{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86724"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86724","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The Roles of Peroxynitrite and Superoxide in Oxidative Damage to E. Coli","abstract":"Peroxynitrite (ONOO$\\sp{-}),$ a toxic biomolecule produced from the reaction of superoxide and nitric oxide (NO$\\cdot)$ in the phagolysosome, may also be toxic by the same mechanism as O$\\sb2{-}.$ Our in vivo results indicated that peroxynitrite has the same intracellular targets as superoxide. Of nineteen enzymes tested, only the dehydratase enzymes containing these iron-sulfur clusters were significantly affected by peroxynitrite challenge. These iron-sulfur clusters could be repaired, and both iron storage proteins and iron import seem to be necessary for efficient repair. This enzyme inactivation led to an increased intracellular free iron. However, unlike superoxide. the free iron was rapidly sequestered.","abstract_html":"Peroxynitrite (ONOO$\\sp{-}),$ a toxic biomolecule produced from the reaction of superoxide and nitric oxide (NO$\\cdot)$ in the phagolysosome, may also be toxic by the same mechanism as O$\\sb2{-}.$ Our in vivo results indicated that peroxynitrite has the same intracellular targets as superoxide. Of nineteen enzymes tested, only the dehydratase enzymes containing these iron-sulfur clusters were significantly affected by peroxynitrite challenge. These iron-sulfur clusters could be repaired, and both iron storage proteins and iron import seem to be necessary for efficient repair. This enzyme inactivation led to an increased intracellular free iron. However, unlike superoxide. the free iron was rapidly sequestered.","abstract_has_math":true,"creators":["Opperman, Kay Keyer"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Imlay, James A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:38Z","date_published":"2015-09-28T15:17:38Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9812724"],"render_values":[{"text":"(MiAaPQ)AAI9812724","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86724","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Imlay, James A."]},{"key":"dc:creator","label":"Author","values":["Opperman, Kay Keyer"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T15:17:38Z","10000-01-01","1997"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Biochemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/86724","(MiAaPQ)AAI9812724"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Peroxynitrite (ONOO$\\sp{-}),$ a toxic biomolecule produced from the reaction of superoxide and nitric oxide (NO$\\cdot)$ in the phagolysosome, may also be toxic by the same mechanism as O$\\sb2{-}.$ Our in vivo results indicated that peroxynitrite has the same intracellular targets as superoxide. Of nineteen enzymes tested, only the dehydratase enzymes containing these iron-sulfur clusters were significantly affected by peroxynitrite challenge. These iron-sulfur clusters could be repaired, and both iron storage proteins and iron import seem to be necessary for efficient repair. This enzyme inactivation led to an increased intracellular free iron. However, unlike superoxide. the free iron was rapidly sequestered.","Made available in DSpace on 2015-09-28T15:17:38Z (GMT). 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Coli"]}]}],"canonical_facts":{"dc:contributor":["Imlay, James A."],"dc:creator":["Opperman, Kay Keyer"],"dc:date":["2015-09-28T15:17:38Z","10000-01-01","1997"],"dc:description":["Peroxynitrite (ONOO$\\sp{-}),$ a toxic biomolecule produced from the reaction of superoxide and nitric oxide (NO$\\cdot)$ in the phagolysosome, may also be toxic by the same mechanism as O$\\sb2{-}.$ Our in vivo results indicated that peroxynitrite has the same intracellular targets as superoxide. Of nineteen enzymes tested, only the dehydratase enzymes containing these iron-sulfur clusters were significantly affected by peroxynitrite challenge. These iron-sulfur clusters could be repaired, and both iron storage proteins and iron import seem to be necessary for efficient repair. This enzyme inactivation led to an increased intracellular free iron. However, unlike superoxide. the free iron was rapidly sequestered.","Made available in DSpace on 2015-09-28T15:17:38Z (GMT). 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