modification associated with the striatal neurotoxicity of methamphetamine: Evidence against a role for extracellular dopamine. J. Neurosci. 19, 1484-1491.
    • (1999) J. Neurosci. , vol.19 , pp. 1484-1491
    • LaVoie, M.J.1    Hastings, T.G.2
  • 47
    • 0029933450 scopus 로고    scopus 로고
    • Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections
    • Hastings, T. G., Lewis, D. A., and Zigmond, M. J. (1996) Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections. Proc. Natl. Acad. Sci. USA 93, 1956-1961.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1956-1961
    • Hastings, T.G.1    Lewis, D.A.2    Zigmond, M.J.3
  • 48
    • 0032842040 scopus 로고    scopus 로고
    • Tyrosine hydroxylase is inactivated by catechol-quinones and converted to a redox-cycling quinoprotein: Possible relevance to Parkinson's disease
    • Kuhn, D. M., Arthur, R.E., Jr., Thomas, D. M., and Elferink, L. A. (1999) Tyrosine hydroxylase is inactivated by catechol-quinones and converted to a redox-cycling quinoprotein: possible relevance to Parkinson's disease. J. Neurochem. 73, 1309-1317.
    • (1999) J. Neurochem. , vol.73 , pp. 1309-1317
    • Kuhn, D.M.1    Arthur Jr., R.E.2    Thomas, D.M.3    Elferink, L.A.4
  • 49
    • 0032531095 scopus 로고    scopus 로고
    • Dopamine inactivates tryptophan hydroxylase and forms a redox-cycling quinoprotein: Possible endogenous toxin to serotonin neurons
    • Kuhn, D. M., and Arthur, R. Jr. (1998) Dopamine inactivates tryptophan hydroxylase and forms a redox-cycling quinoprotein: possible endogenous toxin to serotonin neurons. J. Neurosci. 18, 7111-7117.
    • (1998) J. Neurosci. , vol.18 , pp. 7111-7117
    • Kuhn, D.M.1    Arthur Jr., R.2
  • 50
    • 0030857351 scopus 로고    scopus 로고
    • Inhibition of glutamate transport in synaptosomes by dopamine oxidation and reactive oxygen species
    • Berman, S. B., and Hastings, T. G. (1997) Inhibition of glutamate transport in synaptosomes by dopamine oxidation and reactive oxygen species. J. Neurochem. 69, 1185-1195. (Pubitemid 27364840)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.3 , pp. 1185-1195
    • Berman, S.B.1    Hastings, T.G.2
  • 51
    • 0030056223 scopus 로고    scopus 로고
    • J Modification of dopamine transporter function: Effect of reactive oxygen species and dopamine
    • Berman, S. B., Zigmond, M. J., and Hastings, T. G. (1996) J Modification of dopamine transporter function: Effect of reactive oxygen species and dopamine. J. Neurochem. 67, 593-600.
    • (1996) J. Neurochem. , vol.67 , pp. 593-600
    • Berman, S.B.1    Zigmond, M.J.2    Hastings, T.G.3
  • 52
    • 0028362178 scopus 로고
    • Human exposure to oxides of nitrogen at ambient and supra-ambient concentrations
    • Mohsenin, V. (1994) Human exposure to oxides of nitrogen at ambient and supra-ambient concentrations. Toxicology 89, 301-312.
    • (1994) Toxicology , vol.89 , pp. 301-312
    • Mohsenin, V.1
  • 53
    • 0000741366 scopus 로고    scopus 로고
    • Feelisch, M., and Stamler, J. S., eds. Wiley, Chichester, NY
    • Stamler, J. S., and Feelisch, M. (1996) In Methods in Nitric Oxide Research (Feelisch, M., and Stamler, J. S., eds.). p. 19, Wiley, Chichester, NY.
    • (1996) Methods in Nitric Oxide Research , pp. 19
    • Stamler, J.S.1    Feelisch, M.2
  • 54
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman, J. S., and Koppenol, W. H. (1996) Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly. Am. J. Physiol. 271, C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 55
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. the prototypic redox-based signaling mechanism
    • Stamler, J. S., Lamas, S., and Fang, F. C. (2001) Nitrosylation. The prototypic redox-based signaling mechanism. Cell 106, 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 56
    • 0002880196 scopus 로고    scopus 로고
    • Feelisch, M., and Stamler, J. S., eds. Wiley, Chichester
    • Kelm, M., and Yoshida, K. (1996) In Methods in Nitric Oxide Research (Feelisch, M., and Stamler, J. S., eds.). p. 47-58, Wiley, Chichester.
