{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85436"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85436","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Isolation and Characterization of Reactive Heme -Oxygen Intermediates in Cytochrome P450 Catalysis","abstract":"The P450 monooxygenases, and specifically the intermediate species formed within the course of their reaction cycle, are formidable oxidants, capable of a diverse range of chemical reactions. As the cryoradiolytic methodologies prove a convenient tool for the isolation and stabilization of heme-oxygen intermediates, a range of substrate probes has been coupled to these studies in order to assess their role in known P450 reactions. This provides a template not only for the assorted reactivity of the P450 superfamily, but the utilization of related intermediates in other metalloenzyme systems. In order to assess the commonality of these intermediates, the ferric-peroxo species have also been generated in a number of other heme enzyme systems in order to assess the role of proximal ligand and distal pocket in the proton mediated functionalization of these reactive intermediates, and thus, to compare these to the reaction mechanism associated with the P450 monoxygenases.","abstract_html":"The P450 monooxygenases, and specifically the intermediate species formed within the course of their reaction cycle, are formidable oxidants, capable of a diverse range of chemical reactions. As the cryoradiolytic methodologies prove a convenient tool for the isolation and stabilization of heme-oxygen intermediates, a range of substrate probes has been coupled to these studies in order to assess their role in known P450 reactions. This provides a template not only for the assorted reactivity of the P450 superfamily, but the utilization of related intermediates in other metalloenzyme systems. In order to assess the commonality of these intermediates, the ferric-peroxo species have also been generated in a number of other heme enzyme systems in order to assess the role of proximal ligand and distal pocket in the proton mediated functionalization of these reactive intermediates, and thus, to compare these to the reaction mechanism associated with the P450 monoxygenases.","abstract_has_math":false,"creators":["Makris, Thomas Michael"],"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":["Sligar, Stephen G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:05Z","date_published":"2015-09-25T22:46:05Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3130976"],"render_values":[{"text":"(MiAaPQ)AAI3130976","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85436","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Sligar, Stephen G."]},{"key":"dc:creator","label":"Author","values":["Makris, Thomas Michael"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:46:05Z","10000-01-01","2004"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics and Computational Biology"]},{"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"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/85436","(MiAaPQ)AAI3130976"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The P450 monooxygenases, and specifically the intermediate species formed within the course of their reaction cycle, are formidable oxidants, capable of a diverse range of chemical reactions. As the cryoradiolytic methodologies prove a convenient tool for the isolation and stabilization of heme-oxygen intermediates, a range of substrate probes has been coupled to these studies in order to assess their role in known P450 reactions. This provides a template not only for the assorted reactivity of the P450 superfamily, but the utilization of related intermediates in other metalloenzyme systems. In order to assess the commonality of these intermediates, the ferric-peroxo species have also been generated in a number of other heme enzyme systems in order to assess the role of proximal ligand and distal pocket in the proton mediated functionalization of these reactive intermediates, and thus, to compare these to the reaction mechanism associated with the P450 monoxygenases.","Made available in DSpace on 2015-09-25T22:46:05Z (GMT). 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As the cryoradiolytic methodologies prove a convenient tool for the isolation and stabilization of heme-oxygen intermediates, a range of substrate probes has been coupled to these studies in order to assess their role in known P450 reactions. This provides a template not only for the assorted reactivity of the P450 superfamily, but the utilization of related intermediates in other metalloenzyme systems. In order to assess the commonality of these intermediates, the ferric-peroxo species have also been generated in a number of other heme enzyme systems in order to assess the role of proximal ligand and distal pocket in the proton mediated functionalization of these reactive intermediates, and thus, to compare these to the reaction mechanism associated with the P450 monoxygenases.","Made available in DSpace on 2015-09-25T22:46:05Z (GMT). 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