Механизм реакции усиленной хемилюминесценции, катализируемой пероксидазами
Диссертация
Реакцию проводили в буфере 0.05М Трис-НС1, №С1 0.1М, рН=8.5. Объем реакционной смеси составлял 1 мл. Концентрация фермента составляла 100 нМ, концентрация люминола — 0.25 мМ. Перед инициацией реакции отбирали пробу объемом 100 мкл. Реакцию инициировали добавлением 10 мкл 0.1 М раствора перекиси водорода. Реакцию проводили при температуре 25 °C. Определение общей выделяемой светосуммы проводили… Читать ещё >
Список литературы
- Whitehead, T. P.- Thorpe, G. H. G.- Carter, T. J. N.- Groucutt, C.- Kricka, L. J. //Enhanced Luminescence Procedure for Sensitive Determination of PeroxidaseLabelled Conjugates in Immunoassays. Nature 1983, 305, pp: 158−159.
- Lagrimini L.M.- Burkhart W- Moyer M.- Rothstein S //Tabac Peroxidase. Proc Natl Acad Sci USA 1987,84, pp: 7542−7546.
- Van Huystee, R. B.- Hu, C.- Sesto, P. A. //Comparisons Between Cationic and Anionic Peanut Peroxidase As Glycoproteins. In Isozymes: Structure, Function, and Use in Biology and Medicine- Wiley-Liss: 1990-pp:315−325.
- Shinmen Y.- Asami S.- Amashi T.- Shimizu S.- Yamada H. //Novell Peroxidase From Arthromyces Ramosus. Agric. Biol. Chem. 1986, 241(4), pp: 247−249.
- Welinder, K. G.- Gajhede, M. //Structure and Evolution of Peroxidases. In Plant Peroxidases Biochemistry and Physiology, Welinder, K. G., Rasmussen, S. K., Penel, C., Greppin, H., Eds.- University of Geneva: Geneva, 1993.
- Fujiyama, K.- Takemura, H.- Shinmyo, A.- Okada, H.- Takano, M. //Genomic DNA Structure of Two New Horseradish-Peroxidase-Encoding Genes. Gene 1990,89(2), pp: 163−169.
- Mazza, G.- Welinder, K. G. //Covalent Structure of Turnip Peroxidase 7. Cyanogen Bromide Fragments, Complete Structure and Comparison to Horseradish Peroxidase C. Eur. J. Biochem. 1980,108(2), pp: 481−489.
- Buffard, D.- Breda, С.- Van Huystee, R. В.- Asemota, O.- Pierre, M.- Ha, D. B. D.- Esnault, R. //Molecular Cloning of Complementary DNAs Encoding Two Cationic Peroxidases From Cultivated Peanut Cells. Proc. Nat. Acad. Sci. USA 1990, 87, pp: 8874−8878.
- Abeles, F. В.- Dunn, L. J.- Morgens, P.- Callahan, A.- Dinterman, R. E.- Schmidt, J. //Cucumber Peroxidase. Plant Physiol 1988, 87, pp: 609−615.
- Roberts E- Kutchan T- Kolattukudy P.E. //Potato Peroxidase. Plant Mol Biol 1988,11, pp: 15−31.
- Мухамеджанов Б.Г. //Новые Источники Пероксидаз. Изв. АНКазСС, Сер. Биол. 1983,48(4), рр: 14−17.
- Blauer, G.- Sreerama, N.- Woody, R. W. //Optical Activity of Hemoproteins in the Soret Region Circular Dichroism of the Heme Undecapeptide of Cytochrome- с in Aqueous Solution. Biochemistry 1993, 32, pp: 6674−6679.
- Frew, J. E.- Jones, P. L. //Structure and Functional Properties of Peroxidases and Catalases. Advances in Inorganic and Bioinorganic Mechanisms 1984, 3, pp: 175−212.
- Welinder, K. G. //Amino Acid Sequence Studies of Horseradish Peroxidase. Eur. J. Biochem. 1979, 96, pp: 483−502.
