Abstract

The main cellular source of reactive oxygen species (ROS) is mitochondrial respiratory chain and active NADPH responsible for “respiratory burst” of phagocytes. Whatsmore ROS are produced in endoplasmic reticulum, peroxisomes, with the participation of xanthine and endothelial oxidase and during autoxidation process of small molecules. Mitochondrial respiratory chain is the main cellular source of ROS. It is considered that in aerobic organisms ROS are mainly formed during normal oxygen metabolism, as byproducts of oxidative phosphorylation, during the synthesis of ATP. The intermembranous phagocyte enzyme – activated NADPH oxidase, responsible for the “respiratory burst” of phagocytes, which is another source of ROS, plays an important role in defense of organism against infections.The aim of this article is to resume actuall knowledge about structure and function of the mitochondrial electron transport chain in which ROS are the byproducts and about NADPH oxidase as well as the function of each of its components in the “respiratory burst” of phagocytes.

References

• 1. Abo A., Webb M.R., Grogan A., Segal A.W.: Activation of NADPHoxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to theplasma membrane. Biochem. J., 1994, 298: 585-591
  Google Scholar
• 2. Ackrell B.A.: Progress in understanding structure-function relationshipsin respiratory chain complex II. FEBS Lett., 2000; 466: 1-5
  Google Scholar
• 3. Adams J.D. Jr, Chang M.L., Klaidman L.: Parkinson’s disease – redoxmechanisms. Curr. Med. Chem., 2001; 8: 809-814
  Google Scholar
• 4. Adam-Vizi V., Chinopoulos C.: Bioenergetics and the formationof mitochondrial reactive oxygen species. Trends Pharmacol. Sci.,2006; 27: 639-645
  Google Scholar
• 5. Ambasta R.K., Kumar P., Griendling K.K., Schmidt H.H., BusseR.,Brandes R.P.: Direct interaction of the novel Nox proteins withp22phox is required for the formation of a functionally active NADPHoxidase. J. Biol. Chem., 2004, 279: 45935-45941
  Google Scholar
• 6. Andersen J.K.: Oxidative stress in neurodegeneration: cause orconsequence? Nat. Med., 2004; 10: 18-25
  Google Scholar
• 7. Assari T.: Chronic granulomatous disease; fundamental stages inour understanding of CGD. Med. Immunol., 2006; 21: 5:4
  Google Scholar
• 8. Babior B.M.: NADPH oxidase: an update. Blood. 1999; 93: 1464-1476
  Google Scholar
• 9. Babior B.M.: The respiratory burst of phagocytes. J. Clin. Invest.,1984; 73: 599-601
  Google Scholar
• 10. Babior B.M., Kipnes R.S., Curnutte J.T.: Biological defense mechanisms.Theproduction by leukocytes of superoxide, a potentialbactericidal agent. J. Clin. Invest., 1973; 52: 741-744
  Google Scholar
• 11. Babior B.M., Takeuchi C., Ruedi J., Gutierrez A., Wentworth P.Jr.:Investigating antibody-catalyzed ozone generation by human neutrophils.Proc. Natl. Acad. Sci. USA, 2003, 100: 3031-3034
  Google Scholar
• 12. Balaban R.S., Nemoto S., Finkel T.: Mitochondria, oxidants, andaging. Cell, 2005; 120: 483-495
  Google Scholar
• 13. Baldridge C.W., Gerard R.W.: The extra respiration of phagocytosis.Am. J. Physiol., 1933; 103: 235-236
  Google Scholar
• 14. Bánfi B., Clark R.A., Steger K., Krause K.H.: Two novel proteinsactivate superoxide generation by the NADPH oxidase NOX1. J. Biol.Chem., 2003; 278: 3510-3513
  Google Scholar
• 15. Bartosz G.: Druga twarz tlenu. Wolne rodniki w przyrodzie. Wydawnictwonaukowe PWN, 2008
  Google Scholar
• 16. Bartosz G.: Reactive oxygen species: destroyers or messengers?Biochem Pharmacol., 2009; 77: 1303-1315