    • (1996) Methods in Nitric Oxide Research , pp. 47-58
    • Kelm, M.1    Yoshida, K.2
  • 58
    • 0028827694 scopus 로고
    • Condensed expirate nitrite as a home marker for acute asthma
    • Hunt, J., Byrns, R. E., Ignarro, L. J., and Gaston, B. (1995) Condensed expirate nitrite as a home marker for acute asthma. Lancet 346, 1235-1236.
    • (1995) Lancet , vol.346 , pp. 1235-1236
    • Hunt, J.1    Byrns, R.E.2    Ignarro, L.J.3    Gaston, B.4
  • 59
    • 0029760021 scopus 로고    scopus 로고
    • Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. a novel mechanism for nitric oxide-mediated protein modification
    • Eiserich, J. P., Cross, C. E., Jones, A. D., Halliwell, B., and van der Vliet, A. (1996) Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification. J. Biol. Chem. 271, 19199-19208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19199-19208
    • Eiserich, J.P.1    Cross, C.E.2    Jones, A.D.3    Halliwell, B.4    Van Der Vliet, A.5
  • 60
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. a potential additional mechanism of nitric oxide-dependent toxicity
    • van der Vliet, A., Eiserich, J. P., Halliwell, B., and Cross, C. E. (1997) Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J. Biol. Chem. 272, 7617-7625.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7617-7625
    • Van Der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 61
    • 0032529412 scopus 로고    scopus 로고
    • Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide
    • Sampson, J. B., Ye, Y. Z., Rosen, H., and Beckman, J. S. (1998) Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide. Arch. Biochem. Biophys. 356, 207-213.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 207-213
    • Sampson, J.B.1    Ye, Y.Z.2    Rosen, H.3    Beckman, J.S.4
  • 62
    • 0032556905 scopus 로고    scopus 로고
    • Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
    • DOI 10.1038/34923
    • Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., and van der Vliet, A. (1998) Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils. Nature 391, 393-397. (Pubitemid 28093514)
    • (1998) Nature , vol.391 , Issue.6665 , pp. 393-397
    • Eiserich, J.P.1    Hristova, M.2    Cross, C.E.3    Jones, A.D.4    Freeman, B.A.5    Halliwell, B.6    Van Der Vliet, A.7
  • 63
    • 0029074616 scopus 로고
    • Degradation of chlorophyll by nitrogen dioxide generated from nitrite by the peroxidase reaction
    • Shibata, H., Kono, Y., Yamashita, S., Sawa, Y., Ochiai, H., and Tanaka, K. (1995) Degradation of chlorophyll by nitrogen dioxide generated from nitrite by the peroxidase reaction. Biochim. Biophys. Acta 1230, 45-50.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 45-50
    • Shibata, H.1    Kono, Y.2    Yamashita, S.3    Sawa, Y.4    Ochiai, H.5    Tanaka, K.6
  • 64
    • 0035883152 scopus 로고    scopus 로고
    • 15N chemically induced dynamic nuclear polarization during reaction of N-acetyl-L-tyrosine with the nitrating systems nitrite/hydrogen peroxide/horseradish peroxidase and nitrite/hypochloric acid
    • Lehnig, M. (2001) 15N chemically induced dynamic nuclear polarization during reaction of N-acetyl-L-tyrosine with the nitrating systems nitrite/hydrogen peroxide/horseradish peroxidase and nitrite/hypochloric acid. Arch. Biochem. Biophys. 393, 245-254.
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 245-254
    • Lehnig, M.1
  • 65
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: Defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan, M. L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M. T., Lusis, A. J., Lee, J. J., Lee, N. A., Abu-Soud, H. M., Ischiropoulos, H., and Hazen, S. L. (2002) A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J. Biol. Chem. 277, 17415-17427.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3    Shen, Z.4    Song, W.5    Frost, H.6    Vadseth, C.7    Narine, L.8    Lenkiewicz, E.9    Borchers, M.T.10    Lusis, A.J.11    Lee, J.J.12    Lee, N.A.13    Abu-Soud, H.M.14    Ischiropoulos, H.15    Hazen, S.L.16
  • 66
    • 0001057452 scopus 로고
    • Degradation of environmental pollutants by microorganisms and their metalloenzymes
    • Anni, H., and Yonetani, T. (1992) Degradation of environmental pollutants by microorganisms and their metalloenzymes. Met. Ions Biol. Syst. 28, 219-241.
