Mechanism of peroxynitrite interaction with cytochrome C

• Autorzy: Gebicka L. , Didik J.
• Języki publikacji: EN

Abstrakty

EN

Kinetics of the reaction of peroxynitrite with ferric cytochrome c in the absence and presence of bicarbonate was studied. It was found that the heme iron in ferric cytochrome c does not react directly with peroxynitrite. The rates of the absorbance changes in the Soret region of cytochrome c spectrum caused by peroxynitrite or peroxynitrite/bicarbonate were the same as the rate of spontaneous isomerization of peroxynitrite or as the rate of the reaction of peroxynitrite with bicarbonate, respec­tively. This means that intermediate products of peroxynitrite decomposition, OH/ NO2 or, in the presence of bicarbonate, CO3- / NO2, are the species responsible for the absorbance changes in the Soret band of cytochrome c. Modifications of the heme center of cytochrome c by radiolytically produced radicals, OH, NO2 or CO3- , were also studied. The absorbance changes in the Soret band caused by radiolytically produced OH or CO3- were much more significant that those observed after peroxy­nitrite treatment, compared under similar concentrations of radicals. NO2 produced radiolytically did not interact with the heme center of cytochrome c. Cytochrome c ex­hibited an increased peroxidase-like activity after reaction with peroxynitrite as well as with radiolytically produced OH, NO2 or CO3- radicals. This means that modifi­cation of protein structure: oxidation of amino acids and/or tyrosine nitration, facili­tates reaction of H2O2 with the heme iron of cytochrome c, followed by reaction with the second substrate.

Słowa kluczowe

EN

peroxynitrite interaction; cytochrome C; kinetics

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 3
• Opis fizyczny: p.815-823,fig.

Twórcy

autor

Gebicka L.

• Technical University of Lodz, Wroblewskiego 15, 93-590 Lodz, Poland

autor

Didik J.

