{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84873"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84873","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Cytochrome AA(3) From Rhodobacter Sphaeroides: Affinity Purification and Biophysical Characterization of Site-Directed Mutants","abstract":"Cytochrome c oxidase of R. sphaeroides has been purified using affinity methods and studied using site-directed mutagenesis coupled with a wide variety of biophysical characterization methods. Two methods of affinity purification were developed. Site-directed mutants were constructed in regions of the protein which were predicted to be important for enzyme function by sequence analysis. Methods ranging from visible and vibrational spectroscopy to rapid kinetic measurements of electron and proton transfers were used to probe the various effects of these mutants on the structure and function of the enzyme. Results were interpreted, when possible, in terms of possible redox-linked proton pumping mechanisms, or alternatively, on a purely phenomenological basis.","abstract_html":"Cytochrome c oxidase of R. sphaeroides has been purified using affinity methods and studied using site-directed mutagenesis coupled with a wide variety of biophysical characterization methods. Two methods of affinity purification were developed. Site-directed mutants were constructed in regions of the protein which were predicted to be important for enzyme function by sequence analysis. Methods ranging from visible and vibrational spectroscopy to rapid kinetic measurements of electron and proton transfers were used to probe the various effects of these mutants on the structure and function of the enzyme. Results were interpreted, when possible, in terms of possible redox-linked proton pumping mechanisms, or alternatively, on a purely phenomenological basis.","abstract_has_math":false,"creators":["Mitchell, David Michael"],"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":"2015-09-25T22:28:17Z","date_published":"2015-09-25T22:28:17Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9712382"],"render_values":[{"text":"(MiAaPQ)AAI9712382","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84873","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":["Mitchell, David Michael"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:17Z","10000-01-01","1996"]},{"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/2142/84873","(MiAaPQ)AAI9712382"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Cytochrome c oxidase of R. sphaeroides has been purified using affinity methods and studied using site-directed mutagenesis coupled with a wide variety of biophysical characterization methods. 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