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class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Antioxidant_enzymes" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Antioxidant_enzymes"> <div class="vector-toc-text"> 4 Antioxidant enzymes </div> </a> <button aria-controls="toc-Antioxidant_enzymes-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> Toggle Antioxidant enzymes subsection </button> <ul id="toc-Antioxidant_enzymes-sublist" class="vector-toc-list"> <li id="toc-Superoxide_dismutase" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Superoxide_dismutase"> <div class="vector-toc-text"> 4.1 Superoxide dismutase </div> </a> <ul id="toc-Superoxide_dismutase-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Damaging_effects" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Damaging_effects"> <div 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href="#Impairment_of_cognitive_function"> <div class="vector-toc-text"> 5.3 Impairment of cognitive function </div> </a> <ul id="toc-Impairment_of_cognitive_function-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Cause_of_aging" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Cause_of_aging"> <div class="vector-toc-text"> 6 Cause of aging </div> </a> <ul id="toc-Cause_of_aging-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cancer" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Cancer"> <div class="vector-toc-text"> 7 Cancer </div> </a> <button aria-controls="toc-Cancer-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> Toggle Cancer subsection </button> <ul id="toc-Cancer-sublist" class="vector-toc-list"> <li id="toc-Carcinogenesis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Carcinogenesis"> <div class="vector-toc-text"> 7.1 Carcinogenesis </div> </a> <ul id="toc-Carcinogenesis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cell_proliferation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cell_proliferation"> <div class="vector-toc-text"> 7.2 Cell proliferation </div> </a> <ul id="toc-Cell_proliferation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cell_death" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cell_death"> <div class="vector-toc-text"> 7.3 Cell death </div> </a> <ul id="toc-Cell_death-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Tumor_cell_invasion,_angiogenesis_and_metastasis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Tumor_cell_invasion,_angiogenesis_and_metastasis"> <div class="vector-toc-text"> 7.4 Tumor cell invasion, angiogenesis and metastasis </div> </a> <ul id="toc-Tumor_cell_invasion,_angiogenesis_and_metastasis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chronic_inflammation_and_cancer" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chronic_inflammation_and_cancer"> <div class="vector-toc-text"> 7.5 Chronic inflammation and cancer </div> </a> <ul id="toc-Chronic_inflammation_and_cancer-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cancer_therapy" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cancer_therapy"> <div class="vector-toc-text"> 7.6 Cancer therapy </div> </a> <ul id="toc-Cancer_therapy-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Positive_role_of_ROS_in_memory" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Positive_role_of_ROS_in_memory"> <div class="vector-toc-text"> 8 Positive role of ROS in memory </div> </a> <ul id="toc-Positive_role_of_ROS_in_memory-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> 9 See also </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> 10 References </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Further_reading" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Further_reading"> <div class="vector-toc-text"> 11 Further reading </div> </a> <ul id="toc-Further_reading-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> 12 External links </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Toggle the table of contents </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading">Reactive oxygen species</h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 28 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-28" aria-hidden="true" > 28 languages </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-af mw-list-item"><a href="https://af.wikipedia.org/wiki/Reaktiewe_suurstofkomponent" title="Reaktiewe suurstofkomponent – Afrikaans" lang="af" hreflang="af" data-title="Reaktiewe suurstofkomponent" data-language-autonym="Afrikaans" data-language-local-name="Afrikaans" class="interlanguage-link-target">Afrikaans</a></li><li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D9%85%D8%B1%D9%83%D8%A8%D8%A7%D8%AA_%D8%A7%D9%84%D8%A3%D9%83%D8%B3%D8%AC%D9%8A%D9%86_%D8%A7%D9%84%D8%AA%D9%81%D8%A7%D8%B9%D9%84%D9%8A%D8%A9" title="مركبات الأكسجين التفاعلية – Arabic" lang="ar" hreflang="ar" data-title="مركبات الأكسجين التفاعلية" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target">العربية</a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Reaktivne_vrste_kisika" title="Reaktivne vrste kisika – Bosnian" lang="bs" hreflang="bs" data-title="Reaktivne vrste kisika" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target">Bosanski</a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Esp%C3%A8cies_reactives_de_l%27oxigen" title="Espècies reactives de l'oxigen – Catalan" lang="ca" hreflang="ca" data-title="Espècies reactives de l'oxigen" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target">Català</a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Reaktive_Sauerstoffspezies" title="Reaktive Sauerstoffspezies – German" lang="de" hreflang="de" data-title="Reaktive Sauerstoffspezies" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target">Deutsch</a></li><li class="interlanguage-link interwiki-et mw-list-item"><a href="https://et.wikipedia.org/wiki/Hapnikku_sisaldavad_reaktiivsed_osakesed" title="Hapnikku sisaldavad reaktiivsed osakesed – Estonian" lang="et" hreflang="et" data-title="Hapnikku sisaldavad reaktiivsed osakesed" data-language-autonym="Eesti" data-language-local-name="Estonian" class="interlanguage-link-target">Eesti</a></li><li class="interlanguage-link interwiki-el mw-list-item"><a href="https://el.wikipedia.org/wiki/%CE%94%CF%81%CE%B1%CF%83%CF%84%CE%B9%CE%BA%CE%AD%CF%82_%CE%BC%CE%BF%CF%81%CF%86%CE%AD%CF%82_%CE%BF%CE%BE%CF%85%CE%B3%CF%8C%CE%BD%CE%BF%CF%85" title="Δραστικές μορφές οξυγόνου – Greek" lang="el" hreflang="el" data-title="Δραστικές μορφές οξυγόνου" data-language-autonym="Ελληνικά" data-language-local-name="Greek" class="interlanguage-link-target">Ελληνικά</a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Especie_reactiva_de_ox%C3%ADgeno" title="Especie reactiva de oxígeno – Spanish" lang="es" hreflang="es" data-title="Especie reactiva de oxígeno" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target">Español</a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/D%C3%A9riv%C3%A9_r%C3%A9actif_de_l%27oxyg%C3%A8ne" title="Dérivé réactif de l'oxygène – French" lang="fr" hreflang="fr" data-title="Dérivé réactif de l'oxygène" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target">Français</a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Especie_reactiva_do_os%C3%ADxeno" title="Especie reactiva do osíxeno – Galician" lang="gl" hreflang="gl" data-title="Especie reactiva do osíxeno" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target">Galego</a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%ED%99%9C%EC%84%B1_%EC%82%B0%EC%86%8C" title="활성 산소 – Korean" lang="ko" hreflang="ko" data-title="활성 산소" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target">한국어</a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Spesi_oksigen_reaktif" title="Spesi oksigen reaktif – Indonesian" lang="id" hreflang="id" data-title="Spesi oksigen reaktif" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target">Bahasa Indonesia</a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Specie_reattive_all%27ossigeno" title="Specie reattive all'ossigeno – Italian" lang="it" hreflang="it" data-title="Specie reattive all'ossigeno" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target">Italiano</a></li><li class="interlanguage-link interwiki-ml mw-list-item"><a href="https://ml.wikipedia.org/wiki/%E0%B4%B1%E0%B4%BF%E0%B4%AF%E0%B4%BE%E0%B4%95%E0%B5%8D%E0%B4%9F%E0%B5%80%E0%B4%B5%E0%B5%8D_%E0%B4%93%E0%B4%95%E0%B5%8D%E0%B4%B8%E0%B4%BF%E0%B4%9C%E0%B5%BB_%E0%B4%B8%E0%B5%8D%E0%B4%AA%E0%B5%80%E0%B4%B7%E0%B5%80%E0%B4%B8%E0%B5%8D" title="റിയാക്ടീവ് ഓക്സിജൻ സ്പീഷീസ് – Malayalam" lang="ml" hreflang="ml" data-title="റിയാക്ടീവ് ഓക്സിജൻ സ്പീഷീസ്" data-language-autonym="മലയാളം" data-language-local-name="Malayalam" class="interlanguage-link-target">മലയാളം</a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Spesies_oksigen_reaktif" title="Spesies oksigen reaktif – Malay" lang="ms" hreflang="ms" data-title="Spesies oksigen reaktif" data-language-autonym="Bahasa Melayu" data-language-local-name="Malay" class="interlanguage-link-target">Bahasa Melayu</a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Reactieve_zuurstofcomponent" title="Reactieve zuurstofcomponent – Dutch" lang="nl" hreflang="nl" data-title="Reactieve zuurstofcomponent" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target">Nederlands</a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E6%B4%BB%E6%80%A7%E9%85%B8%E7%B4%A0" title="活性酸素 – Japanese" lang="ja" hreflang="ja" data-title="活性酸素" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target">日本語</a></li><li class="interlanguage-link interwiki-no mw-list-item"><a href="https://no.wikipedia.org/wiki/Frie_radikaler" title="Frie radikaler – Norwegian Bokmål" lang="nb" hreflang="nb" data-title="Frie radikaler" data-language-autonym="Norsk bokmål" data-language-local-name="Norwegian Bokmål" class="interlanguage-link-target">Norsk bokmål</a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Reaktywne_formy_tlenu" title="Reaktywne formy tlenu – Polish" lang="pl" hreflang="pl" data-title="Reaktywne formy tlenu" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target">Polski</a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Esp%C3%A9cie_reactiva_de_oxig%C3%A9nio" title="Espécie reactiva de oxigénio – Portuguese" lang="pt" hreflang="pt" data-title="Espécie reactiva de oxigénio" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target">Português</a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Specie_reactiv%C4%83_de_oxigen" title="Specie reactivă de oxigen – Romanian" lang="ro" hreflang="ro" data-title="Specie reactivă de oxigen" data-language-autonym="Română" data-language-local-name="Romanian" class="interlanguage-link-target">Română</a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%90%D0%BA%D1%82%D0%B8%D0%B2%D0%BD%D1%8B%D0%B5_%D1%84%D0%BE%D1%80%D0%BC%D1%8B_%D0%BA%D0%B8%D1%81%D0%BB%D0%BE%D1%80%D0%BE%D0%B4%D0%B0" title="Активные формы кислорода – Russian" lang="ru" hreflang="ru" data-title="Активные формы кислорода" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target">Русский</a></li><li class="interlanguage-link interwiki-sl mw-list-item"><a href="https://sl.wikipedia.org/wiki/Reaktivna_kisikova_spojina" title="Reaktivna kisikova spojina – Slovenian" lang="sl" hreflang="sl" data-title="Reaktivna kisikova spojina" data-language-autonym="Slovenščina" data-language-local-name="Slovenian" class="interlanguage-link-target">Slovenščina</a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/%D0%A0%D0%B5%D0%B0%D0%BA%D1%82%D0%B8%D0%B2%D0%BD%D0%B5_%D0%B2%D1%80%D1%81%D1%82%D0%B5_%D0%BA%D0%B8%D1%81%D0%B5%D0%BE%D0%BD%D0%B8%D0%BA%D0%B0" title="Реактивне врсте кисеоника – Serbian" lang="sr" hreflang="sr" data-title="Реактивне врсте кисеоника" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target">Српски / srpski</a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Reaktiva_syref%C3%B6reningar" title="Reaktiva syreföreningar – Swedish" lang="sv" hreflang="sv" data-title="Reaktiva syreföreningar" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target">Svenska</a></li><li class="interlanguage-link interwiki-tl mw-list-item"><a href="https://tl.wikipedia.org/wiki/Reactive_oxygen_species" title="Reactive oxygen species – Tagalog" lang="tl" hreflang="tl" data-title="Reactive oxygen species" data-language-autonym="Tagalog" data-language-local-name="Tagalog" class="interlanguage-link-target">Tagalog</a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%90%D0%BA%D1%82%D0%B8%D0%B2%D0%BD%D1%96_%D1%84%D0%BE%D1%80%D0%BC%D0%B8_%D0%BA%D0%B8%D1%81%D0%BD%D1%8E" title="Активні форми кисню – Ukrainian" lang="uk" hreflang="uk" data-title="Активні форми кисню" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target">Українська</a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E6%B4%BB%E6%80%A7%E6%B0%A7%E7%B1%BB" title="活性氧类 – Chinese" lang="zh" hreflang="zh" data-title="活性氧类" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target">中文</a></li> </ul> <div class="after-portlet after-portlet-lang"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q424361#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></div> </div> </div> </div> </header> <div class="vector-page-toolbar"> <div class="vector-page-toolbar-container"> <div id="left-navigation"> <nav aria-label="Namespaces"> <div id="p-associated-pages" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-associated-pages" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-nstab-main" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Reactive_oxygen_species" title="View the content page [c]" 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searchaux" style="display:none">Highly reactive molecules formed from diatomic oxygen (O₂)</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Reactive_oxygen_species_(ROS)_%E2%80%93_some_examples_with_Lewis_structures.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Reactive_oxygen_species_%28ROS%29_%E2%80%93_some_examples_with_Lewis_structures.png/220px-Reactive_oxygen_species_%28ROS%29_%E2%80%93_some_examples_with_Lewis_structures.png" decoding="async" width="220" height="140" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Reactive_oxygen_species_%28ROS%29_%E2%80%93_some_examples_with_Lewis_structures.png/330px-Reactive_oxygen_species_%28ROS%29_%E2%80%93_some_examples_with_Lewis_structures.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Reactive_oxygen_species_%28ROS%29_%E2%80%93_some_examples_with_Lewis_structures.png/440px-Reactive_oxygen_species_%28ROS%29_%E2%80%93_some_examples_with_Lewis_structures.png 2x" data-file-width="1668" data-file-height="1065" /></a><figcaption><a href="/wiki/Lewis_structure" title="Lewis structure">Lewis structure</a> of some of the reactive oxygen species. A: hydroxyl radical (<style data-mw-deduplicate="TemplateStyles:r1123817410">.mw-parser-output .template-chem2-su{display:inline-block;font-size:80%;line-height:1;vertical-align:-0.35em}.mw-parser-output .template-chem2-su>span{display:block;text-align:left}.mw-parser-output sub.template-chem2-sub{font-size:80%;vertical-align:-0.35em}.mw-parser-output sup.template-chem2-sup{font-size:80%;vertical-align:0.65em}</style>HO•); B: hydroxide ion (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">HO−); C: singlet oxygen (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">1O2); D: superoxide anion (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">O2•−); E: peroxide ion (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">O2−2); F: hydrogen peroxide (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">H2O2); G: nitric oxide (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">NO•)</figcaption></figure> In <a href="/wiki/Chemistry" title="Chemistry">chemistry</a> and <a href="/wiki/Biology" title="Biology">biology</a>, reactive oxygen species (ROS) are highly <a href="/wiki/Reactivity_(chemistry)" title="Reactivity (chemistry)">reactive</a> chemicals formed from diatomic <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">O2), <a href="/wiki/Water" title="Water">water</a>, and <a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a>. Some prominent ROS are <a href="/wiki/Hydroperoxide" title="Hydroperoxide">hydroperoxide</a> (O2H), <a href="/wiki/Superoxide" title="Superoxide">superoxide</a> (O2-),<a href="#cite_note-1">[1]</a> <a href="/wiki/Hydroxyl_radical" title="Hydroxyl radical">hydroxyl radical</a> (OH.), and <a href="/wiki/Singlet_oxygen" title="Singlet oxygen">singlet oxygen</a>.<a href="#cite_note-Halliwell2021-2">[2]</a> ROS are pervasive because they are readily produced from O2, which is abundant. ROS are important in many ways, both beneficial and otherwise. ROS function as signals, that turn on and off biological functions. They are intermediates in the redox behavior of O2, which is central to <a href="/wiki/Fuel_cell" title="Fuel cell">fuel cells</a>. ROS are central to the photodegradation of organic pollutants in the atmosphere. Most often however, ROS are discussed in a biological context, ranging from their effects on aging and their role in causing dangerous genetic mutations. <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Inventory_of_ROS">Inventory of ROS</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=1" title="Edit section: Inventory of ROS">edit</a>]</div> ROS are not uniformly defined. All sources include superoxide, singlet oxygen, and hydroxyl radical. Hydrogen peroxide is not nearly as reactive as these species, but is readily activated and is thus included.<a href="#cite_note-3">[3]</a> Peroxynitrite and <a href="/wiki/Nitric_oxide" title="Nitric oxide">nitric oxide</a> are reactive oxygen-containing species as well. <ul><li><a href="/wiki/Hydroxyl_radical" title="Hydroxyl radical">Hydroxyl radical</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">HO·) is generated by <a href="/wiki/Fenton_reaction" class="mw-redirect" title="Fenton reaction">Fenton reaction</a> of hydrogen peroxide with ferrous compounds and related reducing agents:</li></ul> <dl><dd><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">Fe(II) + H2O2 → Fe(III)OH + HO·</dd></dl> In its fleeting existence, the hydroxyl radical reacts rapidly irreversibly with all organic compounds. <ul><li><a href="/wiki/Superoxide" title="Superoxide">superoxide</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">O−2) is produced by reduction of O2.<a href="#cite_note-Turrens_2003-4">[4]</a> Several grams are produced per day in the human body within the mitochondria.<a href="#cite_note-5">[5]</a></li></ul> <dl><dd><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">O2 + e− → O−2</dd></dl> Competing with its formation, superoxide is destroyed by the action of <a href="/wiki/Superoxide_dismutase" title="Superoxide dismutase">superoxide dismutases</a>, enzymes that catalyze its disproportionation: <dl><dd><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">2 O−2 + 2H+ → O2 + H2O2</dd></dl> <ul><li><a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">H2O2) is also produced as a side product of respiration.<a href="#cite_note-Turrens_2003-4">[4]</a></li> <li><a href="/wiki/Peroxynitrite" title="Peroxynitrite">Peroxynitrite</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">ONO−2) results from the reaction of <a href="/wiki/Superoxide" title="Superoxide">superoxide</a> and <a href="/wiki/Nitric_oxide" title="Nitric oxide">nitric oxide</a>.</li> <li><a href="/wiki/Singlet_oxygen" title="Singlet oxygen">Singlet oxygen</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">1O2) is sometimes included as an ROS. <a href="/wiki/Photosensitizer" title="Photosensitizer">Photosensitizers</a> such as <a href="/wiki/Chlorophyll" title="Chlorophyll">chlorophyll</a> may convert <a href="/wiki/Triplet_oxygen" title="Triplet oxygen">triplet</a> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">3O2) to singlet oxygen:<a href="#cite_note-Laloi_2015-6">[6]</a> Singlet oxygen is highly reactive with unsaturated organic compounds. <a href="/wiki/Carotenoid" title="Carotenoid">Carotenoids</a>, <a href="/wiki/Tocopherol" title="Tocopherol">tocopherols</a>, and <a href="/wiki/Plastoquinone" title="Plastoquinone">plastoquinones</a> contained in chloroplasts quench singlet oxygen and protect against its toxic effects. Oxidized products of <a href="/wiki/%CE%92-carotene" class="mw-redirect" title="Β-carotene">β-carotene</a> arising from the presence of singlet oxygen act as <a href="/wiki/Second_messenger_system" title="Second messenger system">second messengers</a> that can either protect against singlet oxygen induced toxicity or initiate programmed cell death. Levels of <a href="/wiki/Jasmonate" title="Jasmonate">jasmonate</a> play a key role in the decision between cell acclimation or cell death in response to elevated levels of this reactive oxygen species.<a href="#cite_note-Laloi_2015-6">[6]</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="Biological_function">Biological function</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=2" title="Edit section: Biological function">edit</a>]</div> In a biological context, ROS are byproducts of the normal metabolism of <a href="/wiki/Oxygen" title="Oxygen">oxygen</a>. ROS have roles in <a href="/wiki/Cell_signaling" title="Cell signaling">cell signaling</a> and <a href="/wiki/Homeostasis" title="Homeostasis">homeostasis</a>.<a href="#cite_note-7">[7]</a><a href="#cite_note-8">[8]</a><a href="#cite_note-Devasagayam_2004_796-9">[9]</a><a href="#cite_note-10">[10]</a> ROS are intrinsic to cellular functioning, and are present at low and stationary levels in normal cells.<a href="#cite_note-11">[11]</a> In plants, ROS are involved in metabolic processes related to photoprotection and tolerance to various types of stress.<a href="#cite_note-12">[12]</a> However, ROS can cause irreversible damage to DNA as they oxidize and modify some cellular components and prevent them from performing their original functions. This suggests that ROS has a dual role; whether they will act as harmful, protective or signaling factors depends on the balance between ROS production and disposal at the right time and place.<a href="#cite_note-13">[13]</a><a href="#cite_note-14">[14]</a><a href="#cite_note-auto-15">[15]</a> In other words, oxygen toxicity can arise both from uncontrolled production and from the inefficient elimination of ROS by the antioxidant system. ROS were also demonstrated to modify the visual appearance of <a href="/wiki/Fish" title="Fish">fish</a>.<a href="#cite_note-FishInteguments-16">[16]</a> This potentially affects their behavior and ecology, such as their temperature control, their visual communication, their reproduction and survival. During times of environmental stress (e.g., <a href="/wiki/Ultraviolet_light" class="mw-redirect" title="Ultraviolet light">UV</a> or heat exposure), ROS levels can increase dramatically.