    • (1992) Met. Ions Biol. Syst. , vol.28 , pp. 219-241
    • Anni, H.1    Yonetani, T.2
  • 69
    • 0028035106 scopus 로고
    • The high-output nitric oxide pathway: Role and regulation
    • Xie, Q. W., and Nathan, C. (1994) The high-output nitric oxide pathway: role and regulation. J. Leukocyte Biol. 56, 576-582. (Pubitemid 24348815)
    • (1994) Journal of Leukocyte Biology , vol.56 , Issue.5 , pp. 576-582
    • Xie, Q.-W.1    Nathan, C.2
  • 70
    • 0030915094 scopus 로고    scopus 로고
    • Increased production of the potent oxidant peroxynitrite in the lungs of patients with idiopathic pulmonary fibrosis
    • Saleh, D., Barnes, P. J., and Giaid, A. (1997) Increased production of the potent oxidant peroxynitrite in the lungs of patients with idiopathic pulmonary fibrosis. Am. J. Respir. Crit. Care Med. 155, 1763-1769.
    • (1997) Am. J. Respir. Crit. Care Med. , vol.155 , pp. 1763-1769
    • Saleh, D.1    Barnes, P.J.2    Giaid, A.3
  • 71
    • 0031567576 scopus 로고    scopus 로고
    • What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo?
    • Halliwell, B. (1997) What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo?. FEBS Lett. 411, 157-160.
    • (1997) FEBS Lett. , vol.411 , pp. 157-160
    • Halliwell, B.1
  • 72
    • 0036890517 scopus 로고    scopus 로고
    • Protein nitration in cardiovascular diseases
    • Turko, I. V., and Murad, F. (2002) Protein nitration in cardiovascular diseases. Pharmacol. Rev. 54, 619-634.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 619-634
    • Turko, I.V.1    Murad, F.2
  • 73
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • Pryor, W. A., and Squadrito, G. L. (1995) The chemistry of peroxynitrite: a product from the reaction of nitric oxide with superoxide. Am. J. Physiol. 268, L699-L722.
    • (1995) Am. J. Physiol. , vol.268
    • Pryor, W.A.1    Squadrito, G.L.2
  • 74
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • Burmester, T., Weich, B., Reinhardt, S., and Hankeln, T. (2000) A vertebrate globin expressed in the brain. Nature 407, 520-523.
    • (2000) Nature , vol.407 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 75
    • 0037449744 scopus 로고    scopus 로고
    • How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina
    • Schmidt, M., Giessl, A., Laufs, T., Hankeln, T., Wolfrum, U., and Burmester, T. (2003) How does the eye breathe? Evidence for neuroglobin-mediated oxygen supply in the mammalian retina. J. Biol. Chem. 278, 1932-1935.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1932-1935
    • Schmidt, M.1    Giessl, A.2    Laufs, T.3    Hankeln, T.4    Wolfrum, U.5    Burmester, T.6
  • 76
    • 0024573682 scopus 로고
    • Structural characterization of nitrimyoglobin
    • Bondoc, L. L., and Timkovic, R. (1989) Structural characterization of nitrimyoglobin. J. Biol. Chem. 264, 6134-6145.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6134-6145
    • Bondoc, L.L.1    Timkovic, R.2
  • 77
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobin
    • DOI 10.1093/embo-reports/kve159
    • Brunori, M., and Gibson, Q. H. (2001) Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep. 8, 674-679. (Pubitemid 32798709)
    • (2001) EMBO Reports , vol.2 , Issue.8 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 78
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • Frauenfelder, H., McMahon, B. H., Austin, R. H., Chu, K., and Groves, J. T. (2001) The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proc. Natl. Acad. Sci. USA 98, 2370-2374.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 79
    • 12944322234 scopus 로고    scopus 로고
    • Catalytic activity, stability, unfolding, and degradation pathways of engineered and reconstituted myoglobins
    • Roncone, R., Monzani, E., Labò, S., Sanangelantoni, A. M., and Casella, L. (2005) Catalytic activity, stability, unfolding, and degradation pathways of engineered and reconstituted myoglobins. J. Biol. Inorg. Chem. 10, 11-24.