- Gajhede, M.- Schuller, D. J.- Henriksen, A.- Smith, A. T.- Poulos, T. L. //Crystal Structure of Horseradish Peroxidase C at 2.15 A Resolution. Nat. Struct. Biol. 1997, 4(12), pp: 1032−1038.
- Piontek, K.- Glumoff, T.- Winterhalter, K. //Low PH Crystal Structure of Glycosylated Lignin Peroxidase From Phanerochaete-Chrysosporium at 2.5 A Resolution. FEBS Lett. 1993, 315, pp: 119−124.
- Poulos, T. L.- Edwards, S. L.- Wariishi, H.- Gold, M. H. //Crystalographic Refinement of Lignin Peroxidase at 2 A. J. Biol. Chem. 1993, 268, pp: 44 294 440.
- Alic, M.- Gold, M. H. //Genetics and Molecular Biology of the Lignin-Degrading Basidiomycete Phanerochaete Chrysosporium. In More Gene Manipulations in Fungi-, Academic Press Inc.: 1991- Chapter 15, pp:320−341.
- Patersen, J. F. W.- Tams, J. W.- Vind, J.- Svensson, A.- Dalboge, H.- Welinder, K. G.- Larsen, S. //Crystallization and X-Ray Diffraction Analysis of Recombinant Coprinus Cinereus Peroxidase. J. Mol. Biol. 1993.
- Patersen, J. W. F.- Kadziola, A.- Larsen, S. //A Preliminary Crystal Structure Analysis of Recombinant Coprinus Cinereus Peroxidase. In Plant Peroxidases
- Biochemistry and Physiology, Welinder, K. G., Rasmussen, S. K., Penel, C., Greppin, H., Eds.- University of Geneva: Geneva, 1993.
- Baunsgaard, L.- Vind, J.- Dalbge, H. //The Sequence of Coprinus Cinereus Peroxidase Gene Cipl. In Plant Peroxidases Biochemistry and Physiology, Welinder, K. G., Rasmussen, S. K., Penel, C., Greppin, H., Eds.- University of Geneva: Geneva, 1993.
- Theorell, H. //The Preparation and Some Properties of Crystalline Horseradish Peroxidase. Ark. Kemi. Min. Geol. A 1942,16, pp: 1−11.
- Jones, P. L.- Dunford, H. B. J. Theor. Biol. 1977, 69, pp: 457−461.
- Chang, C. S.- Yamazaki, I.- Sinclair, R.- Khalid, S.- Powers, L. IIPH Dependence of the Active Site of Horseradish Peroxidase Compound-II. Biochemistry 1993, 32, pp: 923−928.
- Andersen, M. B.- Hsuanyu, Y.- Welinder, K. G.- Schneider, P.- Dunford, H. B. //Kinetics and Equilibria of Cyanide Binding to Coprinus Cinereus Peroxidase. Acta Chem. Scand. 1991, 45, pp: 206−211.
- Araiso, T.- Dunford, H. B. //Horseradish Peroxidase. XLI. Complex Formation With Nitrate and Its Effect Upon Compound I Formation. Biochem. Biophys. Res. Commun. 1980,94, pp: 1177−1182.
- Dunford, H. B.- Araiso, T. //Complex Formation With Nitrate and Its Effect Upon Compound I Formation. Biochem. Biophys. Res. Commun. 1979, 89, pp: 764−775.
- Sontum, S. F.- Case, D. A. //Electronic Structures of Active Site Models for Compounds I and II of Peroxidase. J. Am. Chem. Soc. 1985,107, pp: 4013−4015.
- Sivaraja, M.- Goodin, D. B.- Smith, M.- Hoffman, B. M. //Identification by ENDOR of Trpl91 As the Free-Radical Site in Cytochrome c Peroxidase Compound ES. Science 1989, 245(4919), pp: 738−740.
- Dunford, H. B.- Stillman, J. S. //On the Function and Mechanism of Action of Peroxidases. Coord. Chem. Rev. 1976,19, pp: 187−251.
- Baneijee, R. K. //Mechanism of Horse-Radish Peroxidase Catalyzed Conversion of Iodine to Iodide in the Presence of H202 and EDTA. J. Biol. Chem. 1989, 264, pp: 9188−9194.