<a href="#cite_note-Devasagayam_2004_796-9">[9]</a> This may result in significant damage to cell structures. Cumulatively, this is known as <a href="/wiki/Oxidative_stress" title="Oxidative stress">oxidative stress</a>. The production of ROS is strongly influenced by stress factor responses in plants, these factors that increase ROS production include drought, salinity, chilling, defense of pathogens, nutrient deficiency, metal toxicity and <a href="/wiki/UV-B" class="mw-redirect" title="UV-B">UV-B</a> radiation. ROS are also generated by exogenous sources such as <a href="/wiki/Ionizing_radiation" title="Ionizing radiation">ionizing radiation</a><a href="#cite_note-17">[17]</a> generating irreversible effects in the development of tissues in both animals and plants.<a href="#cite_note-18">[18]</a> <div class="mw-heading mw-heading2"><h2 id="Sources_of_ROS_production">Sources of ROS production</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=3" title="Edit section: Sources of ROS production">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/f8/Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg/220px-Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg" decoding="async" width="220" height="293" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/f8/Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg/330px-Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/f8/Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg/440px-Major_cellular_sources_of_Reactive_Oxygen_Species_in_living_cells.jpg 2x" data-file-width="1200" data-file-height="1600" /></a><figcaption>Major cellular sources of ROS in living non-<a href="/wiki/Photosynthesis" title="Photosynthesis">photosynthetic</a> cells. From a review by Novo and Parola, 2008.<a href="#cite_note-pmid19014652-19">[19]</a><a href="#cite_note-Nachiappan-20">[20]</a></figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Endogenous_sources">Endogenous sources</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=4" title="Edit section: Endogenous sources">edit</a>]</div> ROS are produced during the processes of respiration and photosynthesis in organelles such as <a href="/wiki/Mitochondria" class="mw-redirect" title="Mitochondria">mitochondria</a>, <a href="/wiki/Peroxisomes" class="mw-redirect" title="Peroxisomes">peroxisomes</a> and <a href="/wiki/Chloroplasts" class="mw-redirect" title="Chloroplasts">chloroplasts</a>.<a href="#cite_note-auto-15">[15]</a><a href="#cite_note-21">[21]</a><a href="#cite_note-Muller2000-22">[22]</a><a href="#cite_note-pmid11139407-23">[23]</a> During the respiration process the mitochondria convert energy for the cell into a usable form, <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">adenosine triphosphate</a> (ATP). The process of ATP production in the mitochondria, called <a href="/wiki/Oxidative_phosphorylation" title="Oxidative phosphorylation">oxidative phosphorylation</a>, involves the transport of <a href="/wiki/Protons" class="mw-redirect" title="Protons">protons</a> (hydrogen ions) across the inner mitochondrial membrane by means of the <a href="/wiki/Electron_transport_chain" title="Electron transport chain">electron transport chain</a>. In the electron transport chain, electrons are passed through a series of <a href="/wiki/Protein" title="Protein">proteins</a> via oxidation-reduction reactions, with each acceptor <a href="/wiki/Protein" title="Protein">protein</a> along the chain having a greater reduction potential than the previous. The last destination for an electron along this chain is an oxygen molecule. In normal conditions, the oxygen is reduced to produce water; however, in about 0.1–2% of electrons passing through the chain (this number derives from studies in isolated mitochondria, though the exact rate in live organisms is yet to be fully agreed upon), oxygen is instead prematurely and incompletely reduced to give the <a href="/wiki/Superoxide_radical" class="mw-redirect" title="Superoxide radical">superoxide radical</a> (•O− 2), most well documented for <a href="/wiki/Complex_I" class="mw-redirect" title="Complex I">Complex I</a> and <a href="/wiki/Complex_III" class="mw-redirect" title="Complex III">Complex III</a>.<a href="#cite_note-pmid23442817-24">[24]</a> Another source of ROS production in animal cells is the electron transfer reactions catalyzed by the mitochondrial <a href="/wiki/P450" class="mw-redirect" title="P450">P450</a> systems in <a href="/wiki/Steroidogenic" class="mw-redirect" title="Steroidogenic">steroidogenic</a> tissues.<a href="#cite_note-1993-Hanukoglu-25">[25]</a> These P450 systems are dependent on the transfer of electrons from <a href="/wiki/NADPH" class="mw-redirect" title="NADPH">NADPH</a> to P450. During this process, some electrons "leak" and react with O2 producing superoxide. To cope with this natural source of ROS, the steroidogenic tissues, ovary and testis, have a large concentration of <a href="/wiki/Antioxidant" title="Antioxidant">antioxidants</a> such as <a href="/wiki/Vitamin_C" title="Vitamin C">vitamin C</a> (ascorbate) and <a href="/wiki/%CE%92-carotene" class="mw-redirect" title="Β-carotene">β-carotene</a> and anti-oxidant enzymes.<a href="#cite_note-2006-Hanukoglu-26">[26]</a> If too much damage is present in mitochondria, a cell undergoes <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a> or programmed cell death.<a href="#cite_note-27">[27]</a><a href="#cite_note-28">[28]</a> In addition, ROS are produced in immune cell signaling via the <a href="/wiki/NADPH_oxidase" title="NADPH oxidase">NOX</a> pathway. Phagocytic cells such as <a href="/wiki/Neutrophils" class="mw-redirect" title="Neutrophils">neutrophils</a>, <a href="/wiki/Eosinophils" class="mw-redirect" title="Eosinophils">eosinophils</a>, and mononuclear <a href="/wiki/Phagocyte" title="Phagocyte">phagocytes</a> produce ROS when stimulated.<a href="#cite_note-Functions_of_ROS_in_Macrophages_and-29">[29]</a><a href="#cite_note-30">[30]</a> In <a href="/wiki/Chloroplasts" class="mw-redirect" title="Chloroplasts">chloroplasts</a>, the <a href="/wiki/Carboxylation" title="Carboxylation">carboxylation</a> and oxygenation reactions catalyzed by <a href="/wiki/Rubisco" class="mw-redirect" title="Rubisco">rubisco</a> ensure that the functioning of the electron transport chain (ETC) occurs in an environment rich in O2. The leakage of electrons in the ETC will inevitably produce ROS within the chloroplasts.<a href="#cite_note-auto-15">[15]</a> ETC in photosystem I (PSI) was once believed to be the only source of ROS in chloroplasts. The flow of electrons from the excited reaction centers is directed to the <a href="/wiki/NADP" class="mw-redirect" title="NADP">NADP</a> and these are reduced to NADPH, and then they enter the <a href="/wiki/Calvin_cycle" title="Calvin cycle">Calvin cycle</a> and reduce the final electron acceptor, CO2.<a href="#cite_note-31">[31]</a> In cases where there is an ETC overload, part of the electron flow is diverted from <a href="/wiki/Ferredoxin" title="Ferredoxin">ferredoxin</a> to O2, forming the superoxide free radical (by the <a href="/wiki/Mehler_reaction" title="Mehler reaction">Mehler reaction</a>). In addition, electron leakage to O2 can also occur from the 2Fe-2S and 4Fe-4S clusters in the PSI ETC. However, PSII also provides electron leakage locations (QA, QB) for O2-producing O2-.<a href="#cite_note-auto2-32">[32]</a><a href="#cite_note-33">[33]</a> Superoxide (O2-) is generated from PSII, instead of PSI; QB is shown as the location for the generation of O2•-.<a href="#cite_note-auto2-32">[32]</a> <div class="mw-heading mw-heading3"><h3 id="Exogenous_sources">Exogenous sources</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=5" title="Edit section: Exogenous sources">edit</a>]</div> The formation of ROS can be stimulated by a variety of agents such as pollutants, <a href="/wiki/Heavy_metals" class="mw-redirect" title="Heavy metals">heavy metals</a>,<a href="#cite_note-Nachiappan-20">[20]</a> <a href="/wiki/Tobacco" title="Tobacco">tobacco</a>, smoke, drugs, <a href="/wiki/Xenobiotics" class="mw-redirect" title="Xenobiotics">xenobiotics</a>, <a href="/wiki/Microplastics" title="Microplastics">microplastics</a>, or radiation. In plants, in addition to the action of dry <a href="/wiki/Abiotic_factor" class="mw-redirect" title="Abiotic factor">abiotic factors</a>, high temperature, interaction with other living beings can influence the production of ROS.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] Ionizing radiation can generate damaging intermediates through the interaction with water, a process termed <a href="/wiki/Radiolysis" title="Radiolysis">radiolysis</a>. Since water comprises 55–60% of the human body, the probability of radiolysis is quite high under the presence of ionizing radiation. In the process, water loses an electron and becomes highly reactive. Then through a three-step chain reaction, water is sequentially converted to <a href="/wiki/Hydroxyl_radical" title="Hydroxyl radical">hydroxyl radical</a> (•OH), <a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a> (H2O2), <a href="/wiki/Superoxide_radical" class="mw-redirect" title="Superoxide radical">superoxide radical</a> (•O− 2), and ultimately <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> (O2).[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] The <a href="/wiki/Hydroxyl_radical" title="Hydroxyl radical">hydroxyl radical</a> is extremely reactive and immediately removes electrons from any molecule in its path, turning that molecule into a free radical and thus propagating a chain reaction. However, <a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a> is actually more damaging to DNA than the hydroxyl radical, since the lower reactivity of hydrogen peroxide provides enough time for the molecule to travel into the nucleus of the cell, subsequently reacting with macromolecules such as DNA.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] In plants, the production of ROS occurs during events of abiotic stress that lead to a reduction or interruption of metabolic activity. For example, the increase in temperature, drought are factors that limit the availability of CO2 due to <a href="/wiki/Stomata" class="mw-redirect" title="Stomata">stomatal</a> closure, increasing the production of ROS, such as O2·- and 1O2 in chloroplasts.<a href="#cite_note-34">[34]</a><a href="#cite_note-auto1-35">[35]</a> The production of 1O2 in chloroplasts can cause reprogramming of the expression of nucleus genes leading to <a href="/wiki/Chlorosis" title="Chlorosis">chlorosis</a> and <a href="/wiki/Apoptosis" title="Apoptosis">programmed cell death</a>.<a href="#cite_note-auto1-35">[35]</a> In cases of biotic stress, the generation of ROS occurs quickly and weakly initially and then becomes more solid and lasting.<a href="#cite_note-36">[36]</a> The first phase of ROS accumulation is associated with plant infection and is probably independent of the synthesis of new ROS-generating <a href="/wiki/Enzyme" title="Enzyme">enzymes</a>. However, the second phase of ROS accumulation is associated only with infection by non-virulent pathogens and is an induced response dependent on increased <a href="/wiki/MRNA" class="mw-redirect" title="MRNA">mRNA</a> transcription encoding enzymes. <div class="mw-heading mw-heading2"><h2 id="Antioxidant_enzymes">Antioxidant enzymes</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=6" title="Edit section: Antioxidant enzymes">edit</a>]</div> <div class="mw-heading mw-heading3"><h3 id="Superoxide_dismutase">Superoxide dismutase</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=7" title="Edit section: Superoxide dismutase">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Superoxide_dismutase" title="Superoxide dismutase">Superoxide dismutase</a></div> <a href="/wiki/Superoxide_dismutase" title="Superoxide dismutase">Superoxide dismutases</a> (SOD) are a class of enzymes that catalyzes the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important <a href="/wiki/Antioxidant" title="Antioxidant">antioxidant</a> defense in nearly all cells exposed to oxygen. In mammals and most chordates, three forms of superoxide dismutase are present. SOD1 is located primarily in the cytoplasm, SOD2 in the mitochondria and SOD3 is extracellular. The first is a dimer (consists of two units), while the others are tetramers (four subunits). SOD1 and SOD3 contain copper and zinc ions, while SOD2 has a manganese ion in its reactive centre. The genes are located on chromosomes 21, 6, and 4, respectively (21q22.1, 6q25.3 and 4p15.3-p15.1).