{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84783"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84783","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Biochemical Studies of the Sodium -Translocating NADH:ubiquinone Oxidoreductase","abstract":"In the NqrF subunit, four conserved cysteines (C70, C76, C79 and C111) are predicted to ligate the 2Fe-2S center, and three conserved residues (R210, Y212, S245) are predicted to be essential to the binding of the FAD cofactor. By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. Functional studies on these mutants strongly support an electron transport pathway model in which the non-covalently bound FAD in the NqrF subunit is the first redox cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center.","abstract_html":"In the NqrF subunit, four conserved cysteines (C70, C76, C79 and C111) are predicted to ligate the 2Fe-2S center, and three conserved residues (R210, Y212, S245) are predicted to be essential to the binding of the FAD cofactor. By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. Functional studies on these mutants strongly support an electron transport pathway model in which the non-covalently bound FAD in the NqrF subunit is the first redox cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center.","abstract_has_math":false,"creators":["Zhou, Weidong"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Gennis, Robert B."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:27:52Z","date_published":"2015-09-25T22:27:52Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3044275"],"render_values":[{"text":"(MiAaPQ)AAI3044275","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84783","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Gennis, Robert B."]},{"key":"dc:creator","label":"Author","values":["Zhou, Weidong"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:27:52Z","10000-01-01","2002"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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":["Biophysics, General"]}]},{"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/2142/84783","(MiAaPQ)AAI3044275"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["In the NqrF subunit, four conserved cysteines (C70, C76, C79 and C111) are predicted to ligate the 2Fe-2S center, and three conserved residues (R210, Y212, S245) are predicted to be essential to the binding of the FAD cofactor. By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. Functional studies on these mutants strongly support an electron transport pathway model in which the non-covalently bound FAD in the NqrF subunit is the first redox cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center.","Made available in DSpace on 2015-09-25T22:27:52Z (GMT). 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By mutagenesis and spectroscopic characterization, the four conserved cysteines are confirmed to be the ligands for the 2Fe-2S center, and R210, Y212, S245 are confirmed to be important for the binding of the FAD cofactor in Na +-NQR. Functional studies on these mutants strongly support an electron transport pathway model in which the non-covalently bound FAD in the NqrF subunit is the first redox cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center.","Made available in DSpace on 2015-09-25T22:27:52Z (GMT). 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