{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/21571"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/21571","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Localization of the prosthetic group ligands of cytochrome o terminal oxidase complex of Escherichia coli","abstract":"The cytochrome o ubiquinol oxidase is one of two terminal oxidases present in the aerobic respiratory chain of E. coli. The cytochrome o complex has been purified and found to contain two protoheme IXs and one copper atom. Subsequently the gene encoding the cyo operon has been cloned. The research presented in this thesis focuses on the continued structural analysis of the cytochrome o oxidase complex including the following areas of interest: (i) the DNA sequence of the cyo operon, (ii) subunit analysis, (iii) localization of the prosthetic groups of this complex to specific subunits and (iv) determination of the histidines responsible for ligating the prosthetic groups of this complex.","abstract_html":"The cytochrome o ubiquinol oxidase is one of two terminal oxidases present in the aerobic respiratory chain of E. coli. The cytochrome o complex has been purified and found to contain two protoheme IXs and one copper atom. Subsequently the gene encoding the cyo operon has been cloned. The research presented in this thesis focuses on the continued structural analysis of the cytochrome o oxidase complex including the following areas of interest: (i) the DNA sequence of the cyo operon, (ii) subunit analysis, (iii) localization of the prosthetic groups of this complex to specific subunits and (iv) determination of the histidines responsible for ligating the prosthetic groups of this complex.","abstract_has_math":false,"creators":["Lemieux, Laura Jean"],"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":2011,"date_issued":"2011-05-07T13:12:35Z","date_published":"2011-05-07T13:12:35Z","updated_at":"2026-07-22T22:25:18Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":["Copyright 1991 Lemieux, Laura Jean"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9136656","(UMI)AAI9136656"],"render_values":[{"text":"AAI9136656","href":null,"code":true},{"text":"(UMI)AAI9136656","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/21571","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":["Lemieux, Laura Jean"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T13:12:35Z","10000-01-01","1991"]},{"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":["Chemistry, Biochemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1991 Lemieux, Laura Jean"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9136656","(UMI)AAI9136656","http://hdl.handle.net/2142/21571"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The cytochrome o ubiquinol oxidase is one of two terminal oxidases present in the aerobic respiratory chain of E. coli. The cytochrome o complex has been purified and found to contain two protoheme IXs and one copper atom. Subsequently the gene encoding the cyo operon has been cloned. The research presented in this thesis focuses on the continued structural analysis of the cytochrome o oxidase complex including the following areas of interest: (i) the DNA sequence of the cyo operon, (ii) subunit analysis, (iii) localization of the prosthetic groups of this complex to specific subunits and (iv) determination of the histidines responsible for ligating the prosthetic groups of this complex.","The cyo DNA sequence presented here reveals that there are five open reading frames, cyo A, B, C, D, and E. Similarity searches performed on these putative subunits reveal that three of these ORFs are related to subunits II, I, and III of both bacterial and eukaryotic cytochrome c oxidases. The remaining two putative subunits have sequence similarity with subunits found in bacterial cytochrome c oxidases.","Immunological analyses of subclones of cyoA and cyoB demonstrate that they encode subunits II and I, respectively. Subsequent spectroscopic analysis of these subclones and the cyoBCDE subclone localize both the high and low-spin hemes associated with this complex to subunit I (cyoB) of the cytochrome o oxidase.","The alignment of subunit I from cytochrome o oxidase with the analogous subunit from over 23 different species of bacterial and eukaryotic aa$\\sb3$-type cytochrome c oxidases revealed that there are seven conserved histidines referred to as H106, H284, H333, H334, H411, H419 and H421. Physical data on leucine mutations of these histidines indicate that H106 and H421 serve as ligands for the low-spin heme, H333 and H334 are likely to be copper ligands and H284 is probably the high-spin heme ligand.","Made available in DSpace on 2011-05-07T13:12:35Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9136656.pdf: 5435005 bytes, checksum: cb6cb34a53be77fac028ef9b9cdac557 (MD5) Previous issue date: 1991","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:51:41Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:23:45-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["Localization of the prosthetic group ligands of cytochrome o terminal oxidase complex of Escherichia coli"]}]}],"canonical_facts":{"dc:contributor":["Gennis, Robert B."],"dc:creator":["Lemieux, Laura Jean"],"dc:date":["2011-05-07T13:12:35Z","10000-01-01","1991"],"dc:description":["The cytochrome o ubiquinol oxidase is one of two terminal oxidases present in the aerobic respiratory chain of E. coli. The cytochrome o complex has been purified and found to contain two protoheme IXs and one copper atom. Subsequently the gene encoding the cyo operon has been cloned. The research presented in this thesis focuses on the continued structural analysis of the cytochrome o oxidase complex including the following areas of interest: (i) the DNA sequence of the cyo operon, (ii) subunit analysis, (iii) localization of the prosthetic groups of this complex to specific subunits and (iv) determination of the histidines responsible for ligating the prosthetic groups of this complex.","The cyo DNA sequence presented here reveals that there are five open reading frames, cyo A, B, C, D, and E. Similarity searches performed on these putative subunits reveal that three of these ORFs are related to subunits II, I, and III of both bacterial and eukaryotic cytochrome c oxidases. The remaining two putative subunits have sequence similarity with subunits found in bacterial cytochrome c oxidases.","Immunological analyses of subclones of cyoA and cyoB demonstrate that they encode subunits II and I, respectively. Subsequent spectroscopic analysis of these subclones and the cyoBCDE subclone localize both the high and low-spin hemes associated with this complex to subunit I (cyoB) of the cytochrome o oxidase.","The alignment of subunit I from cytochrome o oxidase with the analogous subunit from over 23 different species of bacterial and eukaryotic aa$\\sb3$-type cytochrome c oxidases revealed that there are seven conserved histidines referred to as H106, H284, H333, H334, H411, H419 and H421. Physical data on leucine mutations of these histidines indicate that H106 and H421 serve as ligands for the low-spin heme, H333 and H334 are likely to be copper ligands and H284 is probably the high-spin heme ligand.","Made available in DSpace on 2011-05-07T13:12:35Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9136656.pdf: 5435005 bytes, checksum: cb6cb34a53be77fac028ef9b9cdac557 (MD5) Previous issue date: 1991","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:51:41Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:23:45-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["AAI9136656","(UMI)AAI9136656","http://hdl.handle.net/2142/21571"],"dc:language":["eng"],"dc:rights":["Copyright 1991 Lemieux, Laura Jean"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Localization of the prosthetic group ligands of cytochrome o terminal oxidase complex of Escherichia coli"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:18Z"}