{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/113341"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/113341","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Using myoglobin models of oxidases for mechanistic understanding of the oxygen reduction reaction","abstract":"Using state-of-the art time resolved structural methods like XFEL and a set of newly designed myoglobin modes, I have set out to understand aspects of the oxygen reduction reaction in metalloenzymes that have remained elusive. There are many pathways for the oxygen reduction reaction to take place in metalloenzymes like oxidases, but strangely, there is a high degree of variance in the active site of these enzymes. Studying the native enzymes has proven difficult using traditional methods due to the insoluble nature of oxidases along with many complicating features like multiple heme and transition metal binding sites. These issues complicate mechanistic studies due to replicating native function as transmembrane proteins and spectroscopy techniques because of the interference with the active site. I will show the benefits of using structural analogs of three oxidase active sites – each with unique and poorly understood features. Crystallographic techniques and XFEL have been used to answer outstanding questions in the field regarding short-lived intermediates in heme copper oxidases and the role of heteronuclear metal active sites. Cytochrome bd oxidase models have been used to make sense of many interesting – but isolated – observations of these peculiar enzymes. These studies come at a serendipitous time for cytochrome bd oxidases, as a recent discovery has made experts in this field rethink much of what they thought they knew about how this enzyme functions in organisms besides E. coli. It is my hope to fill some of those gaps and provide context for this reevaluation.","abstract_html":"Using state-of-the art time resolved structural methods like XFEL and a set of newly designed myoglobin modes, I have set out to understand aspects of the oxygen reduction reaction in metalloenzymes that have remained elusive. There are many pathways for the oxygen reduction reaction to take place in metalloenzymes like oxidases, but strangely, there is a high degree of variance in the active site of these enzymes. Studying the native enzymes has proven difficult using traditional methods due to the insoluble nature of oxidases along with many complicating features like multiple heme and transition metal binding sites. These issues complicate mechanistic studies due to replicating native function as transmembrane proteins and spectroscopy techniques because of the interference with the active site. I will show the benefits of using structural analogs of three oxidase active sites – each with unique and poorly understood features. Crystallographic techniques and XFEL have been used to answer outstanding questions in the field regarding short-lived intermediates in heme copper oxidases and the role of heteronuclear metal active sites. Cytochrome bd oxidase models have been used to make sense of many interesting – but isolated – observations of these peculiar enzymes. These studies come at a serendipitous time for cytochrome bd oxidases, as a recent discovery has made experts in this field rethink much of what they thought they knew about how this enzyme functions in organisms besides E. coli. It is my hope to fill some of those gaps and provide context for this reevaluation.","abstract_has_math":false,"creators":["Wells, Brady"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Lu, Yi"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2022,"date_issued":"2022-01-12T22:56:13Z","date_published":"2022-01-12T22:56:13Z","updated_at":"2026-07-22T22:24:53Z","subjects":["Metalloenzymes, Oxidases, Enzyme Engineering"],"languages":["en"],"rights":["N/A"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/113341","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Lu, Yi"]},{"key":"dc:creator","label":"Author","values":["Wells, Brady"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2022-01-12T22:56:13Z","2024-01-12T22:56:20Z","2021-07-23","2021-08"]},{"key":"dc:type","label":"Dc Type","values":["text","Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"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":["Metalloenzymes, Oxidases, Enzyme Engineering"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["N/A"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/113341"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Using state-of-the art time resolved structural methods like XFEL and a set of newly designed myoglobin modes, I have set out to understand aspects of the oxygen reduction reaction in metalloenzymes that have remained elusive. There are many pathways for the oxygen reduction reaction to take place in metalloenzymes like oxidases, but strangely, there is a high degree of variance in the active site of these enzymes. Studying the native enzymes has proven difficult using