[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] The SOD-catalysed <a href="/wiki/Dismutation" class="mw-redirect" title="Dismutation">dismutation</a> of <a href="/wiki/Superoxide" title="Superoxide">superoxide</a> may be written with the following half-reactions: <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\begin{aligned}&{\ce {M}}^{(n+1)+}+{\ce {O2- ->[SOD]}}\ {\ce {M}}^{n+}+{\ce {O2}}\\&{\ce {M}}^{n+}+{\ce {O2- + 2H+ ->[] [SOD]}}\ {\ce {M}}^{(n+1)+}+{\ce {H2O2}}\end{aligned}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mtable columnalign="right left right left right left right left right left right left" rowspacing="3pt" columnspacing="0em 2em 0em 2em 0em 2em 0em 2em 0em 2em 0em" displaystyle="true"> <mtr> <mtd /> <mtd> <msup> <mrow class="MJX-TeXAtom-ORD"> <mtext>M</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">(</mo> <mi>n</mi> <mo>+</mo> <mn>1</mn> <mo stretchy="false">)</mo> <mo>+</mo> </mrow> </msup> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </msubsup> <mrow class="MJX-TeXAtom-REL"> <mover> <mo>→</mo> <mpadded width="+0.611em" lspace="0.278em" voffset=".15em"> <mi>S</mi> <mi>O</mi> <mi>D</mi> </mpadded> </mover> </mrow> </mrow> <mtext> </mtext> <msup> <mrow class="MJX-TeXAtom-ORD"> <mtext>M</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mi>n</mi> <mo>+</mo> </mrow> </msup> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> </mrow> </mtd> </mtr> <mtr> <mtd /> <mtd> <msup> <mrow class="MJX-TeXAtom-ORD"> <mtext>M</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mi>n</mi> <mo>+</mo> </mrow> </msup> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </msubsup> <mo>+</mo> <mn>2</mn> <mspace width="thinmathspace" /> <msup> <mtext>H</mtext> <mrow class="MJX-TeXAtom-ORD"> <mo>+</mo> </mrow> </msup> <mo stretchy="false">⟶</mo> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>SOD</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> <mtext> </mtext> <msup> <mrow class="MJX-TeXAtom-ORD"> <mtext>M</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">(</mo> <mi>n</mi> <mo>+</mo> <mn>1</mn> <mo stretchy="false">)</mo> <mo>+</mo> </mrow> </msup> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <msubsup> <mtext>H</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> </mrow> </mtd> </mtr> </mtable> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\begin{aligned}&{\ce {M}}^{(n+1)+}+{\ce {O2- ->[SOD]}}\ {\ce {M}}^{n+}+{\ce {O2}}\\&{\ce {M}}^{n+}+{\ce {O2- + 2H+ ->[] [SOD]}}\ {\ce {M}}^{(n+1)+}+{\ce {H2O2}}\end{aligned}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/bbfbaf04f7e7f9d30462802e9722ec06e07e20dd" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.102ex; margin-top: -0.408ex; margin-bottom: -0.236ex; width:47.537ex; height:8.009ex;" alt="{\displaystyle {\begin{aligned}&{\ce {M}}^{(n+1)+}+{\ce {O2- ->[SOD]}}\ {\ce {M}}^{n+}+{\ce {O2}}\\&{\ce {M}}^{n+}+{\ce {O2- + 2H+ ->[] [SOD]}}\ {\ce {M}}^{(n+1)+}+{\ce {H2O2}}\end{aligned}}}"></dd></dl> where M = <a href="/wiki/Copper" title="Copper">Cu</a> (n = 1); <a href="/wiki/Manganese" title="Manganese">Mn</a> (n = 2); <a href="/wiki/Iron" title="Iron">Fe</a> (n = 2); <a href="/wiki/Nickel" title="Nickel">Ni</a> (n = 2). In this reaction the <a href="/wiki/Oxidation_state" title="Oxidation state">oxidation state</a> of the metal cation oscillates between n and n + 1. <a href="/wiki/Catalase" title="Catalase">Catalase</a>, which is concentrated in <a href="/wiki/Peroxisomes" class="mw-redirect" title="Peroxisomes">peroxisomes</a> located next to mitochondria, reacts with the hydrogen peroxide to catalyze the formation of water and oxygen. <a href="/wiki/Glutathione_peroxidase" title="Glutathione peroxidase">Glutathione peroxidase</a> reduces hydrogen peroxide by transferring the energy of the reactive peroxides to a sulfur-containing <a href="/wiki/Tripeptide" title="Tripeptide">tripeptide</a> called <a href="/wiki/Glutathione" title="Glutathione">glutathione</a>. The sulfur contained in these enzymes acts as the reactive center, carrying reactive electrons from the peroxide to the glutathione. <a href="/wiki/Peroxiredoxins" class="mw-redirect" title="Peroxiredoxins">Peroxiredoxins</a> also degrade <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410">H2O2, within the mitochondria, cytosol, and nucleus. <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\begin{aligned}&{\ce {2H2O2->[{\text{catalase}}]2H2O{}+O2}}\\&{\ce {2GSH{}+H2O2->[][{\text{glutathione}} \atop {\text{peroxidase}}]GS-SG{}+2H2O}}\end{aligned}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mtable columnalign="right left right left right left right left right left right left" rowspacing="3pt" columnspacing="0em 2em 0em 2em 0em 2em 0em 2em 0em 2em 0em" displaystyle="true"> <mtr> <mtd /> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> <mspace width="thinmathspace" /> <msubsup> <mtext>H</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <mrow class="MJX-TeXAtom-REL"> <mover> <mo>→</mo> <mpadded width="+0.611em" lspace="0.278em" voffset=".15em"> <mrow class="MJX-TeXAtom-ORD"> <mtext>catalase</mtext> </mrow> </mpadded> </mover> </mrow> <mn>2</mn> <mspace width="thinmathspace" /> <msubsup> <mtext>H</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> </mrow> <mo>+</mo> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> </mrow> </mtd> </mtr> <mtr> <mtd /> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> <mspace width="thinmathspace" /> <mtext>GSH</mtext> <mrow class="MJX-TeXAtom-ORD"> </mrow> <mo>+</mo> <msubsup> <mtext>H</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <msubsup> <mtext>O</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <mrow class="MJX-TeXAtom-REL"> <munderover> <mo>→</mo> <mpadded width="+0.611em" lspace="0.278em" voffset="-.24em"> <mfrac linethickness="0"> <mrow class="MJX-TeXAtom-ORD"> <mtext>glutathione</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mtext>peroxidase</mtext> </mrow> </mfrac> </mpadded> <mpadded width="+0.611em" lspace="0.278em" voffset=".15em" /> </munderover> </mrow> <mtext>GS</mtext> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mtext>SG</mtext> <mrow class="MJX-TeXAtom-ORD"> </mrow> <mo>+</mo> <mn>2</mn> <mspace width="thinmathspace" /> <msubsup> <mtext>H</mtext> <mrow class="MJX-TeXAtom-ORD"> <mn>2</mn> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> <mtext>O</mtext> </mrow> </mtd> </mtr> </mtable> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\begin{aligned}&{\ce {2H2O2->[{\text{catalase}}]2H2O{}+O2}}\\&{\ce {2GSH{}+H2O2->[][{\text{glutathione}} \atop {\text{peroxidase}}]GS-SG{}+2H2O}}\end{aligned}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/699aacd6aea04d8ae2454398770976661e745d19" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -4.311ex; margin-top: -0.365ex; margin-bottom: -0.527ex; width:42.472ex; height:10.676ex;" alt="{\displaystyle {\begin{aligned}&{\ce {2H2O2->[{\text{catalase}}]2H2O{}+O2}}\\&{\ce {2GSH{}+H2O2->[][{\text{glutathione}} \atop {\text{peroxidase}}]GS-SG{}+2H2O}}\end{aligned}}}"></dd></dl> <div class="mw-heading mw-heading2"><h2 id="Damaging_effects">Damaging effects</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=8" title="Edit section: Damaging effects">edit</a>]</div> <figure class="mw-halign-right" typeof="mw:File/Frame"><a href="/wiki/File:Free_Radical_Toxicity.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/7/7c/Free_Radical_Toxicity.svg/603px-Free_Radical_Toxicity.svg.png" decoding="async" width="603" height="652" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/7c/Free_Radical_Toxicity.svg/905px-Free_Radical_Toxicity.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/7c/Free_Radical_Toxicity.svg/1206px-Free_Radical_Toxicity.svg.png 2x" data-file-width="603" data-file-height="652" /></a><figcaption>Free radical mechanisms in tissue injury. Free radical toxicity induced by xenobiotics and the subsequent detoxification by cellular enzymes (termination).</figcaption></figure> Effects of ROS on cell metabolism are well documented in a variety of species.<a href="#cite_note-Nachiappan-20">[20]</a> These include not only roles in <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a> (programmed cell death) but also positive effects such as the induction of host defence<a href="#cite_note-37">[37]</a><a href="#cite_note-38">[38]</a> <a href="/wiki/Genes" class="mw-redirect" title="Genes">genes</a> and mobilization of <a href="/wiki/Ion_transporter" title="Ion transporter">ion transporters</a>.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] This implicates them in control of cellular function. In particular, <a href="/wiki/Platelets" class="mw-redirect" title="Platelets">platelets</a> involved in <a href="/wiki/Wound" title="Wound">wound</a> repair and <a href="/wiki/Blood" title="Blood">blood</a> <a href="/wiki/Homeostasis" title="Homeostasis">homeostasis</a> release ROS to recruit additional platelets to sites of <a href="/wiki/Injury" title="Injury">injury</a>. These also provide a link to the adaptive <a href="/wiki/Immune_system" title="Immune system">immune system</a> via the recruitment of <a href="/wiki/Leukocyte" class="mw-redirect" title="Leukocyte">leukocytes</a>.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] Reactive oxygen species are implicated in cellular activity to a variety of inflammatory responses including <a href="/wiki/Cardiovascular_disease" title="Cardiovascular disease">cardiovascular disease</a>. They may also be involved in <a href="/wiki/Hearing_impairment" class="mw-redirect" title="Hearing impairment">hearing impairment</a> via <a href="/wiki/Cochlea" title="Cochlea">cochlear</a> damage induced by <a href="/wiki/Noise_health_effects" class="mw-redirect" title="Noise health effects">elevated sound levels</a>, in <a href="/wiki/Ototoxicity" title="Ototoxicity">ototoxicity</a> of drugs such as <a href="/wiki/Cisplatin" title="Cisplatin">cisplatin</a>, and in congenital deafness in both animals and humans.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] ROS are also implicated in mediation of <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a> or programmed cell death and <a href="/wiki/Ischaemic" class="mw-redirect" title="Ischaemic">ischaemic</a> injury. Specific examples include <a href="/wiki/Stroke" title="Stroke">stroke</a> and <a href="/wiki/Myocardial_infarction" title="Myocardial infarction">heart attack</a>.[<a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed">citation needed</a>] In general, the harmful effects of reactive oxygen species on the cell are the damage of DNA or RNA, oxidation of polyunsaturated fatty acids in lipids (<a href="/wiki/Lipid_peroxidation" title="Lipid peroxidation">lipid peroxidation</a>), oxidation of amino acids in proteins, and oxidative deactivation of specific enzymes by oxidation co-factors.