Bibliografia

• Alayash AI, Ryan BA, Cashon RE. (1998) Peroxynitrite-mediated heme oxidation and protein modification of native and chemically modified hemoglobins. Arch Biochem Biophys.; 349: 65-73.
• Augusto O, Bonini MG, Amanso AM, Linares E, Santos CCX, De Menezes SL. (2002) Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology. Free Radic Biol Med.; 32: 841-59.
• Bourassa JL, Ives EP, Marqueling AN, Shimanovich R, Groves JT. (2001) Myoglobin catalyzes its own nitration. J Am Chem Soc.; 123: 5142-3.
• Buxton GV, Greenstock CL, Helman WP, Ross AB. (1988) Critical review of rate contants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (OH/O-) in aqueous solution. JPhys Chem Ref Data.; 17: 513-886.
• Cassina AM, Hodara R, Souza JM, Thomson L, Castro L, Ischiropoulos H, Freeman BA, Radi R. (2000) Cytochrome c nitration by peroxynitrite. J Biol Chem.; 275: 21409-15.
• Chen Y-R, Deterding LJ, Sturgeon BE, Tomer KB, Mason RP. (2002) Protein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity. J Biol Chem.; 277: 29781-91.
• Childs RE, Bardsley WG. (1975) The steady-state kinetics of peroxidase with 2,2'-azino-di-(3-ethyl-benzthiazoline-6- sulphonic acid) as chromogen. Biochem J.; 145: 93-103.
• Coddington JW, Hurst JK, Lymar SV. (1999) Hydroxyl radical formation during peroxynitrous acid decomposition. J Am Chem Soc.; 121: 2438-43.
• Deiber A, Herold S, Schoneich C, Namgaladze D, Peterson JA, Ullrich V. (2000) Nitration and inactivation of cytochrome P450(BM-3) by peroxynitrite — Stopped-flow measurements prove ferryl intermediates. Eur J Biochem.; 267: 6729-39.
• Diederix REM, Ubbink M, Canters GW. (2002) Peroxidase activity as a tool for studying the folding of c-type cytochromes. Biochemistry.; 41: 13067-77.
• Exner M, Herold S. (2000) Kinetic and mechanistic studies of the peroxynitrite-mediated oxidation of oxymyoglobin and oxyhemoglobin. Chem Res Toxicol.; 13: 287-93.
• Floris R, Piersma R, Yang G, Jones P, Wever R. (1993) Interaction of myeloperoxidase with peroxynitrite. Eur J Biochem.; 215: 767-75.
• Gerasimov OV, Lymar SV. (1999) The yield of hydroxyl radical from the decomposition of peroxynitrous acid. Inorg Chem.; 38: 4317-21.
• Gebicka L, Gebicki JL. (1992) Redox transformations in peroxidases studied by pulse radiolysis technique. Radiat Phys Chem.; 39: 113-6.
• Gebicka L. (2001) Peroxidase-like activity of cytochrome c in the presence of anionic surfactants. Res Chem Intermed.; 27:717-23.
• Gebicka L, Gebicki JL. (2000) Reactions of heme peroxidases with peroxynitrite. IUBMB Life.; 49: 11-5. Goldstein S, Czapski G. (1998) Formation of peroxynitrate from the reaction of peroxynitrite with CO2: Evidence for carbonate radical production. J Am Chem Soc.; 120: 3458-63.
• Goldstein S, Meyerstein D, van Eldik R, Czapski G. (1999) Peroxynitrous acid decomposes via homolysis: evidence from high-pressure pulse radiolysis. J Phys Chem A.; 103: 6587-90.
• Goto Y, Hagihara Y, Hamada D, Hoshino M, Nishi I. (1993) Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in H2O and D2O. Biochemistry.; 32: 11878-85.
• Gow A, Duran D, Thom SR, Ischiropoulos H. (1996) Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration. Arch Biochem Biophys.; 333: 42-8.
• Grisham MB, Johnson GG, Lancaster Jr JR. (1996) Quantitation of nitrate and nitrite in extracellular fluids. Methods Enzymol.; 268: 237-46.
• Hamachi J, Fujita A, Kunitake T. (1994) Enhanced N-demethylase activity of cytochrome c bound to a phosphate-bearing synthetic bilayer membrane. J Am Chem Soc.; 116: 8811-2.
• Hudges MN, Nicklin HG. (1968) The chemistry of pernitrites. Part I: Kinetics of decomposition of pernitrous acid. J Chem Soc.; 450-2.
• Kissner R, Nauser T, Bugnon P, Lye PG, Koppenol WH. (1998) Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis. Chem Res Toxicol.; 10: 1285-92.
• Koppenol WH, Moreno JJ, Pryor WA, Ischiropoulos H, Beckman JS. (1992) Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide. Chem Res Toxicol.; 5: 834-42.
