Abstract
Generation of reactive oxygen species is a physiological process that take place in every aerobic organism. Oxidative stress is defined as a disturbance in the balance between the production of free radicals and antioxidants in favor of the oxidants. The imbalance between those two fractions may potentially lead to cell damage at molecular level. Since oxidants are formed at a different rate as a normal product of aerobic metabolism, complex biochemical mechanisms are required to regulate the entire process.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Babior BM, Lambeth JD, Nauseef W (2002) The neutrophil NADPH oxidase. Arch Biochem Biophys 397(2):342–344
Bleier L, Drose S (2013) Superoxide generation by complex III: from mechanistic rationales to functional consequences. Biochim Biophys Acta 1827(11–12):1320–1331
Brand MD, Affourtit C, Esteves TC, Green K, Lambert AJ, Miwa S, Pakay JL, Parker N (2004) Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic Biol Med 37(6):755–767
Cooke MS, Evans MD, Dizdaroglu M, Lunec J (2003) Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 17(10):1195–1214
Dalle-Donne I, Aldini G, Carini M, Colombo R, Rossi R, Milzani A (2006) Protein carbonylation, cellular dysfunction, and disease progression. J Cell Mol Med 10(2):389–406
Evans MD, Dizdaroglu M, Cooke MS (2004) Oxidative DNA damage and disease: induction, repair and significance. Mutat Res 567(1):1–61
Farrera C, Fadeel B (2013) Macrophage clearance of neutrophil extracellular traps is a silent process. J Immunol 191(5):2647–2656
Halliwell B, Gutteridge JM (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219(1):1–14
Hampton MB, Kettle AJ, Winterbourn CC (1998) Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92(9):3007–3017
Han D, Williams E, Cadenas E (2001) Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem J 353(Pt 2):411–416
Haynes V, Elfering S, Traaseth N, Giulivi C (2004) Mitochondrial nitric-oxide synthase: enzyme expression, characterization, and regulation. J Bioenerg Biomembr 36(4):341–346
Jezek P, Hlavata L (2005) Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int J Biochem Cell Biol 37(12):2478–2503
Lambeth JD, Kamin H (1976) Adrenodoxin reductase. Properties of the complexes of reduced enzyme with NADP+ and NADPH. J Biol Chem 251(14):4299–4306
Lushchak VI (2007) Free radical oxidation of proteins and its relationship with functional state of organisms. Biochemistry (Mosc) 72(8):809–827
Mitchell P (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems. J Theor Biol 62(2):327–367
Morrison RT, Boyd RN (1992) Organic chemistry, 6th edn. Prentice-Hall, Englewood Cliffs
Nakaya H, Takeda Y, Tohse N, Kanno M (1992) Mechanism of the membrane depolarization induced by oxidative stress in guinea-pig ventricular cells. J Mol Cell Cardiol 24(5):523–534
Niki E, Yoshida Y, Saito Y, Noguchi N (2005) Lipid peroxidation: mechanisms, inhibition, and biological effects. Biochem Biophys Res Commun 338(1):668–676
Paselk R (2008) Biochemical toxicology. Humboldt State University. http://users.humboldt.edu/rpaselk/C451.S10/C451LecNotes/451nLec12.html. Accessed on 27 Mar 2015
Rieske JS, Maclennan DH, Coleman R (1964) Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain. Biochem Biophys Res Commun 15(4):338–344
Rom O, Avezov K, Aizenbud D, Reznick AZ (2013) Cigarette smoking and inflammation revisited. Respir Physiol Neurobiol 187(1):5–10
Schrader M, Fahimi HD (2004) Mammalian peroxisomes and reactive oxygen species. Histochem Cell Biol 122(4):383–393
Sies H (1997) Oxidative stress: oxidants and antioxidants. Exp Physiol 82(2):291–295
Takei H, Araki A, Watanabe H, Ichinose A, Sendo F (1996) Rapid killing of human neutrophils by the potent activator phorbol 12-myristate 13-acetate (PMA) accompanied by changes different from typical apoptosis or necrosis. J Leukoc Biol 59(2):229–240
Takeshita M, Tamura M, Yubisui T (1983) Microsomal electron-transport reductase activities and fatty acid elongation in rat brain. Developmental changes, regional distribution and comparison with liver activity. Biochem J 214(3):751–756
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2015 Springer International Publishing Switzerland
About this chapter
Cite this chapter
Pruchniak, M.P., Araźna, M., Demkow, U. (2015). Biochemistry of Oxidative Stress. In: Pokorski, M. (eds) Advances in Clinical Science. Advances in Experimental Medicine and Biology(), vol 878. Springer, Cham. https://doi.org/10.1007/5584_2015_161
Download citation
DOI: https://doi.org/10.1007/5584_2015_161
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-21496-2
Online ISBN: 978-3-319-21497-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)