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 11-24
    • Roncone, R.1    Monzani, E.2    Labò, S.3    Sanangelantoni, A.M.4    Casella, L.5
  • 80
    • 0036363570 scopus 로고    scopus 로고
    • Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins
    • DOI 10.1016/S0076-6879(02)48634-X, 15, Part B: Protein Sensors and Reactive Oxygen Species
    • Hamann, M., Zhang, T., Hendrich, S., and Thomas, J. A. (2002) Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins. Methods Enzymol. 348, 146-156. (Pubitemid 41103106)
    • (2002) Methods in Enzymology , vol.348 , pp. 146-156
    • Hamann, M.1    Zhang, T.2    Hendrich, S.3    Thomas, J.A.4
  • 81
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins
    • Woo, H. A., Jeong, W., Chang, T.-S., Park, K. J., Park, S. J., Yang, J. S., and Rhee, S. G. (2005) Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins. J. Biol. Chem. 280, 3125-3128.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.-S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6    Rhee, S.G.7
  • 82
  • 83
    • 27644561194 scopus 로고    scopus 로고
    • Perfusion of the isolated trout heart coronary circulation with red blood cells: Effects of oxygen supply and nitrite on coronary flow and myocardial oxygen consumption
    • Jensen, F. B., and Angisola, C. (2005) Perfusion of the isolated trout heart coronary circulation with red blood cells: effects of oxygen supply and nitrite on coronary flow and myocardial oxygen consumption. J. Exp. Biol. 208, 3665-3674.
    • (2005) J. Exp. Biol. , vol.208 , pp. 3665-3674
    • Jensen, F.B.1    Angisola, C.2
  • 84
    • 0028237681 scopus 로고
    • Hydrogen peroxide-mediated ferrylhemoglobin generation in Vitro and in red blood cells
    • DOI 10.1016/0076-6879(94)31032-7
    • Giulivi, C., and Davies, J. A. (1994) Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol. 231, 490-496. (Pubitemid 124015137)
    • (1994) Methods in Enzymology , vol.231 , pp. 490-496
    • Giulivi, C.1
  • 85
    • 0030896551 scopus 로고    scopus 로고
    • The globin-based free radical of ferryl hemoglobin is detected in normal human blood
    • Svistunenko, D. A., Patel, R. P., Voloshchenko, S. V., and Wilson, M. T. (1997) The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J. Biol. Chem. 272, 7114-7121.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7114-7121
    • Svistunenko, D.A.1    Patel, R.P.2    Voloshchenko, S.V.3    Wilson, M.T.4
  • 86
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H., and Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 87
    • 23144439273 scopus 로고    scopus 로고
    • Internal cavities and ligand passageways in human hemoglobin characterized by molecular dynamics simulations
    • Mouawad, L., Maréchal, J.-D., and Perahia, D. (2005) Internal cavities and ligand passageways in human hemoglobin characterized by molecular dynamics simulations. Biochem. Biophys. Acta 1724, 385-393.
    • (2005) Biochem. Biophys. Acta , vol.1724 , pp. 385-393
    • Mouawad, L.1    Maréchal, J.-D.2    Perahia, D.3
  • 88
    • 0031021944 scopus 로고    scopus 로고
    • Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques
    • Leeuwenburgh, C., Rasmussen, J. E., Hsu, F. F., Mueller, D. M., Pennathur, S., and Heinecke, J. W. (1997) Mass spectrometric quantification of markers for protein oxidation by tyrosyl radical, copper, and hydroxyl radical in low density lipoprotein isolated from human atherosclerotic plaques. J. Biol. Chem. 272, 3520-3526.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3520-3526
    • Leeuwenburgh, C.1    Rasmussen, J.E.2    Hsu, F.F.3    Mueller, D.M.4    Pennathur, S.5    Heinecke, J.W.6
  • 89
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley, K., Maidt, M. L., Yu, Z. Q., Sang, H., Markesbery, W. R., and Floyd, R. A. (1998) Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 18, 8126-8132. (Pubitemid 28464991)
    • (1998) Journal of Neuroscience , vol.18 , Issue.20 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 90
    • 0031056208 scopus 로고    scopus 로고
    • The Toxicities of Native and Modified Hemoglobins
