Tyrosine as a redox-active center in electron transfer to ferryl heme in globins

Free Radical Biology and Medicine

Volumn 44, Issue 3, 2008, Pages 274-283

  Reeder, Brandon J ^a   Cutruzzola, Francesca ^b   Bigotti, Maria Giulia ^b   Hider, Robert C ^c   Wilson, Michael T ^a  

^a UNIVERSITY OF ESSEX   (United Kingdom)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

Electron transfer; Ferryl; Hemoglobin; Myoglobin; Tyrosine

Indexed keywords

FERRYLHEME; HEME; HEMOGLOBIN; MYOGLOBIN; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CONCENTRATION (PARAMETERS); CYTOTOXICITY; ELECTRON TRANSPORT; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN ENGINEERING;

ANIMALS; ASCORBIC ACID; ELECTRON TRANSPORT; GLOBINS; HEME; IRON CHELATING AGENTS; KINETICS; METMYOGLOBIN; MODELS, MOLECULAR; OXIDATION-REDUCTION; REDUCING AGENTS; TYROSINE;

EID: 38149097703     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.06.030     Document Type: Article

References (37)

1. Kanner J., and Harel S. Lipid peroxidation and oxidation of several compounds by H2O2 activated metmyoglobin. Lipids 20 (1985) 625-628
2. Kanner J., and Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Arch. Biochem. Biophys. 237 (1985) 314-321
3. Rao S.I., Wilks A., Hamberg M., and Ortiz de Montellano P.R. The lipoxygenase activity of myoglobin. Oxidation of linoleic acid by the ferryl oxygen rather than protein radical. J. Biol. Chem. 269 (1994) 7210-7216
4. Aoshima H., Yoshida Y., and Taniguchi H. Reaction between lipid hydroperoxide and hemoglobin studied by a spectrophotometic and a spin trapping method. Aric. Biol. Chem. 50 (1986) 1777-1783
5. Pace-Asciak C.R. Hemoglobin- and hemin-catalyzed transformation of 12L-hydroperoxy-5,8,10,14-eicosatetraenoic acid. Biochim. Biophys. Acta 793 (1984) 485-488
6. Wilcox A.L., and Marnett L.J. Polyunsaturated fatty acid alkoxyl radicals exist as carbon-centered epoxyallylic radicals: a key step in hydroperoxide-amplified lipid peroxidation. Chem. Res. Toxicol. 6 (1993) 413-416
7. Morrow J.D., Hill K.E., Burk R.F., Nammour T.M., Badr K.F., and Roberts L.J.d. A series of prostaglandin F2-like compounds are produced in vivo in humans by a non-cyclooxygenase, free radical-catalyzed mechanism. Proc. Natl. Acad. Sci. USA 87 (1990) 9383-9387
8. Moore K.P., Holt S.G., Patel R.P., Svistunenko D.A., Zackert W., Goodier D., Reeder B.J., Clozel M., Anand R., Cooper C.E., Morrow J.D., Wilson M.T., Darley-Usmar V., and Roberts Jr. L.J. A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure. J. Biol. Chem. 273 (1998) 31731-31737
9. Rice-Evans C., Okunade G., and Khan R. The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine. Free Radic. Res. Commun. 7 (1989) 45-54
10. Reeder B.J., and Wilson M.T. Desferrioxamine inhibits production of cytotoxic heme to protein cross-linked myoglobin: a mechanism to protect against oxidative stress without iron chelation. Chem. Res. Toxicol. 18 (2005) 1004-1011
11. Reeder B.J., Hider R.C., and Wilson M.T. Iron chelators can protect against oxidative stress through ferryl heme reduction. Free Radic. Biol. 44 (2008) 264-273
12. Dobbin P.S., Hider R.C., Hall A.D., Taylor P.D., Sarpong P., Porter J.B., Xiao G., and van der Helm D. Synthesis, physicochemical properties, and biological evaluation of N-substituted 2-alkyl-3-hydroxy-4(1H)-pyridinones: orally active iron chelators with clinical potential. J. Med. Chem. 36 (1993) 2448-2458
13. Streater M., Taylor P.D., Hider R.C., and Porter J. Novel 3-hydroxy-2(1H)-pyridinones. Synthesis, iron(III)-chelating properties, and biological activity. J. Med. Chem. 33 (1990) 1749-1755
14. Reeder B.J., and Wilson M.T. Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid. Biochem. J. 330 (1998) 1317-1323
15. Antonini E., and Brunori M. In: Neuberger A., and Tatum E.L. (Eds). Frontiers in Biology vol. 21 (1971), North-Holland publishing company, Amsterdam-London 13-52