traditional methods due to the insoluble nature of oxidases along with many complicating features like multiple heme and transition metal binding sites. These issues complicate mechanistic studies due to replicating native function as transmembrane proteins and spectroscopy techniques because of the interference with the active site. I will show the benefits of using structural analogs of three oxidase active sites – each with unique and poorly understood features. Crystallographic techniques and XFEL have been used to answer outstanding questions in the field regarding short-lived intermediates in heme copper oxidases and the role of heteronuclear metal active sites. Cytochrome bd oxidase models have been used to make sense of many interesting – but isolated – observations of these peculiar enzymes. These studies come at a serendipitous time for cytochrome bd oxidases, as a recent discovery has made experts in this field rethink much of what they thought they knew about how this enzyme functions in organisms besides E. coli. It is my hope to fill some of those gaps and provide context for this reevaluation.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2023-08-01","The student, Brady Wells, accepted the attached license on 2021-07-20 at 14:08.","The student, Brady Wells, submitted this Thesis for approval on 2021-07-20 at 14:14.","This Thesis was approved for publication on 2021-07-23 at 09:38.","DSpace SAF Submission Ingestion Package generated from Vireo submission #17030 on 2022-01-12 at 13:05:22","Made available in DSpace on 2022-01-12T22:56:13Z (GMT). No. of bitstreams: 2 WELLS-THESIS-2021.pdf: 772647 bytes, checksum: 2fed2e9d65b2b88f0b9f2c472c4a3395 (MD5) LICENSE.txt: 4208 bytes, checksum: bbe157f6950c73ab454fee55f0e068d3 (MD5) Previous issue date: 2021-07-23","Embargo set by: Seth Robbins for item 121270 Lift date: 2024-01-12T22:56:20Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited"]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Using myoglobin models of oxidases for mechanistic understanding of the oxygen reduction reaction"]}]}],"canonical_facts":{"dc:contributor":["Lu, Yi"],"dc:creator":["Wells, Brady"],"dc:date":["2022-01-12T22:56:13Z","2024-01-12T22:56:20Z","2021-07-23","2021-08"],"dc:description":["Using state-of-the art time resolved structural methods like XFEL and a set of newly designed myoglobin modes, I have set out to understand aspects of the oxygen reduction reaction in metalloenzymes that have remained elusive. There are many pathways for the oxygen reduction reaction to take place in metalloenzymes like oxidases, but strangely, there is a high degree of variance in the active site of these enzymes. Studying the native enzymes has proven difficult using traditional methods due to the insoluble nature of oxidases along with many complicating features like multiple heme and transition metal binding sites. These issues complicate mechanistic studies due to replicating native function as transmembrane proteins and spectroscopy techniques because of the interference with the active site. I will show the benefits of using structural analogs of three oxidase active sites – each with unique and poorly understood features. Crystallographic techniques and XFEL have been used to answer outstanding questions in the field regarding short-lived intermediates in heme copper oxidases and the role of heteronuclear metal active sites. Cytochrome bd oxidase models have been used to make sense of many interesting – but isolated – observations of these peculiar enzymes. These studies come at a serendipitous time for cytochrome bd oxidases, as a recent discovery has made experts in this field rethink much of what they thought they knew about how this enzyme functions in organisms besides E. coli. It is my hope to fill some of those gaps and provide context for this reevaluation.","Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2023-08-01","The student, Brady Wells, accepted the attached license on 2021-07-20 at 14:08.","The student, Brady Wells, submitted this Thesis for approval on 2021-07-20 at 14:14.","This Thesis was approved for publication on 2021-07-23 at 09:38.","DSpace SAF Submission Ingestion Package generated from Vireo submission #17030 on 2022-01-12 at 13:05:22","Made available in DSpace on 2022-01-12T22:56:13Z (GMT). No. of bitstreams: 2 WELLS-THESIS-2021.pdf: 772647 bytes, checksum: 2fed2e9d65b2b88f0b9f2c472c4a3395 (MD5) LICENSE.txt: 4208 bytes, checksum: bbe157f6950c73ab454fee55f0e068d3 (MD5) Previous issue date: 2021-07-23","Embargo set by: Seth Robbins for item 121270 Lift date: 2024-01-12T22:56:20Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited"],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/2142/113341"],"dc:language":["en"],"dc:rights":["N/A"],"dc:subject":["Metalloenzymes, Oxidases, Enzyme Engineering"],"dc:title":["Using myoglobin models of oxidases for mechanistic understanding of the oxygen reduction reaction"],"dc:type":["text","Thesis"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:24:53Z"}