    • Everse, J., and Hsia, N. (1997) The Toxicities of Native and Modified Hemoglobins. Free Radic. Biol. Med. 22, 1075-1099.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 1075-1099
    • Everse, J.1    Hsia, N.2
  • 92
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen
    • Trent, J. T. III, Watts, R. A., and Hargrove, M. S. (2001) Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen. J. Biol. Chem. 276, 30106-30110.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30106-30110
    • Trent III, J.T.1    Watts, R.A.2    Hargrove, M.S.3
  • 93
    • 1242316981 scopus 로고    scopus 로고
    • Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps
    • Uno, T., Ryu, D., Tsutsumi, H., Tomisugi, Y., Ishikawa, Y., Wilkinson, A. J., Sato, H., and Hayashi, T. (2004) Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps. J. Biol. Chem. 279, 5886-5893.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5886-5893
    • Uno, T.1    Ryu, D.2    Tsutsumi, H.3    Tomisugi, Y.4    Ishikawa, Y.5    Wilkinson, A.J.6    Sato, H.7    Hayashi, T.8
  • 96
    • 7244245630 scopus 로고    scopus 로고
    • Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance
    • Fago, A., Hundahl, C., Dewilde, S., Gilany, K., Moens, L., and Weber, R. E. (2004) Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance. J. Biol. Chem. 279, 44417-44426.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44417-44426
    • Fago, A.1    Hundahl, C.2    Dewilde, S.3    Gilany, K.4    Moens, L.5    Weber, R.E.6
  • 97
    • 2542447171 scopus 로고    scopus 로고
    • Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress
    • Herold, S., Fago, A., Weber, R. E., Dewilde, S., and Moens, L. (2004) Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress. J. Biol. Chem. 279, 22841-22847.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22841-22847
    • Herold, S.1    Fago, A.2    Weber, R.E.3    Dewilde, S.4    Moens, L.5
  • 98
    • 0242285663 scopus 로고    scopus 로고
    • Neuromelanin of the substantia nigra: A neuronal black hole with protective and toxic characteristics
    • DOI 10.1016/j.tins.2003.08.009
    • Zecca, L., Zucca, F. A., Wilms, H., and Sulzer, D. (2003) Neuromelanin of the substantia nigra: a neuronal black hole with protective and toxic characteristics. Trends Neurosci. 26, 578-580. (Pubitemid 37338363)
    • (2003) Trends in Neurosciences , vol.26 , Issue.11 , pp. 578-580
    • Zecca, L.1    Zucca, F.A.2    Wilms, H.3    Sulzer, D.4
  • 101
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
    • Xu, J., Kao, S. Y., Lee, F. J., Song, W., Jin, L. W., and Yankner, B. A. (2002) Dopamine-dependent neurotoxicity of α-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8, 600-606.
    • (2002) Nat. Med. , vol.8 , pp. 600-606
    • Xu, J.1    Kao, S.Y.2    Lee, F.J.3    Song, W.4    Jin, L.W.5    Yankner, B.A.6
  • 103
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • DOI 10.1096/fj.03-0770fje
    • Li, J., Zhu, M., Manning-Bog, A. B., Di Monte, D., and Fink, A. L. (2004) Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB J. 18, 962-964. (Pubitemid 39561492)
    • (2004) FASEB Journal , vol.18 , Issue.9 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 105
    • 0024451194 scopus 로고
    • Oxidation of the substituted catechols dihydroxyphenylalanine methyl ester and trihydroxyphenylalanine by lactoperoxidase and its compounds
    • Metodiewa, D., Rezka, K., and Dunford. H. B. (1989) Oxidation of the substituted catechols dihydroxyphenylalanine methyl ester and trihydroxyphenylalanine by lactoperoxidase and its compounds. Arch. Biochem Biopsys. 274, 601-608.
    • (1989) Arch. Biochem Biopsys. , vol.274 , pp. 601-608
    • Metodiewa, D.1    Rezka, K.2    Dunford, H.B.3
  • 106
    • 0030880690 scopus 로고    scopus 로고
    • Tyrosinase-catecholic substrates in vitro model: Kinetic studies on the o-quinone/o-semiquinone radical formation
    • Ferrari, R. P., Laurenti, E., Ghibaudi, E. M., and Casella, L. (1997) Tyrosinase-catecholic substrates in vitro model: kinetic studies on the o-quinone/o-semiquinone radical formation. J. Inorg. Biochem. 68, 61-69.