  Google Scholar
• 17. Bedard K., Krause K.H.: The NOX family of ROS-generatingNADPH oxidases: physiology and pathophysiology. Physiol. Rev.,2007; 87: 245-313
  Google Scholar
• 18. Benham A.M, van Lith M., Sitia R., Braakman I.: Ero1-PDI interactions,the response to redox flux and the implications for disulfidebond formation in the mammalian endoplasmic reticulum. Philos.Trans R Soc. Lond. B Biol. Sci., 2013; 368: 20110403
  Google Scholar
• 19. Berrisford J.M., Sazanov L.A.: Structural basis for the mechanismof respiratory complex I. J. Biol. Chem., 2009; 284: 29773-29783
  Google Scholar
• 20. Bhandary B., Marahatta A., Kim H.R., Chae H.J.: An involvementof oxidative stress in endoplasmic reticulum stress and its associateddiseases. Int. J. Mol. Sci., 2012; 14: 434-456
  Google Scholar
• 21. Blum D., Torch S., Lamberg N., Nissou M.F., Benabid A.L., SadoulR., Verna J.M.: Molecular pathways involved in the neurotoxicity of6-OHDA, dopamine and MPTP: contribution to the apoptotic theoryin Parkinson’s disease. Prog Neurobiol., 2001; 65: 135-172
  Google Scholar
• 22. Bonekamp N.A., Völkl A., Fahimi H.D., Schrader M.: Reactiveoxygen species and peroxisomes: struggling for balance. Biofactors,2009; 35: 346-355
  Google Scholar
• 23. Bréchard S., Plançon S., Tschirhart E.J.: New insights into theregulation of neutrophil NADPH oxidase activity in the phagosome:a focus on the role of lipid and Ca2+ signaling. Antioxid RedoxSignal., 2013; 18: 661-676
  Google Scholar
• 24. Brunori M., Giuffrè A., Sarti P.: Cytochrome c oxidase, ligandsand electrons. J. Inorg. Biochem., 2005; 99: 324-336
  Google Scholar
• 25. Carroll J., Fearnley I.M., Skehel J.M., Shannon R.J., Hirst J., WalkerJ.E.: Bovine complex I is a complex of 45 different subunits., J.Biol. Chem., 2006; 281: 32724-32727
  Google Scholar
• 26. Cecchini G., Maklashina E., Yankovskaya V., Iverson T.M., IwataS.: Variationin proton donor/acceptor pathways in succinate:quinoneoxidoreductases. FEBS Lett., 2003; 545: 31-38
  Google Scholar
• 27. Champe P.C., Harvey R.A.: Lippicott’s Illustrated Reviews: Biochemistry3rd edition. Lippincott, Williams & Wilkins, 2005
  Google Scholar
• 28. Cheng G., Lambeth J.D.: NOXO1, regulation of lipid binding, localization,and activation of Nox1 by the Phox homology (PX) domain.J. Biol. Chem., 2004; 279: 4737-4742
  Google Scholar
• 29. Cross A.R.: p40phox participates in the activation of NADPH oxidaseby increasing the affinity of p47phox for flavocytochrome b558.Biochem. J., 2000, 349: 113-117
  Google Scholar
• 30. Cross A.R., Curnutte J.T.: The cytosolic activating factor p47phoxand p67phox have distinct roles in the regulation of electron flow inNADPH oxidase. J. Biol. Chem., 1995; 270: 6543-6548
  Google Scholar
• 31. Cross A.R, Segal A.W.: The NADPH oxidase of professional phagocytes- prototype of the NOX electron transport chain systems.Biochim. Biophys. Acta, 2004; 1657: 1-22
  Google Scholar
• 32. Dang P.M., Babior B.M., Smith R.M.: NADPH dehydrogenase activityof p67PHOX, a cytosolic subunit of the leukocyte NADPH oxidase.Biochemistry, 1999; 38: 5746-5753
  Google Scholar
• 33. Dang P.M., Morel F., Gougerot-Pocidalo M.A., El Benna J.: Phosphorylationof the NADPH oxidase component p67PHOX by ERK2and P38MAPK: selectivity of phosphorylated sites and existence ofan intramolecular regulatory domain in the tetratricopeptide-richregion. Biochemistry, 2003; 42: 4520-4526
  Google Scholar