<a href="#cite_note-39">[39]</a> <div class="mw-heading mw-heading3"><h3 id="Pathogen_response">Pathogen response</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=9" title="Edit section: Pathogen response">edit</a>]</div> When a plant recognizes an attacking pathogen, one of the first induced reactions is to rapidly produce <a href="/wiki/Superoxide" title="Superoxide">superoxide</a> (O− 2) or <a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a> (H 2O 2) to strengthen the cell wall. This prevents the spread of the pathogen to other parts of the plant, essentially forming a net around the pathogen to restrict movement and reproduction. In the mammalian host, ROS is induced as an antimicrobial defense.<a href="#cite_note-Functions_of_ROS_in_Macrophages_and-29">[29]</a> To highlight the importance of this defense, individuals with <a href="/wiki/Chronic_granulomatous_disease" title="Chronic granulomatous disease">chronic granulomatous disease</a> who have deficiencies in generating ROS, are highly susceptible to infection by a broad range of microbes including <a href="/wiki/Salmonella_enterica" title="Salmonella enterica">Salmonella enterica</a>, <a href="/wiki/Staphylococcus_aureus" title="Staphylococcus aureus">Staphylococcus aureus</a>, <a href="/wiki/Serratia_marcescens" title="Serratia marcescens">Serratia marcescens</a>, and <a href="/wiki/Aspergillus" title="Aspergillus">Aspergillus</a> spp. Studies on the <a href="/wiki/Homeostasis" title="Homeostasis">homeostasis</a> of the <a href="/wiki/Drosophila_melanogaster" title="Drosophila melanogaster">Drosophila melanogaster</a>'s intestines have shown the production of ROS as a key component of the immune response in the gut of the fly. ROS acts both as a bactericide, damaging the bacterial DNA, RNA and proteins, as well as a signalling molecule that induces repair mechanisms of the <a href="/wiki/Epithelium" title="Epithelium">epithelium</a>.<a href="#cite_note-40">[40]</a> The <a href="/wiki/Uracil" title="Uracil">uracil</a> released by microorganism triggers the production and activity of DUOX, the ROS-producing enzyme in the intestine. DUOX activity is induced according to the level of uracil in the gut; under basal conditions, it is down-regulated by the protein kinase <a href="/wiki/Mitogen-activated_protein_kinase" title="Mitogen-activated protein kinase">MkP3</a>. The tight regulation of DUOX avoids excessive production of ROS and facilitates differentiation between benign and damage-inducing microorganisms in the gut.<a href="#cite_note-41">[41]</a> The manner in which ROS defends the host from invading microbe is not fully understood. One of the more likely modes of defense is damage to microbial DNA. Studies using Salmonella demonstrated that DNA repair mechanisms were required to resist killing by ROS. A role for ROS in antiviral defense mechanisms has been demonstrated via Rig-like helicase-1 and mitochondrial antiviral signaling protein. Increased levels of ROS potentiate signaling through this mitochondria-associated antiviral receptor to activate interferon regulatory factor (IRF)-3, IRF-7, and nuclear factor kappa B (NF-κB), resulting in an antiviral state.<a href="#cite_note-pmid21597473-42">[42]</a> Respiratory epithelial cells induce mitochondrial ROS in response to influenza infection. This induction of ROS led to the induction of type III interferon and the induction of an antiviral state, limiting viral replication.<a href="#cite_note-pmid23786562-43">[43]</a> In host defense against mycobacteria, ROS play a role, although direct killing is likely not the key mechanism; rather, ROS likely affect ROS-dependent signalling controls, such as cytokine production, autophagy, and granuloma formation.<a href="#cite_note-44">[44]</a><a href="#cite_note-45">[45]</a> Reactive oxygen species are also implicated in activation, <a href="/wiki/Clonal_anergy" title="Clonal anergy">anergy</a> and apoptosis of <a href="/wiki/T_cells" class="mw-redirect" title="T cells">T cells</a>.<a href="#cite_note-46">[46]</a> <div class="mw-heading mw-heading3"><h3 id="Oxidative_damage">Oxidative damage</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=10" title="Edit section: Oxidative damage">edit</a>]</div> In <a href="/wiki/Aerobic_organism" title="Aerobic organism">aerobic organisms</a> the energy needed to fuel biological functions is produced in the <a href="/wiki/Mitochondria" class="mw-redirect" title="Mitochondria">mitochondria</a> via the <a href="/wiki/Electron_transport_chain" title="Electron transport chain">electron transport chain</a>. Reactive oxygen species (ROS) with the potential to cause <a href="/wiki/Cell_(biology)" title="Cell (biology)">cellular</a> damage are produced along with the release of energy. ROS can damage lipids, <a href="/wiki/DNA" title="DNA">DNA</a>, <a href="/wiki/RNA" title="RNA">RNA</a>, and proteins, which, in theory, contributes to the <a href="/wiki/Physiology" title="Physiology">physiology</a> of <a href="/wiki/Aging" class="mw-redirect" title="Aging">aging</a>. ROS are produced as a normal product of <a href="/wiki/Cellular_metabolism" class="mw-redirect" title="Cellular metabolism">cellular metabolism</a>. In particular, one major contributor to oxidative damage is <a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a> (H2O2), which is converted from <a href="/wiki/Superoxide" title="Superoxide">superoxide</a> that leaks from the mitochondria. <a href="/wiki/Catalase" title="Catalase">Catalase</a> and <a href="/wiki/Superoxide_dismutase" title="Superoxide dismutase">superoxide dismutase</a> ameliorate the damaging effects of hydrogen peroxide and superoxide, respectively, by converting these compounds into <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> and <a href="/wiki/Hydrogen_peroxide" title="Hydrogen peroxide">hydrogen peroxide</a> (which is later converted to water), resulting in the production of <a href="/wiki/Benign" class="mw-redirect" title="Benign">benign</a> <a href="/wiki/Molecule" title="Molecule">molecules</a>. However, this conversion is not 100% efficient, and residual peroxides persist in the cell. While ROS are produced as a product of normal cellular functioning, excessive amounts can cause deleterious effects.<a href="#cite_note-isbn0-8247-1723-6-47">[47]</a> <div class="mw-heading mw-heading3"><h3 id="Impairment_of_cognitive_function">Impairment of cognitive function</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=11" title="Edit section: Impairment of cognitive function">edit</a>]</div> Memory capabilities decline with age, evident in human degenerative diseases such as <a href="/wiki/Alzheimer%27s_disease" title="Alzheimer's disease">Alzheimer's disease</a>, which is accompanied by an accumulation of oxidative damage. Current studies demonstrate that the accumulation of ROS can decrease an organism's <a href="/wiki/Physical_fitness" title="Physical fitness">fitness</a> because oxidative damage is a contributor to senescence. In particular, the accumulation of oxidative damage may lead to cognitive dysfunction, as demonstrated in a study in which old rats were given mitochondrial <a href="/wiki/Metabolite" title="Metabolite">metabolites</a> and then given <a href="/wiki/Cognitive_tests" class="mw-redirect" title="Cognitive tests">cognitive tests</a>. Results showed that the <a href="/wiki/Rat" title="Rat">rats</a> performed better after receiving the metabolites, suggesting that the metabolites reduced oxidative damage and improved mitochondrial function.<a href="#cite_note-pmid11854529-48">[48]</a> Accumulating oxidative damage can then affect the efficiency of mitochondria and further increase the rate of ROS production.<a href="#cite_note-pmid1355616-49">[49]</a> The accumulation of oxidative damage and its implications for aging depends on the particular <a href="/wiki/Tissue_(biology)" title="Tissue (biology)">tissue</a> type where the damage is occurring. Additional experimental results suggest that oxidative damage is responsible for age-related decline in <a href="/wiki/Brain" title="Brain">brain</a> functioning. Older <a href="/wiki/Gerbil" class="mw-redirect" title="Gerbil">gerbils</a> were found to have higher levels of oxidized protein in comparison to younger gerbils. Treatment of old and young <a href="/wiki/Mice" class="mw-redirect" title="Mice">mice</a> with a <a href="/wiki/Spin_trapping" title="Spin trapping">spin trapping</a> compound caused a decrease in the level of oxidized proteins in older gerbils but did not have an effect on younger gerbils. In addition, older gerbils performed cognitive tasks better during treatment but ceased functional capacity when treatment was discontinued, causing oxidized protein levels to increase. This led researchers to conclude that oxidation of cellular proteins is potentially important for brain function.<a href="#cite_note-CarneyStarke-Reed1991-50">[50]</a> <div class="mw-heading mw-heading2"><h2 id="Cause_of_aging">Cause of aging</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=12" title="Edit section: Cause of aging">edit</a>]</div> According to the <a href="/wiki/Free_radical_theory_of_aging" class="mw-redirect" title="Free radical theory of aging">free radical theory of aging</a>, oxidative damage initiated by reactive oxygen species is a major contributor to the functional decline that is characteristic of aging. While studies in invertebrate models indicate that animals genetically engineered to lack specific antioxidant enzymes (such as SOD), in general, show a shortened lifespan (as one would expect from the theory), the converse manipulation, increasing the levels of antioxidant enzymes, has yielded inconsistent effects on lifespan (though some studies in <a href="/wiki/Drosophila" title="Drosophila">Drosophila</a> do show that lifespan can be increased by the overexpression of MnSOD or glutathione biosynthesizing enzymes). Also contrary to this theory, deletion of <a href="/wiki/SOD2" title="SOD2">mitochondrial SOD2</a> can extend lifespan in <a href="/wiki/Caenorhabditis_elegans" title="Caenorhabditis elegans">Caenorhabditis elegans</a>.<a href="#cite_note-pmid19197346-51">[51]</a> In mice, the story is somewhat similar. Deleting antioxidant enzymes, in general, yields shorter lifespan, although overexpression studies have not (with some exceptions) consistently extended lifespan.<a href="#cite_note-pmid17640558-52">[52]</a> Study of a rat model of premature <a href="/wiki/Ageing" title="Ageing">aging</a> found increased <a href="/wiki/Oxidative_stress" title="Oxidative stress">oxidative stress</a>, reduced <a href="/wiki/Antioxidant" title="Antioxidant">antioxidant</a> enzyme activity and substantially greater <a href="/wiki/DNA_damage_(naturally_occurring)" title="DNA damage (naturally occurring)">DNA damage</a> in the brain <a href="/wiki/Neocortex" title="Neocortex">neocortex</a> and <a href="/wiki/Hippocampus" title="Hippocampus">hippocampus</a> of the prematurely aged rats than in normally aging control rats.<a href="#cite_note-pmid24709042-53">[53]</a> The DNA damage <a href="/wiki/8-Oxo-2%27-deoxyguanosine" title="8-Oxo-2'-deoxyguanosine">8-OHdG</a> is a product of ROS interaction with DNA. Numerous studies have shown that <a href="/wiki/8-Oxo-2%27-deoxyguanosine" title="8-Oxo-2'-deoxyguanosine">8-OHdG</a> increases with age<a href="#cite_note-54">[54]</a> (see <a href="/wiki/DNA_damage_theory_of_aging" title="DNA damage theory of aging">DNA damage theory of aging</a>). <div class="mw-heading mw-heading2"><h2 id="Cancer">Cancer</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=13" title="Edit section: Cancer">edit</a>]</div> ROS are constantly generated and eliminated in the biological system and are required to drive regulatory pathways.