    • (1997) J. Inorg. Biochem. , vol.68 , pp. 61-69
    • Ferrari, R.P.1    Laurenti, E.2    Ghibaudi, E.M.3    Casella, L.4
  • 107
    • 0036523459 scopus 로고    scopus 로고
    • Characterization and peroxidase activity of a myoglobin mutant containing a distal arginine
    • DOI 10.1002/1439-7633(20020301)3:2/3<226::AID-CBIC226>3.0.CO;2-7
    • Redaelli, C., Monzani, E., Santagostini, L., Casella, L., Sanangelantoni, A. M., Pierattelli, R., and Banci, L. (2002) Characterization and Peroxidase Activity of a Myoglobin Mutant Containing a Distal Arginine. ChemBioChem 3, 226-233. (Pubitemid 36004499)
    • (2002) ChemBioChem , vol.3 , Issue.2-3 , pp. 226-233
    • Redaelli, C.1    Monzani, E.2    Santagostini, L.3    Casella, L.4    Sanangelantoni, A.M.5    Pierattelli, R.6    Banci, L.7
  • 109
    • 0016907344 scopus 로고
    • Potential oxidative pathways of brain catecholamines
    • Tse, D. C. S., McCreery, R. L., and Adams, R. N. (1976) Potential oxidative pathways of brain catecholamines. J. Med. Chem. 19, 37-40.
    • (1976) J. Med. Chem. , vol.19 , pp. 37-40
    • Tse, D.C.S.1    McCreery, R.L.2    Adams, R.N.3
  • 110
    • 0029931085 scopus 로고    scopus 로고
    • Characterization of products from the reactions of N-acetyldopamine quinone with N-acetylhistidine
    • Xu, R., Huang, X., Morgan, T. D., Prakash, O., Kramer, K. J., and Hawley, M. D. (1996) Characterization of products from the reactions of N-acetyldopamine quinone with N-acetylhistidine. Arch. Biochem. Biophys. 329, 56-64.
    • (1996) Arch. Biochem. Biophys. , vol.329 , pp. 56-64
    • Xu, R.1    Huang, X.2    Morgan, T.D.3    Prakash, O.4    Kramer, K.J.5    Hawley, M.D.6
  • 111
    • 0031164759 scopus 로고    scopus 로고
    • Model insect cuticle sclerotization: Reactions of catecholamine quinones with the nitrogen-centered nucleophiles imidazole and N-acetylhistidine
    • Huang, X., Xu, R., Hawley, M. D., and Kramer, K. J. (1997) Model insect cuticle sclerotization: reactions of catecholamine quinones with the nitrogen-centered nucleophiles imidazole and N-acetylhistidine. Bioorg. Chem. 25, 179-202.
    • (1997) Bioorg. Chem. , vol.25 , pp. 179-202
    • Huang, X.1    Xu, R.2    Hawley, M.D.3    Kramer, K.J.4
  • 113
    • 0032052389 scopus 로고    scopus 로고
    • Electrochemical oxidation of N-acyldopamines and regioselective reactions of their quinones with N-acetylcysteine and thiourea
    • Huang, X., Xu, R., Hawley, D., Hopkins, T. L., and Kramer, K. J. (1998) Electrochemical oxidation of N-acyldopamines and regioselective reactions of their quinones with N-acetylcysteine and thiourea. Arch. Biochem. Biophys. 352, 19-30.
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 19-30
    • Huang, X.1    Xu, R.2    Hawley, D.3    Hopkins, T.L.4    Kramer, K.J.5
  • 114
    • 0025289622 scopus 로고
    • X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution
    • Hubbard, S. R., Hendrickson, W. A., Lambright, D. G., and Boxer, S. G. (1990) X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution. J. Mol. Biol. 213, 215-218.
    • (1990) J. Mol. Biol. , vol.213 , pp. 215-218
    • Hubbard, S.R.1    Hendrickson, W.A.2    Lambright, D.G.3    Boxer, S.G.4
  • 116
    • 0042206787 scopus 로고    scopus 로고
    • Dopamine prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide. Is nitrotyrosine formation an early step in dopamine neuronal damage?
    • Park, S., Geddes, T. J., Javitch, J. A., and Kuhn, D. M. (2003) Dopamine prevents nitration of tyrosine hydroxylase by peroxynitrite and nitrogen dioxide. Is nitrotyrosine formation an early step in dopamine neuronal damage? J. Biol. Chem. 278, 28736-28742.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28736-28742
    • Park, S.1    Geddes, T.J.2    Javitch, J.A.3    Kuhn, D.M.4
  • 117
    • 0041833723 scopus 로고    scopus 로고
    • Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity
    • DOI 10.1016/S0969-2126(03)00166-7
    • Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., Burmester, T., and Bolognesi, M. (2003) Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure 11, 1087-1095. (Pubitemid 37103070)
    • (2003) Structure , vol.11 , Issue.9 , pp. 1087-1095
    • Pesce, A.1    Dewilde, S.2    Nardini, M.3    Moens, L.4    Ascenzi, P.5    Hankeln, T.6    Burmester, T.7    Bolognesi, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.