• 34. Dang P.M., Raad H., Derkawi R.A., Boussetta T., Paclet M.H., BelambriS.A., Makni-Maalej K., Kroviarski Y., Morel F., Gougerot-PocidaloM.A., El-Benna J.: The NADPH oxidase cytosolic componentp67phox is constitutively phosphorylated in human neutrophils:Regulation by a protein tyrosine kinase, MEK1/2 and phosphatases1/2A. Biochem Pharmacol., 2011; 82: 1145-1152
  Google Scholar
• 35. Davis W.B., Mohammed B.S., Mays D.C., She Z.W., MohammedJ.R., Husney R.M., Sagone A.L.: Hydroxylation of salicylate by activatedneutrophils. Biochem. Pharmacol., 1989, 38: 4013-4019
  Google Scholar
• 36. DeLeo F.R., Burritt J.B., Yu L., Jesaitis A.J., Dinauer M.C., NauseefW.M.: Processing and maturation of flavocytochrome b558 includeincorporation of heme as a prerequisite for heterodimer assembly.J. Biol. Chem., 2000; 275: 13986-13993
  Google Scholar
• 37. Dexter D.T, Jenner P.: Parkinson disease: from pathology to moleculardisease mechanisms. Free Radic. Biol. Med., 2013; 62: 132-144
  Google Scholar
• 38. Dikalova A., Clempus R., Lassègue B., Cheng G., McCoy J., DikalovS., San Martin A., Lyle A., Weber, D.S., Weiss D., Taylor W.R., SchmidtH.H., Owens G. K., Lambeth J.D., Griendling K.K.: Nox1 overexpressionpotentiates angiotensin II-induced hypertension and vascularsmooth muscle hypertrophy in transgenic mice circulation. Circulation,2005; 112: 2668-2676
  Google Scholar
• 39. Dinauer M.C.: Chronic granulomatous disease and other disordersof phagocyte function. Hematology Am. Soc. Hematol. Educ.Program, 2005; 2005: 89-95
  Google Scholar
• 40. Dröge W.: Free radicals in the physiological control of cell function.Physiol. Rev., 2002: 82: 47-95
  Google Scholar
• 41. Dröge W.: Oxidative stress and aging. Adv. Exp. Med. Biol., 2003;543: 191-200
  Google Scholar
• 42. Dusi S., Donini M., Rossi F.: Mechanisms of NADPH oxidase activation:translocation of p40phox, Rac1 and Rac2 from the cytosolto the membranes in human neutrophils lacking p47phox or p67phox.Biochem. J., 1996; 314: 409-412
  Google Scholar
• 43. El-Benna J., Dang P.M., Gougerot-Pocidalo M.A., Marie J.C., Braut–Boucher F.: p47phox, the phagocyte NADPH oxidase/NOX2 organizer:structure, phosphorylation and implication in diseases. Exp.Mol. Med., 2009; 41: 217-225
  Google Scholar
• 44. El-Benna J., Dang P.M., Périanin A.: Peptide-based inhibitorsof the phagocyte NADPH oxidase. Biochem. Pharmacol., 2010; 80:778-785
  Google Scholar
• 45. Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A.,Xia D.: Crystallographic studies of quinol oxidation site inhibitors:a modified classification of inhibitors for the cytochrome bc1 complex.J. Mol. Biol., 2004; 341: 281-302
  Google Scholar
• 46. Ferro E., Goitre L., Retta S.F., Trabalzini L.: The interplay betweenROS and Ras GTPases: physiological and pathological implications.J. Signal Transduct., 2012; 2012: 365769
  Google Scholar
• 47. Fisher N., Meunier B.: Molecular basis of resistance to cytochromebc1 inhibitors. FEMS Yeast Res., 2008; 8: 183-192
  Google Scholar
• 48. Fontanesi F., Soto I.C., Horn D., Barrientos A.: Assembly of mitochondrialcytochrome c-oxidase, a complicated and highly regulatedcellular process. Am. J. Physiol. Cell Physiol., 2006; 291: C1129-C1147
  Google Scholar
• 49. Foubert T.R., Bleazard J.B., Burritt J.B., Gripentrog J.M., BaniulisD.,Taylor R.M., Jesaitis A.J.: Identification of a spectrally stable proteolyticfragment of human neutrophil flavocytochrome b composedof the NH2-terminal regions of gp91phox and p22phox. J. Biol. Chem.,2001; 276: 38852-38861