16. Cutruzzola F., Travaglini Allocatelli C., Brancaccio A., and Brunori M. Aplysia limacina myoglobin cDNA cloning: an alternative mechanism of oxygen stabilization as studied by active-site mutagenesis. Biochem. J. 314 Pt 1 (1996) 83-90
17. Cutruzzola F., Allocatelli C.T., Ascenzi P., Bolognesi M., Sligar S.G., and Brunori M. Control and recognition of anionic ligands in myoglobin. FEBS Lett. 282 (1991) 281-284
18. Svistunenko D.A., Dunne J., Fryer M., Nicholls P., Reeder B.J., Wilson M.T., Bigotti M.G., Cutruzzola F., and Cooper C.E. Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide. Biophys. J. 83 (2002) 2845-2855
19. Reeder B.J., Svistunenko D.A., Sharpe M.A., and Wilson M.T. Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin. Biochemistry 41 (2002) 367-375
20. Svistunenko D.A. Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view. Biochim. Biophys. Acta 1707 (2005) 127-155
21. Lardinois O.M., and Ortiz de Montellano P.R. Autoreduction of ferryl myoglobin: discrimination among the three tyrosine and two tryptophan residues as electron donors. Biochemistry 43 (2004) 4601-4610
22. Reeder B.J., and Wilson M.T. The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species. Free Radic. Biol. Med. 30 (2001) 1311-1318
23. Wilbur D.J., and Allerhand A. Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo. J. Biol. Chem. 251 (1976) 5187-5194
24. DeFelippis M.R., Murthy C.P., Faraggi M., and Klapper M.H. Pulse radiolytic measurement of redox potentials: the tyrosine and tryptophan radicals. Biochemistry 28 (1989) 4847-4853
25. He B., Sinclair R., Copeland B.R., Makino R., Powers L.S., and Yamazaki I. The structure-function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase. Biochemistry 35 (1996) 2413-2420
26. Galaris D., and Korantzopoulos P. On the molecular mechanism of metmyoglobin-catalyzed reduction of hydrogen peroxide by ascorbate. Free Radic. Biol. Med. 22 (1997) 657-667
27. Bruck T.B., Gerini M.F., Baciocchi E., and Harvey P.J. Oxidation of thioanisole and p-methoxythioanisole by lignin peroxidase: kinetic evidence of a direct reaction between compound II and a radical cation. Biochem. J. 374 (2003) 761-766
28. Doyle W.A., Blodig W., Veitch N.C., Piontek K., and Smith A.T. Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37 (1998) 15097-15105
29. Blodig W., Doyle W.A., Smith A.T., Winterhalter K., Choinowski T., and Piontek K. Autocatalytic formation of a hydroxy group at C beta of trp171 in lignin peroxidase. Biochemistry 37 (1998) 8832-8838
30. Harvey P.J., Floris R., Lundell T., Palmer J.M., Schoemaker H.E., and Wever R. Catalytic mechanisms and regulation of lignin peroxidase. Biochem. Soc. Trans. 20 (1992) 345-349
31. Johjima T., Itoh N., Kabuto M., Tokimura F., Nakagawa T., Wariishi H., and Tanaka H. Direct interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium. Proc. Natl. Acad. Sci. USA 96 (1999) 1989-1994
32. Schoemaker H.E., Lundell T.K., Floris R., Glumoff T., Winterhalter K.H., and Piontek K. Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force. Bioorg. Med. Chem. 2 (1994) 509-519
33. Walters F.P., Kennedy F.G., and Jones D.P. Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid. FEBS Lett. 163 (1983) 292-296
34. Holt S., Reeder B., Wilson M., Harvey S., Morrow J.D., Roberts Jr. L.J., and Moore K. Increased lipid peroxidation in patients with rhabdomyolysis [letter]. Lancet 353 (1999) 1241
35. Reeder B.J., Sharpe M.A., Kay A.D., Kerr M., Moore K., and Wilson M.T. Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage. Biochem. Soc. Trans. 30 (2002) 745-748
36. Porter J.B. Deferoxamine pharmacokinetics. Semin. Hematol. 38 (2001) 63-68
37. Thuma P.E., Olivieri N.F., Mabeza G.F., Biemba G., Parry D., Zulu S., Fassos F.F., McClelland R.A., Koren G., Brittenham G.M., and Gordeuk V.R. Assessment of the effect of the oral iron chelator deferiprone on asymptomatic Plasmodium falciparum parasitemia in humans. Am. J. Trop. Med. Hyg. 58 (1998) 358-364