<a href="#cite_note-55">[55]</a> Under normal physiological conditions, cells control ROS levels by balancing the generation of ROS with their elimination by scavenging systems. But under oxidative stress conditions, excessive ROS can damage cellular proteins, lipids and DNA, leading to fatal lesions in the cell that contribute to carcinogenesis. Cancer cells exhibit greater ROS stress than normal cells do, partly due to oncogenic stimulation, increased metabolic activity and mitochondrial malfunction. ROS is a double-edged sword. On one hand, at low levels, ROS facilitates cancer cell survival since cell-cycle progression driven by growth factors and receptor tyrosine kinases (RTK) require ROS for activation<a href="#cite_note-56">[56]</a> and chronic inflammation, a major mediator of cancer, is regulated by ROS. On the other hand, a high level of ROS can suppress tumor growth through the sustained activation of cell-cycle inhibitor<a href="#cite_note-57">[57]</a><a href="#cite_note-58">[58]</a> and induction of cell death as well as senescence by damaging macromolecules. In fact, most of the chemotherapeutic and radiotherapeutic agents kill cancer cells by augmenting ROS stress.<a href="#cite_note-59">[59]</a><a href="#cite_note-60">[60]</a> The ability of cancer cells to distinguish between ROS as a survival or apoptotic signal is controlled by the dosage, duration, type, and site of ROS production. Modest levels of ROS are required for cancer cells to survive, whereas excessive levels kill them. Metabolic adaptation in tumours balances the cells' need for energy with equally important need for macromolecular building blocks and tighter control of redox balance. As a result, production of <a href="/wiki/NADPH" class="mw-redirect" title="NADPH">NADPH</a> is greatly enhanced, which functions as a cofactor to provide reducing power in many enzymatic reactions for macromolecular biosynthesis and at the same time rescuing the cells from excessive ROS produced during rapid proliferation. Cells counterbalance the detrimental effects of ROS by producing antioxidant molecules, such as reduced glutathione (GSH) and thioredoxin (TRX), which rely on the reducing power of NADPH to maintain their activities.<a href="#cite_note-61">[61]</a> Most risk factors associated with cancer interact with cells through the generation of ROS. ROS then activate various transcription factors such as nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), activator protein-1 (AP-1), hypoxia-inducible factor-1α and signal transducer and activator of transcription 3 (STAT3), leading to expression of proteins that control inflammation; cellular transformation; tumor cell survival; tumor cell proliferation; and invasion, angiogenesis as well as metastasis. And ROS also control the expression of various tumor suppressor genes such as p53, retinoblastoma gene (Rb), and phosphatase and tensin homolog (PTEN).<a href="#cite_note-pmid22117137-62">[62]</a> <div class="mw-heading mw-heading3"><h3 id="Carcinogenesis">Carcinogenesis</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=14" title="Edit section: Carcinogenesis">edit</a>]</div> ROS-related oxidation of DNA is one of the main causes of mutations, which can produce several types of DNA damage, including non-bulky (8-oxoguanine and formamidopyrimidine) and bulky (cyclopurine and etheno adducts) base modifications, abasic sites, non-conventional single-strand breaks, protein-DNA adducts, and intra/interstrand DNA crosslinks.<a href="#cite_note-63">[63]</a> It has been estimated that endogenous ROS produced via normal cell metabolism modify approximately 20,000 bases of DNA per day in a single cell. 8-oxoguanine is the most abundant among various oxidized nitrogeneous bases observed. During DNA replication, DNA polymerase mispairs 8-oxoguanine with adenine, leading to a G→T transversion mutation. The resulting genomic instability directly contributes to carcinogenesis. Cellular transformation leads to cancer and interaction of atypical PKC-ζ isoform with p47phox controls ROS production and transformation from apoptotic cancer stem cells through <a href="/wiki/Blebbishield_emergency_program" title="Blebbishield emergency program">blebbishield emergency program</a>.<a href="#cite_note-64">[64]</a><a href="#cite_note-65">[65]</a> <div class="mw-heading mw-heading3"><h3 id="Cell_proliferation">Cell proliferation</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=15" title="Edit section: Cell proliferation">edit</a>]</div> Uncontrolled proliferation is a hallmark of cancer cells. Both exogenous and endogenous ROS have been shown to enhance proliferation of cancer cells. The role of ROS in promoting tumor proliferation is further supported by the observation that agents with potential to inhibit ROS generation can also inhibit cancer cell proliferation.<a href="#cite_note-pmid22117137-62">[62]</a> Although ROS can promote tumor cell proliferation, a great increase in ROS has been associated with reduced cancer cell proliferation by induction of G2/M cell cycle arrest; increased phosphorylation of <a href="/wiki/ATM_serine/threonine_kinase" title="ATM serine/threonine kinase">ataxia telangiectasia mutated</a> (ATM), checkpoint kinase 1 (Chk 1), Chk 2; and reduced cell division cycle 25 homolog c (CDC25).<a href="#cite_note-66">[66]</a> <div class="mw-heading mw-heading3"><h3 id="Cell_death">Cell death</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=16" title="Edit section: Cell death">edit</a>]</div> A cancer cell can die in three ways: <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a>, <a href="/wiki/Necrosis" title="Necrosis">necrosis</a>, and <a href="/wiki/Autophagy" title="Autophagy">autophagy</a>. Excessive ROS can induce apoptosis through both the extrinsic and intrinsic pathways.<a href="#cite_note-67">[67]</a> In the extrinsic pathway of apoptosis, ROS are generated by Fas ligand as an upstream event for Fas activation via phosphorylation, which is necessary for subsequent recruitment of Fas-associated protein with death domain and caspase 8 as well as apoptosis induction.<a href="#cite_note-pmid22117137-62">[62]</a> In the intrinsic pathway, ROS function to facilitate cytochrome c release by activating pore-stabilizing proteins (Bcl-2 and Bcl-xL) as well as inhibiting pore-destabilizing proteins (Bcl-2-associated X protein, Bcl-2 homologous antagonist/killer).<a href="#cite_note-68">[68]</a> The intrinsic pathway is also known as the caspase cascade and is induced through mitochondrial damage which triggers the release of cytochrome c. DNA damage, oxidative stress, and loss of mitochondrial membrane potential lead to the release of the pro-apoptotic proteins mentioned above stimulating apoptosis.<a href="#cite_note-pmid17717517-69">[69]</a> Mitochondrial damage is closely linked to apoptosis and since mitochondria are easily targeted there is potential for cancer therapy.<a href="#cite_note-pmid20467424-70">[70]</a> The cytotoxic nature of ROS is a driving force behind apoptosis, but in even higher amounts, ROS can result in both apoptosis and necrosis, a form of uncontrolled cell death, in cancer cells.<a href="#cite_note-71">[71]</a> Numerous studies have shown the pathways and associations between ROS levels and apoptosis, but a newer line of study has connected ROS levels and autophagy.<a href="#cite_note-72">[72]</a> ROS can also induce cell death through autophagy, which is a self-catabolic process involving sequestration of cytoplasmic contents (exhausted or damaged organelles and protein aggregates) for degradation in lysosomes.<a href="#cite_note-73">[73]</a> Therefore, autophagy can also regulate the cell's health in times of oxidative stress. Autophagy can be induced by ROS levels through many pathways in the cell in an attempt to dispose of harmful organelles and prevent damage, such as carcinogens, without inducing apoptosis.<a href="#cite_note-sciencedirect.com-74">[74]</a> Autophagic cell death can be prompted by the over expression of autophagy where the cell digests too much of itself in an attempt to minimize the damage and can no longer survive. When this type of cell death occurs, an increase or loss of control of autophagy regulating genes is commonly co-observed.<a href="#cite_note-75">[75]</a> Thus, once a more in-depth understanding of autophagic cell death is attained and its relation to ROS, this form of programmed cell death may serve as a future cancer therapy. Autophagy and apoptosis are distinct mechanisms for cell death brought on by high levels of ROS. Aautophagy and apoptosis, however, rarely act through strictly independent pathways. There is a clear connection between ROS and autophagy and a correlation seen between excessive amounts of ROS leading to apoptosis.<a href="#cite_note-sciencedirect.com-74">[74]</a> The depolarization of the mitochondrial membrane is also characteristic of the initiation of autophagy. When mitochondria are damaged and begin to release ROS, autophagy is initiated to dispose of the damaging organelle. If a drug targets mitochondria and creates ROS, autophagy may dispose of so many mitochondria and other damaged organelles that the cell is no longer viable. The extensive amount of ROS and mitochondrial damage may also signal for apoptosis. The balance of autophagy within the cell and the crosstalk between autophagy and apoptosis mediated by ROS is crucial for a cell's survival. This crosstalk and connection between autophagy and apoptosis could be a mechanism targeted by cancer therapies or used in combination therapies for highly resistant cancers. <div class="mw-heading mw-heading3"><h3 id="Tumor_cell_invasion,_angiogenesis_and_metastasis">Tumor cell invasion, angiogenesis and metastasis</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=17" title="Edit section: Tumor cell invasion, angiogenesis and metastasis">edit</a>]</div> After growth factor stimulation of RTKs, ROS can trigger activation of signaling pathways involved in cell migration and invasion such as members of the mitogen activated protein kinase (MAPK) family – extracellular regulated kinase (ERK), c-jun NH-2 terminal kinase (JNK) and p38 MAPK. ROS can also promote migration by augmenting phosphorylation of the focal adhesion kinase (FAK) p130Cas and paxilin.<a href="#cite_note-76">[76]</a> Both in vitro and in vivo, ROS have been shown to induce transcription factors and modulate signaling molecules involved in angiogenesis (MMP, VEGF) and metastasis (upregulation of AP-1, CXCR4, AKT and downregulation of PTEN).<a href="#cite_note-pmid22117137-62">[62]</a> <div class="mw-heading mw-heading3"><h3 id="Chronic_inflammation_and_cancer">Chronic inflammation and cancer</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=18" title="Edit section: Chronic inflammation and cancer">edit</a>]</div> Experimental and epidemiologic research over the past several years has indicated close associations among ROS, chronic inflammation, and cancer.<a href="#cite_note-pmid22117137-62">[62]</a> ROS induces chronic inflammation by the induction of COX-2, inflammatory cytokines (TNFα, interleukin 1 (IL-1), IL-6), chemokines (IL-8, CXCR4) and pro-inflammatory transcription factors (NF-κB).