  Google Scholar
• 50. Fransen M., Nordgren M., Wang B., Apanasets O.: Role of peroxisomesin ROS/RNS-metabolism: implications for human disease.Biochim. Biophys. Acta, 2012; 1822: 1363-1373
  Google Scholar
• 51. Freeman J.L., Abo A., Lambeth J.D.: Rac “insert region” is a noveleffector region that is implicated in the activation of NADPH oxidase,but not PAK65. J. Biol. Chem., 1996; 271: 19794-19801
  Google Scholar
• 52. Geiszt M., Lekstrom K., Brenner S., Hewitt S.M., Dana R., MalechH.L., Leto T.L.: NAD(P)H oxidase 1, a product of differentiatedcolon epithelial cells, can partially replace glycoprotein 91phox inthe regulated production of superoxide by phagocytes. J. Immunol.,2003; 171: 299-306
  Google Scholar
• 53. Geiszt M., Lekstrom K., Witta J., Leto T.L.: Proteins homologous top47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J. Biol. Chem., 2003, 278: 20006-20012
  Google Scholar
• 54. Gorzalczany Y., Sigal N., Itan M., Lotan O., Pick E.: Targetingof Rac1 to the phagocyte membrane is sufficient for the inductionof NADPH oxidase assembly. J. Biol. Chem., 2000; 275: 40073-40081
  Google Scholar
• 55. Groemping Y., Rittinger K.: Activation and assembly of theNADPH oxidase:a structural perspective. Biochem. J., 2005; 386:401-416
  Google Scholar
• 56. Gutteridge J.M., Halliwell B.: Antioxidants: molecules, medicines,and myths. Biochem. Biophys. Res. Commun., 2010; 393: 561-564
  Google Scholar
• 57. Halliwell B.: Phagocyte-derived reactive species: salvation orsuicide? Trends Biochem. Sci., 2006; 31: 509-515
  Google Scholar
• 58. Han C.H., Lee M.H.: Activation domain in P67phox regulates thesteady state reduction of FAD in gp91phox. J. Vet. Sci., 2000; 1: 27-31
  Google Scholar
• 59. Hanna I.R., Hilenski L.L., Dikalova A., Taniyama Y., Dikalov S., LyleA., Quinn M.T., Lassègue B., Griendling K.K.: Functional associationof nox1 with p22phox in vascular smooth muscle cells. Free Radic.Biol. Med., 2004; 37: 1542-1549
  Google Scholar
• 60. Hashida S., Yuzawa S., Suzuki N.N., Fujioka Y., Takikawa T., SumimotoH., Inagaki F., Fujii H.: Binding of FAD to cytochrome b558 is facilitatedduring activation of the phagocyte NADPH oxidase, leadingto superoxide production. J. Biol. Chem., 2004; 279: 26378-26386
  Google Scholar
• 61. Hinchliffe P., Sazanov L.A.: Organization of iron-sulfur clustersin respiratory complex I. Science, 2005; 309: 771-774
  Google Scholar
• 62. Hirst J., Carroll J, Fearnley I.M., Shannon R.J., Walker J.E.: The nuclear encoded subunits of complex I from bovine heart mitochondria.Biochim. Biophys. Acta, 2003; 1604: 135-150
  Google Scholar
• 63. Holland S.M.: Chronic granulomatous disease. Hematol. Oncol.Clin. North Am., 2013; 27: 89-99
  Google Scholar
• 64. Horsefield R., Yankovskaya V., Sexton G., Whittingham W., ShiomiK., Omura S., Byrne B., Cecchini G., Iwata S.: Structural and computationalanalysis of the quinone-binding site of complex II (succinate-ubiquinoneoxidoreductase): a mechanism of electron transferand proton conduction during ubiquinone reduction. J. Biol. Chem.,2006; 281: 7309-7316
  Google Scholar
• 65. Hosler J.P.: The influence of subunit III of cytochrome c oxidaseon the D pathway, the proton exit pathway and mechanism-basedinactivation in subunit I. Biochim. Biophys. Acta, 2004; 1655: 332-339
  Google Scholar
• 66. Hunte C., Palsdottir H., Trumpower B.L.: Protonmotive pathwaysand mechanisms in the cytochrome bc1 complex. FEBS Lett.,2003; 545: 39-46
