{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85460"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85460","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigation of the Interaction Between Cytochrome b(H) and the Q(i)-Site in Rhodobacter Sphaeroides","abstract":"In characterization of strains generated with mutations at the Q i-site, it was noticed that several paradoxical properties could not be readily explained under current paradigms of mechanism, leading to a reinvestigation of the thermodynamic properties of the main redox partners involved---heme bH and the SQ---and the mechanistic consequences of mutation in key residues. Notable findings of this work are that the pH dependence of the midpoint potential of cytochrome bH differs substantially from what was published previously; a high potential component of bH remains even in the presence of Antimycin, and the thermodynamic properties of bH are substantially modified in strains with mutations at Asparagine 221. There also appears to be substantial redox cooperatively between the hemes of the complex, which is more pronounced in some of the mutants studied. The relationship between b150 and the Qi site SQ was also investigated.","abstract_html":"In characterization of strains generated with mutations at the Q i-site, it was noticed that several paradoxical properties could not be readily explained under current paradigms of mechanism, leading to a reinvestigation of the thermodynamic properties of the main redox partners involved---heme bH and the SQ---and the mechanistic consequences of mutation in key residues. Notable findings of this work are that the pH dependence of the midpoint potential of cytochrome bH differs substantially from what was published previously; a high potential component of bH remains even in the presence of Antimycin, and the thermodynamic properties of bH are substantially modified in strains with mutations at Asparagine 221. There also appears to be substantial redox cooperatively between the hemes of the complex, which is more pronounced in some of the mutants studied. The relationship between b150 and the Qi site SQ was also investigated.","abstract_has_math":false,"creators":["Holland, J. Todd"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics and Computational Biology","degree_department":null,"school":null,"contributors":["Anthony R. Crofts"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:10Z","date_published":"2015-09-25T22:46:10Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3290248"],"render_values":[{"text":"(MiAaPQ)AAI3290248","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85460","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Anthony R. Crofts"]},{"key":"dc:creator","label":"Author","values":["Holland, J. 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Notable findings of this work are that the pH dependence of the midpoint potential of cytochrome bH differs substantially from what was published previously; a high potential component of bH remains even in the presence of Antimycin, and the thermodynamic properties of bH are substantially modified in strains with mutations at Asparagine 221. There also appears to be substantial redox cooperatively between the hemes of the complex, which is more pronounced in some of the mutants studied. The relationship between b150 and the Qi site SQ was also investigated.","Made available in DSpace on 2015-09-25T22:46:10Z (GMT). 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Todd"],"dc:date":["2015-09-25T22:46:10Z","10000-01-01","2007"],"dc:description":["In characterization of strains generated with mutations at the Q i-site, it was noticed that several paradoxical properties could not be readily explained under current paradigms of mechanism, leading to a reinvestigation of the thermodynamic properties of the main redox partners involved---heme bH and the SQ---and the mechanistic consequences of mutation in key residues. Notable findings of this work are that the pH dependence of the midpoint potential of cytochrome bH differs substantially from what was published previously; a high potential component of bH remains even in the presence of Antimycin, and the thermodynamic properties of bH are substantially modified in strains with mutations at Asparagine 221. There also appears to be substantial redox cooperatively between the hemes of the complex, which is more pronounced in some of the mutants studied. The relationship between b150 and the Qi site SQ was also investigated.","Made available in DSpace on 2015-09-25T22:46:10Z (GMT). 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