메뉴 건너뛰기




Volumn 407, Issue 1, 2007, Pages 89-99

Reactivity and endogenous modification by nitrite and hydrogen peroxide: Does human neuroglobin act only as a scavenger?

Author keywords

Cysteine oxidation; Haem; Human neuroglobin (NGB); Oxidative stress; Peroxynitrite; Tyrosine nitration

Indexed keywords

CYSTEINE OXIDATION; HUMAN NEUROGLOBIN (NGB); PEROXYNITRITE; TYROSINE NITRATION;

EID: 35148878780     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070372     Document Type: Article
Times cited : (50)

References (52)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen
    • Trent, III, J. T., 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
  • 4
    • 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
  • 6
    • 0042170141 scopus 로고    scopus 로고
    • Neuroprotection and the role of neuroglobin
    • Garry, D. J. and Mammen, P. P. A. (2003) Neuroprotection and the role of neuroglobin. Lancet 362, 342-343
    • (2003) Lancet , vol.362 , pp. 342-343
    • Garry, D.J.1    Mammen, P.P.A.2
  • 11
    • 30744469606 scopus 로고    scopus 로고
    • Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species
    • Smagghe, B. J., Sarath, G., Ross, E., Hilbert, J-L. and Hargrove, M. S. (2006) Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species. Biochemistry 45, 561-570
    • (2006) Biochemistry , vol.45 , pp. 561-570
    • Smagghe, B.J.1    Sarath, G.2    Ross, E.3    Hilbert, J.-L.4    Hargrove, M.S.5
  • 12
    • 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
  • 14
    • 10644251786 scopus 로고    scopus 로고
    • The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity
    • Vallone, B., Nienhaus, K., Matthes, A., Brunori, M. and Nienhaus, G. U. (2004) The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Proc. Natl. Acad. Sci. U.S.A. 101, 17351-17356
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 17351-17356
    • Vallone, B.1    Nienhaus, K.2    Matthes, A.3    Brunori, M.4    Nienhaus, G.U.5
  • 17
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury
    • Sun, Y., Jin, K., Mao, X. O., Zhu, Y. and Greenberg, D. A. (2001) Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc. Natl. Acad. Sci. U.S.A. 98, 15306-15311
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, Y.4    Greenberg, D.A.5
  • 18
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton, P. (1999) Ischemic cell death in brain neurons. Physiol. Rev. 79, 1431-1568
    • (1999) Physiol. Rev , vol.79 , pp. 1431-1568
    • Lipton, P.1
  • 20
    • 26644473174 scopus 로고    scopus 로고
    • Reactions of peroxynitrite with globin proteins and their possible physiological role
    • Herold, S. and Fago, A. (2005) Reactions of peroxynitrite with globin proteins and their possible physiological role. Comp. Biochem. Physiol. A: Mol. Integr. Physiol. 142, 124-129
    • (2005) Comp. Biochem. Physiol. A: Mol. Integr. Physiol , vol.142 , pp. 124-129
    • Herold, S.1    Fago, A.2
  • 21
    • 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
  • 22
    • 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
  • 23
    • 2442450674 scopus 로고    scopus 로고
    • Metmyoglobin-catalyzed exogenous and endogenous tyrosine nitration by nitrite and hydrogen peroxide
    • Nicolis, S., Monzani, E., Roncone, R., Gianelli, L. and Casella, L. (2004) Metmyoglobin-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
    • 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
  • 27
    • 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
  • 29
    • 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
  • 32
    • 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
  • 34
    • 0014060675 scopus 로고
    • Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine
    • Grassetti, D. R. and Murray, J. F. (1967) Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine. Arch. Biochem. Biophys. 119, 41-49
    • (1967) Arch. Biochem. Biophys , vol.119 , pp. 41-49
    • Grassetti, D.R.1    Murray, J.F.2
  • 35
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg, P. J. (2003) Disulfide bonds as switches for protein function. Trends Biochem. Sci. 28, 210-214
    • (2003) Trends Biochem. Sci , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 36
    • 0038682731 scopus 로고    scopus 로고
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin. J. Am. Chem. Soc. 125, 8080-8081
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8080-8081
    • Du, W.1    Syvitski, R.2    Dewilde, S.3    Moens, L.4    La Mar, G.N.5
  • 38
    • 0041565319 scopus 로고    scopus 로고
    • Introduction of P450, peroxidase, and catalase activities into myoglobin by site-directed mutagenesis: Diverse reactivities of compound I
    • Watanabe, Y. and Ueno, T. (2003) Introduction of P450, peroxidase, and catalase activities into myoglobin by site-directed mutagenesis: diverse reactivities of compound I. Bull. Chem. Soc. Jpn. 76, 1309-1322
    • (2003) Bull. Chem. Soc. Jpn , vol.76 , pp. 1309-1322
    • Watanabe, Y.1    Ueno, T.2
  • 39
    • 4544256622 scopus 로고    scopus 로고
    • Engineering and prosthetic group modification of myoglobin: Peroxidase activity, chemical stability and unfolding properties
    • Roncone, R., Monzani, E., Nicolis, S. and Casella, L. (2004) Engineering and prosthetic group modification of myoglobin: peroxidase activity, chemical stability and unfolding properties, Eur. J. Inorg. Chem., 2203-2213
    • (2004) Eur. J. Inorg. Chem , pp. 2203-2213
    • Roncone, R.1    Monzani, E.2    Nicolis, S.3    Casella, L.4
  • 42
    • 0031032436 scopus 로고    scopus 로고
    • Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover
    • Monzani, E., Gatti, A. L., Profumo, A., Casella, L. and Gullotti, M. (1997) Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover. Biochemistry 36, 1918-1926
    • (1997) Biochemistry , vol.36 , pp. 1918-1926
    • Monzani, E.1    Gatti, A.L.2    Profumo, A.3    Casella, L.4    Gullotti, M.5
  • 43
    • 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
  • 45
    • 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. (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.2
  • 46
    • 0036801298 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species at biologic 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 biologic 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
  • 47
    • 0024573682 scopus 로고
    • Structural characterization of nitrimyoglobin
    • Bondoc, L. L. and Timkovich, 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    Timkovich, R.2
  • 48
    • 33745739596 scopus 로고    scopus 로고
    • The reactions of neuroglobin with CO: Evidence for two forms of the ferrous protein
    • Fago, A., Mathews, A. J., Dewilde, S., Moens, L. and Brittain, T. (2006) The reactions of neuroglobin with CO: evidence for two forms of the ferrous protein. J. Inorg. Biochem. 100, 1339-1343
    • (2006) J. Inorg. Biochem , vol.100 , pp. 1339-1343
    • Fago, A.1    Mathews, A.J.2    Dewilde, S.3    Moens, L.4    Brittain, T.5
  • 49
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., Beckman, J. S., Bush, K. M. and Freeman, B. A. (1991) Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266, 4244-4250
    • (1991) J. Biol. Chem , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 50
    • 0036363570 scopus 로고    scopus 로고
    • Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins
    • 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
    • (2002) Methods Enzymol , vol.348 , pp. 146-156
    • Hamann, M.1    Zhang, T.2    Hendrich, S.3    Thomas, J.A.4
  • 51
    • 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
  • 52
    • 3843064487 scopus 로고    scopus 로고
    • The sulfinic acid switch in proteins
    • Jacob, C., Holme, A. L. and Fry, F. H. (2004) The sulfinic acid switch in proteins. Org. Biomol. Chem. 2, 1953-1956
    • (2004) Org. Biomol. Chem , vol.2 , pp. 1953-1956
    • Jacob, C.1    Holme, A.L.2    Fry, F.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.