- Du, P.- Axe, F. U.- Loew, G. H.- Canuto, S.- Zerner, M. C. //Theoretical Study on the Electronic Spectra of Model Compound II Complexes of Peroxidases. J. Am. Chem. Soc. 1991,113, w 8614−8621.
- Dordick, J. S.- Klibanov, A. M.- Marietta, M. A. //Horseradish Peroxidase Catalyzed Hydroxylations- Mechanistic Studies. Biochemistry 1986,25, pp: 2946−2951.
- Aguda, B. D.- Larter, R. //Periodic-Chaotic Sequences in a Detailed Mechanism of the Peroxidase-Oxidase Reaction. J. Am. Chem. Soc. 1991,113, pp: 79 137 916.
- Gazaryan, I.- Doseeva, V.-.- Tishkov, V.-.- Galkin, A.-. //Production and Catalytic Properties of Phe41→His and Phel43→Glu Single-Point Mutants of Horseradish Peroxidase Expressed in E-Coli. Biochemistry Moscow 1995, 60(10), pp: 1187−1192.
- Dunford, H. B. ??Horseradish Peroxidase: Structure and Kinetic Properties. In Peroxidase in Chemistry and Biology, J. Everse, K. E. E. a. M. B. G., Ed.- CRC Press: Boca Raton, Florida: 1992-pp:l-24.
- Nagano, S.- Tanaka, M.- Watanabe, Y.- Morishima, I. //Putative Hydrogen Bond Network in the Heme Distal Site of Horseradish Peroxidase. Biochemical and Biophysical Research Communications 1995, 207(1), pp: 417−423.
- Nagano, S.- Tanaka, M.- Watanabe, Y.- Morishima, I. //Catalytic Roles of the Distal Site Asparagine-Histidine Couple in Peroxidases. Biochemistry 1996, 35(45), pp: 14 251−14 258.
- Welinder, K. G.//Plant Peroxidases, Their Primary, Secondary and Tertiary Structures, and Relation to Cytochrome C Peroxidase. Eur. J. Biochem. 1985, 151, pp: 497−504.
- Kremer, M. L. //Independent Activity of Catalase Haematins. J. Theor. Biol. 1970, 29, pp: 387−394.
- Gochran, A. G.- Schultz, P. G. J. Am. Chem. Soc. 1990,112, pp: 9414−9415.
- Haschke, R. H.- Friedhof, J. M. Biochem. Biophys. Res. Commun. 1978, 80, pp: 1039−1042.
- Maranon, M. J. R.- Stillman, M. J.- Vanhuystee, R. B. //Co-Dependency of Calcium and Porphyrin for an Integrated Molecular Structure of Peanut Peroxidase A Circular Dichroism Analysis. Biochem. Biophys. Res. Commun. 1993,194, pp: 326−326.
- Chance, B. Arch. Biochem. Biophys. 1949, 21, pp: 416−430.
- Keilin, D.- Hartree, E. F. //Purification of Horseradish Peroxidase and Comparison of Its Properties With Those of Catalase and Methaemoglobin. Biochem. J. 1951, 49, pp: 88−104.
- Nakajima, R.- Yamazaki, I. J. Biol. Chem. 1980,255, pp: 2067−2072.
- Arnao, M. B.- Acosta, M.- Del Rio, J. A.- Varon, R.- Garcia-Canovas, F. //A Kinetic Study on the Suicide Inactivation of Peroxidase by Peroxide. Biochim. Biophys. Acta 1990,1041, pp: 43−47.
- Arnao, M. В.- Acosta, M.- Del Rio, J. A.- Garcia-Canovas, F. //Inactivation of Peroxidase by Hydrogen Peroxide and Its Protection by a Reductant Agent. Biochim. Biophys. Acta 1990,1038, pp: 85−89.
- Ator, M. A.- David, S. K.- De Montellano, P. R. O. //Structure and Catalytic Mechanism of Horseradish Peroxidase. Regiospecific Meso Alkylation of the Prosthetic Heme Group by Alkylhydrazines. J. Biol. Chem. 1987,262, pp: 14 954−14 960.