  Google Scholar
• 67. Hyslop P.A., Hinshaw D.B., Scraufstatter I.U., Cochrane C.G.,Kunz S.,Vosbeck K.: Hydrogen peroxide as a potent bacteriostaticantibiotic: implications for host defense. Free Radic. Biol. Med.,1995; 19: 31-37
  Google Scholar
• 68. Isogai Y., Iizuka T., Makino R., Iyanagi T., Orii Y.: Superoxide–producing cytochrome b. Enzymatic and electron paramagneticresonance properties of cytochrome b558 purified from neutrophils.J. Biol. Chem., 1993; 268: 4025-4031
  Google Scholar
• 69. Iyer G.Y., Islam D.M., Quastel J.H.: Biochemical aspects of phagocytosis.Nature, 1961, 192: 535-541
  Google Scholar
• 70. Kawahara T., Kuwano Y., Teshima-Kondo S., Takeya R., SumimotoH., Kishi K., Tsunawaki S., Hirayama T., Rokutan K.: Role of nicotinamideadenine dinucleotide phosphate oxidase 1 in oxidativeburst response to Toll-like receptor 5 signaling in large intestinalepithelial cells. J. Immunol., 2004; 172: 3051-3058
  Google Scholar
• 71. Kawahara T., Ritsick D., Cheng G., Lambeth J.D.: Point mutationsin the proline-rich region of p22phox are dominant inhibitorsof Nox1- and Nox2-dependent reactive oxygen generation. J. Biol.Chem., 2005; 280: 31859-31869
  Google Scholar
• 72. Klebanoff S.J.: Myeloperoxidase: friend and foe. J. Leukoc. Biol.,2005; 77: 598-625
  Google Scholar
• 73. Klebanoff S.J., Kettle A.J., Rosen H., Winterbourn C.C., NauseefW.M.: Myeloperoxidase: a front-line defender against phagocytosedmicroorganisms. J. Leukoc. Biol., 2013; 93:185-198
  Google Scholar
• 74. Kleniewska P., Piechota A., Skibska B., Gorąca A.: The NADPHoxidase family and its inhibitors. Arch. Immunol. Ther. Exp., 2012;60: 277-294
  Google Scholar
• 75. Koshkin V., Lotan O., Pick E.: The cytosolic component p47phox isnot a sine qua non participant in the activation of NADPH oxidasebut is required for optimal superoxide production. J. Biol. Chem.,1996; 271: 30326-30329
  Google Scholar
• 76. Lam G.Y., Huang J., Brumell J.H.: The many roles of NOX2 NADPHoxidase-derived ROS in immunity. Semin. Immunopathol., 2010;32: 415-430
  Google Scholar
• 77. Lambeth J.D.: Nox enzymes, ROS, and chronic disease: an exampleof antagonistic pleiotropy. Free Radic. Biol. Med., 2007; 43: 332-347
  Google Scholar
• 78. Lanza I.R., Nair K.S.: Mitochondrial function as a determinantof life span. Pflugers Arch., 2010; 459: 277-289
  Google Scholar
• 79. Lapouge K., Smith S.J., Groemping Y. Rittinger K.: Architectureof the p40-p47-p67phox complex in the resting state of the NADPHoxidase. J. Biol. Chem., 2002; 277: 10121-10128
  Google Scholar
• 80. Lefer D.J., Granger D.N.: Oxidative stress and cardiac disease.Am. J. Med., 2000; 109: 315-323
  Google Scholar
• 81. Lopes L.R., Dagher M.C., Gutierrez A., Young B., Bouin A.P., Fuchs A., Babior B.M.: Phosphorylated p40PHOX as a negative regulator ofNADPH oxidase. Biochemistry, 2004; 43: 3723-3730
  Google Scholar
• 82. Madani S., Hichami A., Legrand A., Belleville J., Khan N.A.: Implicationof acyl chain of diacylglycerols in activation of differentisoforms of protein kinase C. FASEB J., 2001; 15: 2595-2601
  Google Scholar
• 83. Malhotra J.D., Kaufman R.J.: Endoplasmic reticulum stress andoxidative stress:a vicious cycle or a double-edged sword? Antioxid.Redox Signal., 2007; 9: 2277-2293
  Google Scholar
• 84. Manivannan S., Scheckhuber C.Q., Veenhuis M., van der KleiI.J.: The impact of peroxisomes on cellular aging and death. FrontOncol., 2012; 2: 50
  Google Scholar