• Lemercier JN, Padmaja S, Cueto R, Squadrito GL, Uppu RM, Pryor WA. (1997) Carbon dioxide modulation of hydroxylation and nitration of phenol by peroxynitrite. Arch Biochem Biophys.; 345: 160-70.
• Lymar SV, . (1995) Rapid reaction between peroxynitrite ion and carbon dioxide: implications for biological activity. J Am Chem Soc.; 117: 8867-8.
• Mehl M, Daibler A, Herold S, Shoun H, Ullrich V. (1999) Peroxynitrite reaction with heme protein. Nitric Oxide.; 3: 142-52.
• Meli R, Nauser T, Latal P, Koppenol WH. (2002) Reaction of peroxynitrite with carbon dioxide: intermediates and determination of the yield of CO3- and NO2. J Biol Inorg Chem.; 7: 31-6.
• Merenyi G, Lind J. (1997) Thermodynamics of peroxynitrite and its CO2 adduct. Chem Res Toxicol.; 10: 1216-20.
• Merenyi G, Lind J. (1998) Free radical formation in the peroxynitrous acid (ONOOH)/peroxynitrite (ONOO-) system. Chem Res Toxicol.; 11: 243-6.
• Minetti M, Scorza G, Pietraforte D. (1999) Peroxynitrite induces long-lived tyrosyl radical(s) in oxyhemoglobin of red blood cells through a reaction involving CO2 and ferryl species. Biochemistry.; 38: 2078-87.
• Nakagawa H, Ohshima Y, Takusagawa M, Ikota N, Takahashi Y, Shimizu S, Ozawa T. (2001) Functional modification of cytochrome c by peroxynitrite in an electron transfer reaction. Chem Pharm Bull.; 49: 1547-54.
• Neta P, Huie RE, Ross AB. (1988) Rate constants for reactions of inorganic radicals in aqueous solution. JPhys RefData.; 17:1027-284.
• Oellerich S, Wackerbarth H, Hildebrandt P. (2002) Spectroscopic characterization of nonnative conformational states of cytochrome c. J Phys Chem B.; 106: 6566-80.
• Patel RP, McAndrew J, Sellak H, White CR, Jo H, Freeman BA, Darley-Usmar VM. (1999) Biological aspects of reactive nitrogen species. Biochim Biophys Acta.; 1411: 385-400.
• Pietraforte D, Salzano AM, Scorza G, Marino G, Minetti M. (2001) Mechanism of peroxynitrite interaction with ferric hemoglobin and identification of nitrated tyrosine residues. CO2 inhibits heme-catalyzed scavenging and isomerization. Biochemistry.; 40: 15300-9.
• Prutz A, Monig H, Butler J, Land EJ. (1985) Reactions of nitrogen dioxide in aqueous model systems: oxidation of tyrosine units in peptides and proteins. Arch Biochem Biophys.; 243: 125-34.
• Pryor WA, Cueto R, Jin X, Koppenol WH, Ngu-Schwemlein M, Squadrito GL, Uppu PL, Uppu MR. (1995) A practical method for preparing peroxynitrite solutions of low ionic strength and free of hydrogen peroxide. Free Radic Biol Med.; 18: 75-83.
• Radi R, Peluffo G, Alvarez MN, Navillat M, Cayota A. (2001) Unraveling peroxynitrite formation in biological systems. Free Radic Biol Med.; 30: 463-88.
• Radi R, Thomson L, Rubbo H, Prodanov E. (1991) Cytochrome c-catalyzed oxidation of organic molecules by hydrogen peroxide. Arch Biochem Biophys.; 288: 112-7.
• Simic MG, Taub IA. (1977) Mechanisms of inter- and intra-molecular electron transfer in cytochromes. Faraday Discuss Chem Soc.; 63: 270-8.
• Squadrito GL, Pryor WA. (1998) Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite and carbon dioxide. Free Radic Biol Med.; 25: 392-403.
• Thomson L, Trujillo M, Telleri R, Radi R. (1995) Kinetics of cytochrome c2+ oxidation by peroxynitrite: implications for superoxide measurements in nitric oxide-producing biological systems. Arch Biochem Biophys.; 319: 491-7.
• Uppu RM, Squadrito GL, Cueto R, Pryor WA. (1996) Synthesis of peroxynitrite by azide-ozone reaction. Methods Enzymol.; 269: 311-21.
• Whitburn KD, Shieh JJ, Sellers RM, Hoffman MZ, Taub IA. (1982) Redox transformations in ferrimyoglobin induced by radiation-generated free radicals in aqueous solution. J Biol Chem.; 257: 1860-9.
• Yeh SR, Han S, Rousseau DL. (1998) Cytochrome c folding and unfolding: A biphasic mechanism. Acc Chem Res.; 31: 727-36.
• Yermilov V, Yoshie Y, Rubio J, Ohshima H. (1996) Effects of carbon dioxide/bicarbonate on induction of DNA single­strand breaks and formation of 8-nitroguanine, 8-oxoguanine and base-propenal mediated by peroxynitrite. FEBS Lett.; 399: 67-70.