- Ator, M. A.- De Montellano, P. R. 0. //Protein Control of Prostetic Heme Reactivity. Reaction of Substrates. J. Biol. Chem. 1987,262, pp: 1542−1551.
- Ator, M. A.- De Montellano, P. R. 0. //Mechanism-Based (Suicide) Enzyme Inactivation. In The Enzymes-, Sigman, D. S., Boyer, P. D., Eds.- Academic Press, Inc.: San Diego, 1990- Chapter 5, pp:213−282.
- De Montellano, P. R. O. //Catalytic Sites of Hemoprotein Peroxidases. Annu. Rev. Pharmacol. Toxicol. 1992, 3289−107, pp: -107.
- Kanemox, Ю. Jl. //Кинетика и Механизм Инактивации Пероксидазы в Хемилюминесцентной Реакции Окисления Люминола в Присутствии Производных Фенола. Диссетация На Соискание Ученой Степени Кандидата Химических Наук — 1998.
- Acosta, M.- Arnao, M. В.- Del Rio, J. A.- Garcia-Canovas, F. //Inactivation of Peroxidase. In Biochemical, Molecular, and Physiological Aspects of Plant Peroxidases-, J. Lobarzewski, e. al., Ed.- Imprimerie Nationale: Geneva, 1991.
- Chance, В. //The Kinetics and Stoichiometry of the Transition From the Primary to the Secondary Peroxidase-Peroxide Complexes. Arch. Biochem. Biophys. 1952, 41, pp: 416−424.
- Adediran, S. A.- Lambeir, A.-M. //Kinetics of the Reaction of Compound II of Horseradish Peroxidase With Hydrogen Peroxide to Form Compound III. Eur. J. Biochem. 1989,186, pp: 571−576.
- Cormier, M. J.- Prichard, P. M. //An Investigation of the Mechanism of the Luminescent Peroxidation of Luminol by Stopped Flow Techniques. J. Biol. Chem. 1968,243, pp: 4706−4714.
- Akimoto, K.- Shinmen, Y.- Sumida, M.- Asami, S.- Amachi, T.- Yoshizumi, H.- Saeki, Y.- Shimizu, S.- Yamada, H. //Luminol Chemiluminescence Reaction Catalyzed by a Microbial Peroxidase. Anal. Biochem. 1990,189, pp: 182−185.
- Tanaka, M.- Ishimori, К.- Morishima, I. //Luminol Activity of Horseradish Peroxidase Mutant Mimicking a Proposed Binding Site for Luminol in Arthromyces Ramosus Peroxidase. Biochemistry 1999,38(32), pp: 1 046 310 473.
- Thorpe, G. H. G.- Williams, L. A.- Kricka, L. J.- Whitehead, T. P.- Evans, H.- Stanworth, D. R. //A Rapid Luminescently Monitored Enzyme Immunoassay for IgE. J. Immunol. Method. 1985, 79, pp: 57−63.
- Kricka, L. J.- Stott, R. A. W.- Thorpe, G. H. G. //Enhanced Chemiluminescence Enzyme Immunoassays. In Complementary Immunoassays', W.P.Collins, Ed.- Chichester, Willey: 1988.
- Andersen, M. B. //Enhancement of Peroxidase Catalyzed Oxidations. In Plant Peroxidases Biochemistry and Physiology — Welinder, K. G., Rasmussen, S. K., Penel, C., Greppin, H., Eds.- University of Geneva: Geneva, 1993.
- Ohnishi, Т.- Jamasaki, I.- Jyanagi, Т.- Nakamura, T. //EPR Investigation of Cooxidation of Two Peroxidase Substrates. Biochim. Biophys. Acta 1969, 172(3), pp: 357−359.
- Piette, L. H.- Jamasaki, I. //The Rapid Oxidation of Ascorbic
- Acid by HRP-Containing System. Biochim. Biophys. Acta 1963, 77(1), pp: 4764.
- Лебедева, О. В.- Угарова, Н. Н.- Березин, И. В. //Совместное Окисление Ферроцианида Калия и О-Дианизидина Перекисью Водорода, Катализируемое Пероксидазой Хрена. Субстрат-Субстратная Активация. Биохимия 1981, 46(7), рр: 1202−1209.
