Nitration of the tyrosyl radical in ribonucleotide reductase by nitrogen dioxide: A gamma radiolysis study

Free Radical Biology and Medicine

Volumn 38, Issue 11, 2005, Pages 1511-1517

  Lepoivre, Michel ^a   Houée Levin, Chantal ^b   Coeytaux, Karen ^a   Decottignies, Paulette ^a   Auger, Geneviève ^a   Lemaire, Geneviève ^a  

^a CNRS   (France)

^b UNIVERSITÉ PARIS SUD   (France)

Author keywords

Gamma radiolysis; Nitric oxide; Nitrogen dioxide; Peroxynitrite; Ribonucleotide reductase; Tyrosine nitration; Tyrosine radical

Indexed keywords

NITROGEN DIOXIDE; NITROGEN OXIDE; PEPTIDE DERIVATIVE; PROTEIN SUBUNIT; RIBONUCLEOTIDE REDUCTASE; TYROSINE DERIVATIVE;

ARTICLE; CATALYSIS; CATALYST; CHEMICAL BOND; NITRATION; PRIORITY JOURNAL; RADIOLYSIS;

CATALYSIS; DOSE-RESPONSE RELATIONSHIP, RADIATION; ELECTRONS; ESCHERICHIA COLI; FREE RADICALS; GAMMA RAYS; MODELS, CHEMICAL; MODELS, STATISTICAL; NITRIC OXIDE; NITROGEN; NITROGEN DIOXIDE; OXYGEN; PEROXIDASE; PLASMIDS; RIBONUCLEOTIDE REDUCTASES; TIME FACTORS; TYROSINE;

EID: 18844455826     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.02.013     Document Type: Article

References (25)

1. R. Radi Nitric oxide, oxidants, and protein tyrosine nitration Proc. Natl. Acad. Sci. USA 101 2004 4003 4008
2. F.J. Schopfer, P.R. Baker, and B.A. Freeman NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response? Trends Biochem. Sci. 28 2003 646 654
3. J.M. Souza, Q. Chen, B. Blanchard-Fillion, S.A. Lorch, C. Hertkorn, R. Lightfoot, M. Weisse, T. Friel, E. Paxinou, M. Themistocleous, S. Chov, and H. Ischiropoulos Reactive nitrogen species and proteins: biological significance and clinical relevance Adv. Exp. Med. Biol. 500 2001 169 174
4. W.A. Prutz, H. Monig, J. Butler, and E.J. Land Reactions of nitrogen dioxide in aqueous model systems: oxidation of tyrosine units in peptides and proteins Arch. Biochem. Biophys. 243 1985 125 134
5. C.W. Hoganson, and C. Tommos The function and characteristics of tyrosyl radical cofactors Biochim. Biophys. Acta 1655 2004 116 122
6. R.P. Pesavento, and W.A. van der Donk Tyrosyl radical cofactors Adv. Protein Chem. 58 2001 317 385
7. P. Nordlund, and H. Eklund Structure and function of the Escherichia coli ribonucleotide reductase protein R2 J. Mol. Biol. 232 1993 123 164
8. B. Kauppi, B.B. Nielsen, S. Ramaswamy, I.K. Larsen, M. Thelander, L. Thelander, and H. Eklund The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2 J. Mol. Biol. 262 1996 706 720
9. M.C. Chang, C.S. Yee, J. Stubbe, and D.G. Nocera Turning on ribonucleotide reductase by light-initiated amino acid radical generation Proc. Natl. Acad. Sci. USA 101 2004 6882 6887
10. O. Guittet, B. Ducastel, J.S. Salem, Y. Henry, H. Rubin, G. Lemaire, and M. Lepoivtore Differential sensitivity of the tyrosyl radical of mouse ribonucleotide reductase to nitric oxide and peroxynitrite J. Biol. Chem. 273 1998 22136 22144
11. C. Gerez, E. Elleingand, B. Kauppi, H. Eklund, and M. Fontecave Reactivity of the tyrosyl radical of Escherichia coli ribonucleotide reductase-Control by the protein Eur. J. Biochem. 249 1997 401 407
12. B.M. Sjoberg, S. Hahne, M. Karlsson, H. Jornvall, M. Goransson, and B.E. Uhlin Overproduction and purification of the B2 subunit of ribonucleotide reductase from Escherichia coli J. Biol. Chem. 261 1986 5658 5662
13. J.W.T. Spinks, and R.J. Woods Introduction to radiation chemistry 1990 Wiley Intersciences New York
14. P. Neta, R. Huie, and A.B. Ross Rate constants for reactions of inorganic radicals in aqueous solutions J. Phys. Chem. Ref. Data 17 1988 1027 1284
15. S. Moore, and W. Stein Chromatographic detection of amino acids by the use of automatic recording equipment Methods Enzymol. 6 1963 819 831
16. A.S. Petersson, H. Steen, D.E. Kalume, K. Caidahl, and P. Roepstorff Investigation of tyrosine nitration in proteins by mass spectrometry J. Mass Spectrom. 36 2001 616 625
17. O. Guittet, P. Decottignies, L. Serani, Y. Henry, P. Le Marechal, O. Laprevote, and M. Lepoivre Peroxynitrite-mediated nitration of the stable free radical tyrosine residue of the ribonucleotide reductase small subunit Biochemistry 39 2000 4640 4648
18. M. Kirsch, H.G. Korth, R. Sustmann, and H. de Groot The pathobiochemistry of nitrogen dioxide J. Biol. Chem. 383 2002 389 399
19. O. Augusto, M.G. Bonini, A.M. Amanso, E. Linares, C.C. Santos, and S.L. De Menezes Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology Free Radic. Biol. Med. 32 2002 841 859
20. S. Goldstein, G. Czapski, J. Lind, and G. Merenyi Tyrosine nitration by simultaneous generation of ()NO and O-(2) under physiological conditions. How the radicals do the job J. Biol. Chem. 275 2000 3031 3036
21. M. Cudic, M. Dendane, C. Houe-Levin, and C. Ducrocq Nitration of angiotensin II by NO2 radicals and peroxynitrite. NO protects against, NO2 radical reaction Eur. J. Biochem. 265 1999 967 971
22. M. Stuart-Audette, Y. Blouquit, M. Faraggi, C. Sicard-Roselli, C. Houee-Levin, and P. Jolles Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes. Evidence for the participation of other residues Eur. J. Biochem. 270 2003 3565 3571
23. K.-Y. Lam, K. Govindaraju, J.-Y. Han, G.A. Salmon, and G. Sykes Free-radical formation in the pulse-radiolysis oxidation of inactive Escherichia coli met-R2 ribonucleotide reductase J. Chem. Soc. Dalton Trans. 17 1993 2797 2801
24. K.E. Silva, T.E. Elgren, L. Que Jr., and M.T. Stankovich Electron transfer properties of the R2 protein of ribonucleotide reductase from Escherichia coli Biochemistry 34 1995 14093 14103
25. D.T. Logan, X.D. Su, A. Aberg, K. Regnstrom, J. Hajdu, H. Eklund, and P. Nordlund Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site Structure 4 1996 1053 1064