• 85. Marcoux J., Man P., Petit-Haertlein I., Vivès C., Forest E., FieschiF.: p47phox molecular activation for assembly of the neutrophil NADPHoxidase complex. J. Biol. Chem., 2010; 285: 28980-28990
  Google Scholar
• 86. Matsuno K., Yamada H., Iwata K., Jin, D., Katsuyama M., MatsukiM., Takai S., Yamanishi K., Miyazaki M., Matsubara H., Yabe-NishimuraC.: Nox1 is involved in angiotensin II-mediated hypertension:a study in Nox1-deficient mice. Circulation, 2005; 112: 2677-2685
  Google Scholar
• 87. Matute J.D., Arias A.A., Dinauer M.C., Patiño P.J.: p40phox: thelast NADPH oxidase subunit. Blood Cells Mol. Dis., 2005; 35: 291-302
  Google Scholar
• 88. Matute J.D., Arias A.A., Wright N.A., Wrobel I., Waterhouse C.C.,Li X.J., Marchal C.C., Stull N.D., Lewis D.B., Steele M., Kellner J.D., YuW., Meroueh S.O., Nauseef W.M., Dinauer M.C.: A new genetic subgroupof chronic granulomatous disease with autosomal recessivemutations in p40phox and selective defectsin neutrophil NADPH oxidaseactivity. Blood, 2009; 114: 3309-3315
  Google Scholar
• 89. Miyano K., Ueno N., Takeya R., Sumimoto H.: Direct involvementof the small GTPase Rac in activation of the superoxide-producingNADPH oxidase Nox1. J. Biol. Chem., 2006; 281: 21857-21868
  Google Scholar
• 90. Murphy M.P.: How mitochondria produce reactive oxygen species.Biochem. J., 2009; 417: 1-13
  Google Scholar
• 91. Musatov A., Robinson N.C.: Cholate-induced dimerization of detergent-orphospholipid-solubilized bovine cytochrome C oxidase.Biochemistry, 2002; 41: 4371-4376
  Google Scholar
• 92. Nauseef W.M.: Assembly of the phagocyte NADPH oxidase. HistochemCell Biol., 2004; 122: 277-291
  Google Scholar
• 93. Nemoto S., Takeda K., Yu Z.X., Ferrans V.J., Finkel T.: Role formitochondrial oxidants as regulators of cellular metabolism. Mol.Cell. Biol., 2000; 20: 7311-7318
  Google Scholar
• 94. Pohl T., Bauer T., Dörner K., Stolpe S., Sell P., Zocher G., FriedrichT.: Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase(complex I) is essential for stability but not involved in electrontransfer. Biochemistry, 2007; 46: 6588-6596
  Google Scholar
• 95. Rada B. Hably C., Meczner A., Timár C., Lakatos G., Enyedi P.,Ligeti E.: Role of Nox2 in elimination of microorganisms. Semin.Immunopathol., 2008; 30: 237-253
  Google Scholar
• 96. Rees M.D., Pattison D.I., Davies M.J.: Oxidation of heparan sulphateby hypochlorite: role of N-chloro derivatives and dichloramine-dependentfragmentation. Biochem. J., 2005; 391: 125-134
  Google Scholar
• 97. Rossi F., Zatti M.: Biochemical aspects of phagocytosis in polymorphonuclearleucocytes. NADH and NADPH oxidation by the granulesof resting and phagocytizing cells. Experientia, 1964; 20: 21-23
  Google Scholar
• 98. Sarfstein R., Gorzalczany Y., Mizrahi A., Berdichevsky Y., Molshanski-MorS., Weinbaum C., Hirshberg M., Dagher M.C., Pick E.:Dual role of Rac in the assembly of NADPH oxidase, tethering to themembrane and activation of p67phox: a study based on mutagenesisof p67phox-Rac1 chimeras. J. Biol. Chem., 2004; 279: 16007-16016
  Google Scholar
• 99. Segal A.W.: How neutrophils kill microbes. Annu. Rev. Immunol.,2005; 23: 197-223
  Google Scholar
• 100. Seguchi H., Kobayashi T.: Study of NADPH oxidase-activatedsites in human neutrophils. J. Electron Microsc., 2002; 51: 87-91
  Google Scholar
• 101. Shen Z., Wu W., Hazen S.L.: Activated leukocytes oxidativelydamage DNA, RNA, and the nucleotide pool through halide-dependentformation of hydroxyl radical. Biochemistry, 2000; 39: 5474-5482