<a href="#cite_note-pmid22117137-62">[62]</a> These chemokines and chemokine receptors, in turn, promote invasion and metastasis of various tumor types. <div class="mw-heading mw-heading3"><h3 id="Cancer_therapy">Cancer therapy</h3>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=19" title="Edit section: Cancer therapy">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cc/Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf/page1-220px-Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf.jpg" decoding="async" width="220" height="174" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/cc/Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf/page1-330px-Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/cc/Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf/page1-440px-Open_source_and_reduced_expenditure_ROS_generation_strategy.pdf.jpg 2x" data-file-width="900" data-file-height="712" /></a><figcaption>The scheme of fabrication process and therapeutic mechanism of thermo-responsive (MSNs@CaO2-ICG)@LA NPs for synergistic CDT/PDT with H2O2/O2 self-supply and GSH depletion</figcaption></figure> Both ROS-elevating and ROS-eliminating strategies have been developed with the former being predominantly used. Cancer cells with elevated ROS levels depend heavily on the antioxidant defense system. ROS-elevating drugs further increase cellular ROS stress level, either by direct ROS-generation (e.g. motexafin gadolinium, elesclomol) or by agents that abrogate the inherent antioxidant system such as SOD inhibitor (e.g. ATN-224, 2-methoxyestradiol) and GSH inhibitor (e.g. PEITC, buthionine sulfoximine (BSO)). The result is an overall increase in endogenous ROS, which when above a cellular tolerability threshold, may induce cell death.<a href="#cite_note-77">[77]</a> On the other hand, normal cells appear to have, under lower basal stress and reserve, a higher capacity to cope with additional ROS-generating insults than cancer cells do.<a href="#cite_note-78">[78]</a> Therefore, the elevation of ROS in all cells can be used to achieve the selective killing of cancer cells. Radiotherapy also relies on ROS toxicity to eradicate tumor cells. Radiotherapy uses X-rays, γ-rays as well as heavy particle radiation such as protons and neutrons to induce ROS-mediated cell death and mitotic failure.<a href="#cite_note-pmid22117137-62">[62]</a> Due to the dual role of ROS, both prooxidant and antioxidant-based anticancer agents have been developed. However, modulation of ROS signaling alone seems not to be an ideal approach due to adaptation of cancer cells to ROS stress, redundant pathways for supporting cancer growth and toxicity from ROS-generating anticancer drugs. Combinations of ROS-generating drugs with pharmaceuticals that can break the redox adaptation could be a better strategy for enhancing cancer cell cytotoxicity.<a href="#cite_note-pmid22117137-62">[62]</a> <a href="/wiki/James_Watson" title="James Watson">James Watson</a><a href="#cite_note-79">[79]</a> and others<a href="#cite_note-ReferenceA-80">[80]</a> have proposed that lack of intracellular ROS due to a lack of physical exercise may contribute to the malignant progression of cancer, because spikes of ROS are needed to correctly fold proteins in the endoplasmatic reticulum and low ROS levels may thus aspecifically hamper the formation of tumor suppressor proteins.<a href="#cite_note-ReferenceA-80">[80]</a> Since physical exercise induces temporary spikes of ROS, this may explain why physical exercise is beneficial for cancer patient prognosis.<a href="#cite_note-81">[81]</a> Moreover, high inducers of ROS such as 2-deoxy-D-glucose and carbohydrate-based inducers of cellular stress induce cancer cell death more potently because they exploit the cancer cell's high avidity for sugars.<a href="#cite_note-82">[82]</a> <div class="mw-heading mw-heading2"><h2 id="Positive_role_of_ROS_in_memory">Positive role of ROS in memory</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=20" title="Edit section: Positive role of ROS in memory">edit</a>]</div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Initiation_of_DNA_demethylation_at_a_CpG_site.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/0/07/Initiation_of_DNA_demethylation_at_a_CpG_site.svg/400px-Initiation_of_DNA_demethylation_at_a_CpG_site.svg.png" decoding="async" width="400" height="460" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/0/07/Initiation_of_DNA_demethylation_at_a_CpG_site.svg/600px-Initiation_of_DNA_demethylation_at_a_CpG_site.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/0/07/Initiation_of_DNA_demethylation_at_a_CpG_site.svg/800px-Initiation_of_DNA_demethylation_at_a_CpG_site.svg.png 2x" data-file-width="643" data-file-height="739" /></a><figcaption>Initiation of <a href="/wiki/DNA_demethylation" title="DNA demethylation">DNA demethylation</a> at a <a href="/wiki/CpG_site" title="CpG site">CpG site</a>. In adult somatic cells DNA methylation typically occurs in the context of CpG dinucleotides (<a href="/wiki/CpG_sites" class="mw-redirect" title="CpG sites">CpG sites</a>), forming <a href="/wiki/5-methylcytosine" class="mw-redirect" title="5-methylcytosine">5-methylcytosine</a>-pG, or 5mCpG. Reactive oxygen species (ROS) may attack guanine at the dinucleotide site, forming <a href="/wiki/8-oxo-2%27-deoxyguanosine" class="mw-redirect" title="8-oxo-2'-deoxyguanosine">8-hydroxy-2'-deoxyguanosine</a> (8-OHdG), and resulting in a 5mCp-8-OHdG dinucleotide site. The <a href="/wiki/Base_excision_repair" title="Base excision repair">base excision repair</a> enzyme <a href="/wiki/Oxoguanine_glycosylase" title="Oxoguanine glycosylase">OGG1</a> targets 8-OHdG and binds to the lesion without immediate excision. OGG1, present at a 5mCp-8-OHdG site recruits <a href="/wiki/Tet_methylcytosine_dioxygenase_1" title="Tet methylcytosine dioxygenase 1">TET1</a> and TET1 oxidizes the 5mC adjacent to the 8-OHdG. This initiates demethylation of 5mC.<a href="#cite_note-Zhou-83">[83]</a></figcaption></figure> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Demethylation_of_5-methylcytosine.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/3/3a/Demethylation_of_5-methylcytosine.svg/400px-Demethylation_of_5-methylcytosine.svg.png" decoding="async" width="400" height="518" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/3a/Demethylation_of_5-methylcytosine.svg/600px-Demethylation_of_5-methylcytosine.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/3a/Demethylation_of_5-methylcytosine.svg/800px-Demethylation_of_5-methylcytosine.svg.png 2x" data-file-width="816" data-file-height="1056" /></a><figcaption>Demethylation of <a href="/wiki/5-Methylcytosine" title="5-Methylcytosine">5-Methylcytosine</a> (5mC) in neuron DNA. As reviewed in 2018,<a href="#cite_note-pmid29875631-84">[84]</a> in brain neurons, 5mC is oxidized by the ten-eleven translocation (TET) family of dioxygenases (<a href="/wiki/Tet_methylcytosine_dioxygenase_1" title="Tet methylcytosine dioxygenase 1">TET1</a>, <a href="/wiki/Tet_methylcytosine_dioxygenase_2" title="Tet methylcytosine dioxygenase 2">TET2</a>, <a href="/wiki/Tet_methylcytosine_dioxygenase_3" title="Tet methylcytosine dioxygenase 3">TET3</a>) to generate <a href="/wiki/5-hydroxymethylcytosine" class="mw-redirect" title="5-hydroxymethylcytosine">5-hydroxymethylcytosine</a> (5hmC). In successive steps TET enzymes further hydroxylate 5hmC to generate 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). <a href="/wiki/Thymine-DNA_glycosylase" title="Thymine-DNA glycosylase">Thymine-DNA glycosylase</a> (TDG) recognizes the intermediate bases 5fC and 5caC and excises the <a href="/wiki/Glycosidic_bond" title="Glycosidic bond">glycosidic bond</a> resulting in an apyrimidinic site (<a href="/wiki/AP_site" title="AP site">AP site</a>). In an alternative oxidative deamination pathway, 5hmC can be oxidatively deaminated by activity-induced cytidine deaminase/apolipoprotein B mRNA editing complex <a href="/wiki/APOBEC3G" title="APOBEC3G">(AID/APOBEC)</a> deaminases to form 5-hydroxymethyluracil (5hmU) or 5mC can be converted to <a href="/wiki/Thymine" title="Thymine">thymine</a> (Thy). 5hmU can be cleaved by TDG, single-strand-selective monofunctional uracil-DNA glycosylase 1 (<a href="/wiki/SMUG1" title="SMUG1">SMUG1</a>), Nei-Like DNA Glycosylase 1 (<a href="/wiki/NEIL1" title="NEIL1">NEIL1</a>), or methyl-CpG binding protein 4 (<a href="/wiki/MBD4" title="MBD4">MBD4</a>). AP sites and T:G mismatches are then repaired by base excision repair (BER) enzymes to yield <a href="/wiki/Cytosine" title="Cytosine">cytosine</a> (Cyt).</figcaption></figure> ROS are critical in <a href="/wiki/Memory" title="Memory">memory</a> formation.<a href="#cite_note-pmid20649473-85">[85]</a><a href="#cite_note-pmid27625575-86">[86]</a> ROS also have a central role in epigenetic <a href="/wiki/DNA_demethylation" title="DNA demethylation">DNA demethylation</a>, which is relevant to <a href="/wiki/Epigenetics_in_learning_and_memory" title="Epigenetics in learning and memory">learning and memory</a><a href="#cite_note-pmid21116250-87">[87]</a><a href="#cite_note-pmid26875778-88">[88]</a> In mammalian nuclear DNA, a methyl group can be added, by a <a href="/wiki/DNA_methyltransferase" title="DNA methyltransferase">DNA methyltransferase</a>, to the 5th carbon of cytosine to form 5mC (see red methyl group added to form 5mC near the top of the first figure). The DNA methyltransferases most often form 5mC within the dinucleotide sequence "cytosine-phosphate-guanine" to form 5mCpG. This addition is a major type of epigenetic alteration and it can <a href="/wiki/Regulation_of_gene_expression#Chemical" title="Regulation of gene expression">silence gene expression</a>. Methylated cytosine can also be <a href="/wiki/DNA_demethylation" title="DNA demethylation">demethylated</a>, an epigenetic alteration that can increase the expression of a gene. A major enzyme involved in demethylating 5mCpG is <a href="/wiki/Tet_methylcytosine_dioxygenase_1" title="Tet methylcytosine dioxygenase 1">TET1</a>. However, TET1 is only able to act on 5mCpG if an ROS has first acted on the guanine to form <a href="/wiki/8-oxo-2%27-deoxyguanosine" class="mw-redirect" title="8-oxo-2'-deoxyguanosine">8-hydroxy-2'-deoxyguanosine</a> (8-OHdG), resulting in a 5mCp-8-OHdG dinucleotide .<a href="#cite_note-Zhou-83">[83]</a> However, TET1 is only able to act on the 5mC part of the dinucleotide when the <a href="/wiki/Base_excision_repair" title="Base excision repair">base excision repair</a> enzyme <a href="/wiki/Oxoguanine_glycosylase" title="Oxoguanine glycosylase">OGG1</a> binds to the 8-OHdG lesion without immediate excision. Adherence of OGG1 to the 5mCp-8-OHdG site recruits <a href="/wiki/Tet_methylcytosine_dioxygenase_1" title="Tet methylcytosine dioxygenase 1">TET1</a> and TET1 then oxidizes the 5mC adjacent to 8-OHdG, as shown in the first figure, initiating a demethylation pathway shown in the second figure. The thousands of CpG sites being demethylated during memory formation depend on ROS in an initial step. The altered protein expression in neurons, controlled in part by ROS-dependent demethylation of CpG sites in gene promoters within neuron DNA, are central to memory formation.