Reactome | Detoxification of Reactive Oxygen Species

Detoxification of Reactive Oxygen Species

Stable Identifier

R-HSA-3299685

DOI

10.3180/REACT_172715.1

Type

Pathway

Species

Homo sapiens

Compartment

cytosol, endoplasmic reticulum lumen, extracellular region, mitochondrial inner membrane, mitochondrial intermembrane space, mitochondrial matrix, peroxisomal matrix

ReviewStatus

5/5

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Detoxification of Reactive Oxygen Species

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Reactive oxygen species such as superoxide (O2.-), peroxides (ROOR), singlet oxygen, peroxynitrite (ONOO-), and hydroxyl radical (OH.) are generated by cellular processes such as respiration (reviewed in Murphy 2009, Brand 2010) and redox enzymes and are required for signaling yet they are damaging due to their high reactivity (reviewed in Imlay 2008, Buettner 2011, Kavdia 2011, Birben et al. 2012, Ray et al. 2012). Aerobic cells have defenses that detoxify reactive oxygen species by converting them to less reactive products. Superoxide dismutases convert superoxide to hydrogen peroxide and oxygen (reviewed in Fukai and Ushio-Fukai 2011). Catalase and peroxidases then convert hydrogen peroxide to water.
Humans contain 3 superoxide dismutases: SOD1 is located in the cytosol and mitochondrial intermembrane space, SOD2 is located in the mitochondrial matrix, and SOD3 is located in the extracellular region. Superoxide, a negative ion, is unable to easily cross membranes and tends to remain in the compartment where it was produced. Hydrogen peroxide, one of the products of superoxide dismutase, is able to diffuse across membranes and pass through aquaporin channels. In most cells the primary source of hydrogen peroxide is mitochondria and, once in the cytosol, hydrogen peroxide serves as a signaling molecule to regulate redox-sensitive proteins such as transcription factors, kinases, phosphatases, ion channels, and others (reviewed in Veal and Day 2011, Ray et al. 2012). Hydrogen peroxide is decomposed to water by catalase, decomposed to water plus oxidized thioredoxin by peroxiredoxins, and decomposed to water plus oxidized glutathione by glutathione peroxidases (Presnell et al. 2013).

Literature References

PubMed ID	Title	Journal	Year
22196163	Mathematical and computational models of oxidative and nitrosative stress Kavdia, M	Crit Rev Biomed Eng	2011
21453242	Superoxide dismutase in redox biology: the roles of superoxide and hydrogen peroxide Buettner, GR	Anticancer Agents Med Chem	2011
21473702	Superoxide dismutases: role in redox signaling, vascular function, and diseases Ushio-Fukai, M, Fukai, T	Antioxid. Redox Signal.	2011
19061483	How mitochondria produce reactive oxygen species Murphy, MP	Biochem. J.	2009
22286106	Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling Tsuji, Y, Huang, BW, Ray, PD	Cell. Signal.	2012
20064600	The sites and topology of mitochondrial superoxide production Brand, MD	Exp. Gerontol.	2010
23268465	Oxidative stress and antioxidant defense Kalayci, O, Birben, E, Sahiner, UM, Sackesen, C, Erzurum, S	World Allergy Organ J	2012
21375475	Hydrogen peroxide as a signaling molecule Day, A, Veal, E	Antioxid. Redox Signal.	2011
23469953	Computational insights into the role of glutathione in oxidative stress Lerche, M, Shammaa, M, Presnell, CE, Ghalib, M, Alkhateeb, SK, Bhatti, G, Numan, LS, Kavdia, M	Curr Neurovasc Res	2013