  Google Scholar
• 102. Sheppard F.R., Kelher M.R., Moore E.E., McLaughlin N.J., BanerjeeA., Silliman C.C.: Structural organization of the neutrophilNADPH oxidase: phosphorylation and translocation during primingand activation. J. Leukoc. Biol., 2005; 78: 1025-1042
  Google Scholar
• 103. Shukla V., Mishra S.K., Pant H.C.: Oxidative stress in neurodegeneration.Adv. Pharmacol. Sci., 2011; 2011: 572634
  Google Scholar
• 104. Sigal N., Gorzalczany Y., Pick E.: Two pathways of activationof the superoxide-generating NADPH oxidase of phagocytes in vitro- distinctive effects of inhibitors. Inflammation, 2003; 27: 147-159
  Google Scholar
• 105. Smith R.M., Connor J.A., Chen L.M., Babior B.M.: The cytosolicsubunit p67phox contains an NADPH-binding site that participatesin catalysis by the leukocyte NADPH oxidase. J. Clin. Invest., 1996;98: 977-983
  Google Scholar
• 106. Steinbeck M.J., Khan A.U., Karnovsky M.J: Intracellular singletoxygen generation by phagocytosing neutrophils in responseto particles coated with a chemical trap. J. Biol. Chem., 1992; 267:13425-13433
  Google Scholar
• 107. Stiburek L., Hansikova H., Tesarova M., Cerna L., Zeman J.:Biogenesis of eukaryotic cytochrome c oxidase. Physiol. Res., 2006;55, Suppl. 2: S27-S41
  Google Scholar
• 108. Suh Y.A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D.,Chun A.B., Griendling K.K., Lambeth J.D.: Cell transformation bythe superoxide-generating oxidase Mox1. Nature, 1999; 401: 79-82
  Google Scholar
• 109. Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T.,Nunoi H., Sumimoto H.: Novel human homologues of p47phox andp67phox participate in activation of superoxide-producing NADPHoxidases J. Biol. Chem., 2003; 278: 25234-25246
  Google Scholar
• 110. Terlecky S.R., Terlecky L.J., Giordano C.R.: Peroxisomes, oxidativestress, and inflammation. World J. Biol. Chem., 2012; 3: 93-97
  Google Scholar
• 111. Thannickal V.J., Fanburg B.L.: Reactive oxygen species in cell signaling.Am. J. Physiol. Lung Cell Mol. Physiol., 2000: 279: L1005-L1028
  Google Scholar
• 112. Valko M., Leibfritz D., Moncol J., Cronin M.T., Mazur M., TelserJ.: Free radicals and antioxidants in normal physiological functionsand human disease. Int. J. Biochem. Cell Biol., 2007; 39: 44-84
  Google Scholar
• 113. van Bruggen R., Anthony E., Fernandez-Borja M., Roos D.: Continuoustranslocation of Rac2 and the NADPH oxidase componentp67phox during phagocytosis. J. Biol. Chem., 2004; 279: 9097-9102
  Google Scholar
• 114. Vergnaud S., Paclet M.H., El Benna J., Pocidalo M.A., Morel F.:Complementation of NADPH oxidase in p67-phox-deficient CGDpatients p67-phox/p40-phox interaction Eur. J. Biochem., 2000; 267:1059-1067
  Google Scholar
• 115. Vignais P.V. The superoxide-generating NADPH oxidase: structuralaspects and activation mechanism. Cell. Mol. Life Sci., 2002;59: 1428-1459
  Google Scholar
• 116. Wentworth P. Jr, McDunn J.E., Wentworth A.D., Takeuchi C.,Nieva J., Jones T., Bautista C., Ruedi J.M., Gutierrez A., Janda K.D.,Babior B.M., Eschenmoser A., Lerner R.A.: Evidence for antibody–catalyzed ozone formation in bacterial killing and inflammation.Science, 2002; 298: 2195-2199
  Google Scholar
• 117. Wikström M.: Proton translocation by cytochrome c oxidase:a rejoinder to recent criticism. Biochemistry, 2000; 39: 3515-3519
  Google Scholar
• 118. Winterbourn C.C.: Biological reactivity and biomarkers of theneutrophil oxidant, hypochlorous acid. Toxicology, 2002; 181-182:223-227
  Google Scholar

Full text