<a href="#cite_note-pmid20975755-89">[89]</a> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=21" title="Edit section: See also">edit</a>]</div> <ul><li><a href="/wiki/Antioxidant_effect_of_polyphenols_and_natural_phenols" title="Antioxidant effect of polyphenols and natural phenols">Antioxidant effect of polyphenols and natural phenols</a></li> <li><a href="/wiki/Iodide" title="Iodide">Iodide</a></li> <li><a href="/wiki/Melanin" title="Melanin">Melanin</a></li> <li><a href="/wiki/Mitohormesis" class="mw-redirect" title="Mitohormesis">Mitohormesis</a></li> <li><a href="/wiki/Oxidative_stress" title="Oxidative stress">Oxidative stress</a></li> <li><a href="/wiki/Oxygen_toxicity" title="Oxygen toxicity">Oxygen toxicity</a></li> <li><a href="/wiki/Pro-oxidant" title="Pro-oxidant">Pro-oxidant</a></li> <li><a href="/wiki/Reactive_nitrogen_species" title="Reactive nitrogen species">Reactive nitrogen species</a></li> <li><a href="/wiki/Reactive_sulfur_species" title="Reactive sulfur species">Reactive sulfur species</a></li> <li><a href="/wiki/Reactive_carbonyl_species" title="Reactive carbonyl species">Reactive carbonyl species</a></li> <li><a href="/wiki/Reactive_oxygen_species_production_in_marine_microalgae" title="Reactive oxygen species production in marine microalgae">Reactive oxygen species production in marine microalgae</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=22" title="Edit section: References">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output 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Antioxidants & Redox Signaling. 14 (10): 2013–2054. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1089%2Fars.2010.3208">10.1089/ars.2010.3208</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078504">3078504</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20649473">20649473</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Antioxidants+%26+Redox+Signaling&rft.atitle=Reactive+oxygen+species+in+the+regulation+of+synaptic+plasticity+and+memory&rft.volume=14&rft.issue=10&rft.pages=2013-2054&rft.date=2011-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3078504%23id-name%3DPMC&rft_id=info%3Apmid%2F20649473&rft_id=info%3Adoi%2F10.1089%2Fars.2010.3208&rft.aulast=Massaad&rft.aufirst=CA&rft.au=Klann%2C+E&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3078504&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"> </li> <li id="cite_note-pmid27625575-86"><a href="#cite_ref-pmid27625575_86-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFBeckhauserFrancis-OliveiraDe_Pasquale2016" class="citation journal cs1">Beckhauser TF, Francis-Oliveira J, De Pasquale R (2016). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5012454">"Reactive Oxygen Species: Physiological and Physiopathological Effects on Synaptic Plasticity"</a>. Journal of Experimental Neuroscience. 10 (Suppl 1): 23–48. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.4137%2FJEN.S39887">10.4137/JEN.S39887</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5012454">5012454</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/27625575">27625575</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Experimental+Neuroscience&rft.atitle=Reactive+Oxygen+Species%3A+Physiological+and+Physiopathological+Effects+on+Synaptic+Plasticity&rft.volume=10&rft.issue=Suppl+1&rft.pages=23-48&rft.date=2016&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5012454%23id-name%3DPMC&rft_id=info%3Apmid%2F27625575&rft_id=info%3Adoi%2F10.4137%2FJEN.S39887&rft.aulast=Beckhauser&rft.aufirst=TF&rft.au=Francis-Oliveira%2C+J&rft.au=De+Pasquale%2C+R&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5012454&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"> </li> <li id="cite_note-pmid21116250-87"><a href="#cite_ref-pmid21116250_87-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDaySweatt2011" class="citation journal cs1">Day JJ, Sweatt JD (January 2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3055499">"Epigenetic modifications in neurons are essential for formation and storage of behavioral memory"</a>. Neuropsychopharmacology. 36 (1): 357–358. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnpp.2010.125">10.1038/npp.2010.125</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3055499">3055499</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21116250">21116250</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Neuropsychopharmacology&rft.atitle=Epigenetic+modifications+in+neurons+are+essential+for+formation+and+storage+of+behavioral+memory&rft.volume=36&rft.issue=1&rft.pages=357-358&rft.date=2011-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3055499%23id-name%3DPMC&rft_id=info%3Apmid%2F21116250&rft_id=info%3Adoi%2F10.1038%2Fnpp.2010.125&rft.aulast=Day&rft.aufirst=JJ&rft.au=Sweatt%2C+JD&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3055499&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"> </li> <li id="cite_note-pmid26875778-88"><a href="#cite_ref-pmid26875778_88-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFSweatt2016" class="citation journal cs1">Sweatt JD (October 2016). <a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fjnc.13580">"Neural plasticity and behavior - sixty years of conceptual advances"</a>. Journal of Neurochemistry. 139 (Suppl 2): 179–199. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fjnc.13580">10.1111/jnc.13580</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/26875778">26875778</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Neurochemistry&rft.atitle=Neural+plasticity+and+behavior+-+sixty+years+of+conceptual+advances&rft.volume=139&rft.issue=Suppl+2&rft.pages=179-199&rft.date=2016-10&rft_id=info%3Adoi%2F10.1111%2Fjnc.13580&rft_id=info%3Apmid%2F26875778&rft.aulast=Sweatt&rft.aufirst=JD&rft_id=https%3A%2F%2Fdoi.org%2F10.1111%252Fjnc.13580&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"> </li> <li id="cite_note-pmid20975755-89"><a href="#cite_ref-pmid20975755_89-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDaySweatt2010" class="citation journal cs1">Day JJ, Sweatt JD (November 2010). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130618">"DNA methylation and memory formation"</a>. Nature Neuroscience. 13 (11): 1319–1323. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnn.2666">10.1038/nn.2666</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3130618">3130618</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20975755">20975755</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Neuroscience&rft.atitle=DNA+methylation+and+memory+formation&rft.volume=13&rft.issue=11&rft.pages=1319-1323&rft.date=2010-11&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3130618%23id-name%3DPMC&rft_id=info%3Apmid%2F20975755&rft_id=info%3Adoi%2F10.1038%2Fnn.2666&rft.aulast=Day&rft.aufirst=JJ&rft.au=Sweatt%2C+JD&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3130618&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"> </li> </ol></div> <div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=23" title="Edit section: Further reading">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1239549316">.mw-parser-output .refbegin{margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}@media screen{.mw-parser-output .refbegin{font-size:90%}}</style><div class="refbegin refbegin-columns references-column-width" style="column-width: 32em"> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFSen2003" class="citation journal cs1">Sen CK (2003). "The general case for redox control of wound repair". Wound Repair and Regeneration. 11 (6): 431–438. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1046%2Fj.1524-475X.2003.11607.x">10.1046/j.1524-475X.2003.11607.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14617282">14617282</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:40770160">40770160</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Wound+Repair+and+Regeneration&rft.atitle=The+general+case+for+redox+control+of+wound+repair&rft.volume=11&rft.issue=6&rft.pages=431-438&rft.date=2003&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A40770160%23id-name%3DS2CID&rft_id=info%3Apmid%2F14617282&rft_id=info%3Adoi%2F10.1046%2Fj.1524-475X.2003.11607.x&rft.aulast=Sen&rft.aufirst=CK&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKrötzSohnGloeZahler2002" class="citation journal cs1">Krötz F, Sohn HY, Gloe T, Zahler S, Riexinger T, Schiele TM, et al. (August 2002). <a rel="nofollow" class="external text" href="https://doi.org/10.1182%2Fblood.V100.3.917">"NAD(P)H oxidase-dependent platelet superoxide anion release increases platelet recruitment"</a>. Blood. 100 (3): 917–924. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1182%2Fblood.V100.3.917">10.1182/blood.V100.3.917</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12130503">12130503</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Blood&rft.atitle=NAD%28P%29H+oxidase-dependent+platelet+superoxide+anion+release+increases+platelet+recruitment&rft.volume=100&rft.issue=3&rft.pages=917-924&rft.date=2002-08&rft_id=info%3Adoi%2F10.1182%2Fblood.V100.3.917&rft_id=info%3Apmid%2F12130503&rft.aulast=Kr%C3%B6tz&rft.aufirst=F&rft.au=Sohn%2C+HY&rft.au=Gloe%2C+T&rft.au=Zahler%2C+S&rft.au=Riexinger%2C+T&rft.au=Schiele%2C+TM&rft.au=Becker%2C+BF&rft.au=Theisen%2C+K&rft.au=Klauss%2C+V&rft.au=Pohl%2C+U&rft_id=https%3A%2F%2Fdoi.org%2F10.1182%252Fblood.V100.3.917&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFPignatelliPulcinelliLentiGazzaniga1998" class="citation journal cs1">Pignatelli P, Pulcinelli FM, Lenti L, Gazzaniga PP, Violi F (January 1998). <a rel="nofollow" class="external text" href="https://doi.org/10.1182%2Fblood.V91.2.484">"Hydrogen peroxide is involved in collagen-induced platelet activation"</a>. Blood. 91 (2): 484–490. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1182%2Fblood.V91.2.484">10.1182/blood.V91.2.484</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9427701">9427701</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Blood&rft.atitle=Hydrogen+peroxide+is+involved+in+collagen-induced+platelet+activation&rft.volume=91&rft.issue=2&rft.pages=484-490&rft.date=1998-01&rft_id=info%3Adoi%2F10.1182%2Fblood.V91.2.484&rft_id=info%3Apmid%2F9427701&rft.aulast=Pignatelli&rft.aufirst=P&rft.au=Pulcinelli%2C+FM&rft.au=Lenti%2C+L&rft.au=Gazzaniga%2C+PP&rft.au=Violi%2C+F&rft_id=https%3A%2F%2Fdoi.org%2F10.1182%252Fblood.V91.2.484&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFGuzikKorbutAdamek-Guzik2003" class="citation journal cs1">Guzik TJ, Korbut R, Adamek-Guzik T (December 2003). "Nitric oxide and superoxide in inflammation and immune regulation". Journal of Physiology and Pharmacology. 54 (4): 469–487. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14726604">14726604</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Physiology+and+Pharmacology&rft.atitle=Nitric+oxide+and+superoxide+in+inflammation+and+immune+regulation&rft.volume=54&rft.issue=4&rft.pages=469-487&rft.date=2003-12&rft_id=info%3Apmid%2F14726604&rft.aulast=Guzik&rft.aufirst=TJ&rft.au=Korbut%2C+R&rft.au=Adamek-Guzik%2C+T&rfr_id=info%3Asid%2Fen.wikipedia.org%3AReactive+oxygen+species" class="Z3988"></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2>[<a href="/w/index.php?title=Reactive_oxygen_species&action=edit&section=24" title="Edit section: External links">edit</a>]</div> <ul><li><a rel="nofollow" class="external text" href="http://www.cshl.edu/Article-Page/nobel-laureate-james-watson-publishes-novel-hypothesis-on-curing-late-stage-cancers">Nobel laureate James Watson's novel hypothesis</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20130601193118/http://www.cshl.edu/Article-Page/nobel-laureate-james-watson-publishes-novel-hypothesis-on-curing-late-stage-cancers">Archived</a> 2013-06-01 at the <a href="/wiki/Wayback_Machine" title="Wayback Machine">Wayback Machine</a></li> <li><a rel="nofollow" class="external text" href="http://www.slate.com/articles/health_and_science/medical_examiner/2011/08/the_doctor_and_the_pomegranate.html">Antioxidants don't work, but no one wants to hear it.</a></li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist 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