- Nakamura, М.- Nakamura, S. //One- and Two-Electron Oxidation of Luminol by Peroxidase System. Free Radical Biology & Medicine 1998,24(4), pp: 537−544.
- Merenyi, G.- Lind, J.- Eriksen, Т. E. //The Equilibrium Reaction of the Luminol Radical With Oxigen and the One-Electron-Reduction Potential of 5-Aminophtalazine-1,4-Dione. J. Phys. Chem. 1984,88(11), pp: 2320−2323.
- Hodson, M.- Jones, P. L. //Enhanced Chemiluminescence in the Peroxidase-Luminol-H 2 0 2 System: Anomalous Reactivity of Enhancer Phenols With Enzyme Intermediates. J. Biolumines. Chemilumines. 1989, 3(1), pp: 21−25.
- Кулис, Ю. Ю.- Казлаускайте, Ю. Д.- Виджюнайте, А.- Разумас, В. Й. Биохимия 1991, 56, рр: 78−84.
- Власенко, С. Б. //Кинетика реакции окисления люминола, катализируемой пероксидазами и ее использование в люминесцентном иммуноанализе. Диссетация На Соискание Ученой Степени Кандидата Химических Наук- 1989.
- Merenyi, G.- Lind, J.- Shen, X.- Eriksen, Т. E. //Oxidation Potential of Luminol. Is the Autoxidation of Singlet Organic Molecules an Oute-Sphere Electron Transfer? J. Phys. Chem. 1990, 94, pp: 748−758.
- Jansen, E. H. J. M.- Van der Berg, R. H. //High-Performance Liquid Chromatographic Investigation of Product Formation in the Horseradish Peroxidase-Enhanced Chemiluminescence of Luminol With Different Enhancers. J. Chromatogr. 1991, 566, pp: 461−469.
- Diaz.A.N.- Sanchez, F. G.- Garcia, J. A. G. //Enhancement and Inhibition of Luminol Chemiluminescence by Phenolic Acids. J. Biolumines. Chemilumines. 1995,10(3), pp: 175−184.
- Sanchez, F. G.- Diaz, A. N.- Garcia, J. A. G. //P-Phenol Derivatives As Enhancers of the Chemiluminescent Luminol-Horseradish Peroxidase-H202 Reaction: Substituent Effects. Journal of Luminescence 1995, 65(1), pp: 33−39.
- Candy, Т. E. G.- Hodgson, M.- Jones, P. L. //Kinetic and Mechanism of a Chemical Clock Reaction Based on the HRP Oxidation of Luminol. J. C. S. Perkin II1990, 8, pp: 1385−1388.
- Easton, P.- Simmonds, A. C.- Rakishev, A.- Egorov, A. M.- Candeias, L. P. //Quantitative Model of the Enhancement of Peroxidase-Induced Luminol Luminescence. J. Am. Chem. Soc. 1996,118(28), pp: 6619−6624.
- Diaz, A. N.- Sanchez, F. G.- Garcia, J. A. G. //Phenol Derivatives As Enchancers and Inhibitors of Luminol-H202-Horseradish Peroxidase Chemiluminscence. J. Biolumines. Chemilumines. 1998,13, pp: 75−84.
- Wurzberg, E.- Haas, Y. //Chemiluminescence of Luminol and Relative Compounds Under E-Beam Exitation. Absolute Chemicaland Light Yields. Chem. Phys. Lett. 1978, 55(2), pp: 250−253.
- Русин, Б. А.- Лексин, A. H. //Гидролиз и Хемилюминесценция Диазахинонов. Изв. АН СССР, сер. хим. 1982,12, рр: 2685−2692.
- Калениченко, И. Е.- Пилипенко, А. Т.- Боровский, В. А. //Константы Ионизации Фталевого Гидразида и Некоторых Его Производных. Журнал общей химии 1978,48(2), рр: 334−338.
- Русин, Б. А.//Хемилюминесценция Фталгидазидов. In Биохемилюминесценция- М., Наука: 1983-рр:69−117.
- Baxendale, J. Н. //Precusors to the Chemiluminescence of Luminol, 6-Aminophtalazine-l, 4(2H, 3H)-Dione. J. Am. Chem. Soc., Chem. Commun. 1971, 22, pp: 1489−1490.
- Baxendale, J. H. //Pulse Radiolysis Study of the Chemiluminescence From Luminol. J. Am. Chem. Soc., Farad. Trans. 1973, 69(9), pp: 1665−1667.
- Wurzberg, E.- Haas, Y. //A Pulse Radiolysis Study of the Chemiluminescence of Some Luminol-Like Molecules. J. Phys. Chem. 1979, 83(21), pp: 2687−2692.
- Merenyi, G.- Lind, J. //Oxidation and Chemiluminescence of Cyclic Hydrazides. In Proc. of the Tihamy Symposium on Radiation Chemistry, Akademiai Kiado, Budapest: 1983- Vol. l, pp:103−109.
- Merenyi, G.- Lind, J. //Role of Peroxide Intermediate in the Chemiluminescence of Luminol. A Mechanistic Study. J. Am, Chem. Soc. 1980,102(18), pp: 58 305 835.
- Lind, J.- Merenyi, G.- Eriksen, Т. E. //Chemiluminescence Mechanism of Cyclic Hydrazides Such As Luminol in Aqueous Solutions. J. Am. Chem. Soc. 1983, 105(26), pp: 7655−7661.
- Eriksen, Т. E.- Lind, J.- Merenyi, G. //Chemiluminescence of 5-Aminophtalazine-l, 4-Dione in the Presence of Hydrogen Peroxide. J. Am. Chem. Soc. 1987, 77(9), pp: 2137−2148.
- Merenyi, G.- Lind, J.- Eriksen, Т. E. //Luminol Chemiluminescence: Chemistry, Excitation, Emitter. J. Biolumines. Chemilumines. 1990, 5, pp: 53−56.
- Lind, J.- Merenyi, G. //Determination of the Chemiluminescence Quantum Yield of Luminol in Rapid Chemical Reactions. Chem. Phys. Lett. 1981, 82(2), pp: 331−334.
- Лайтинен, Г. А.- Харис, В. E. Химический Анализ- Москва: Химия: 1979- рр 624.
- Nakane, Р. К.- Kawaoi, A. //Peroxidase-Labeled Antibody a New Method of Conjugation. J. Histochem. Cytochem. 1974, 22, pp: 1084−1091.
- Sakurada, J.- Sekiguchi, R.- Sato, K.- Hosoya, T. //Kinetic and Molecular Orbital Studies on the Rate of Oxidation of Monosubstituted Phenols and Anilines by Horseradish Peroxidase Compound II. Biochemistry 1990,29, pp: 4093−4098.
- Patel, P. K.- Mondal, M. S.- Modi, S.- Behere, D. V. //Kinetic Studies on the Oxidation of Phenols by the Horseradish Peroxidase Compound II. Biochim. Biophys. Acta 1997,1339(1), pp: 79−87.
- Rodriguez-Lopez, J. N.- Lagrimini, L. M.- Thorneley, N. F. //Luminol Oxidation by Hydrogen Peroxide Catalyzed by Tobacco Anionic Peroxidase: Steady-State Luminiscence and Transient Kinetic Studies. Photochem. Photobiol. 1998, 67(1), pp: 85−90.
- Vlasenko, S. В.- Arefyev, A. A.- Klimov, A. D.- Kim, В. В.- Gorovits, E. L.- Osipov, A. P.- Gavrilova, E. M.- Yegorov, A. M. //Investigation of the Catalytic
- Mechanism of Enhanced Chemiluminescence: Immunochemical Applications of This Reaction. J. Biolumines. Chemilumines. 1989, 4, pp: 164−176.
- Kapeluich, Yu. L.- Rubtsova, M. Yu.- Egorov, A. M. //Enchanced
- Chemiluminescence Reaction Applied to the Study of Horseradish Peroxidase Stability in the Course of P-Iodophenol Oxidation. J. Biolumines. Chemilumines. 1997,12, pp: 299−308.