{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84482"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84482","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The Protein Redesign Approach to Modeling Manganese Peroxidase","abstract":"The active site tryptophans were removed from MnCcP in order to investigate the roles of Trp51 and Trp191 in MnP activity. These residues are phenyalanines in MnP. In CcP mutants without the Mn(II)-binding site, Trp191 and Trp51 greatly influence the lifetime of the porphyrin pi-cation radical. The W51F, W191F, and W51F/W191F double mutations were incorporated along with the binding-site mutations (G41E,V45E,H181D) to create MnCcP(W51F), MnCcP(W191F) and MnCcP(W51F, W191F). The MnP activity observed varied between mutants and increased activity was observed for MnCcP(W51F,W191F) and MnCcP(W51F). The trend in activity reflects the extent of compound II stabilization present for the various mutants. MnC cP(W51F,W191F) is the most active protein model of MnP constructed to date.","abstract_html":"The active site tryptophans were removed from MnCcP in order to investigate the roles of Trp51 and Trp191 in MnP activity. These residues are phenyalanines in MnP. In CcP mutants without the Mn(II)-binding site, Trp191 and Trp51 greatly influence the lifetime of the porphyrin pi-cation radical. The W51F, W191F, and W51F/W191F double mutations were incorporated along with the binding-site mutations (G41E,V45E,H181D) to create MnCcP(W51F), MnCcP(W191F) and MnCcP(W51F, W191F). The MnP activity observed varied between mutants and increased activity was observed for MnCcP(W51F,W191F) and MnCcP(W51F). The trend in activity reflects the extent of compound II stabilization present for the various mutants. MnC cP(W51F,W191F) is the most active protein model of MnP constructed to date.","abstract_has_math":false,"creators":["Gengenbach, Alan James"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Lu, Yi"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:14:45Z","date_published":"2015-09-25T22:14:45Z","updated_at":"2026-07-22T22:26:23Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9990003"],"render_values":[{"text":"(MiAaPQ)AAI9990003","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84482","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":["Gengenbach, Alan James"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:14:45Z","10000-01-01","2000"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"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/2142/84482","(MiAaPQ)AAI9990003"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The active site tryptophans were removed from MnCcP in order to investigate the roles of Trp51 and Trp191 in MnP activity. These residues are phenyalanines in MnP. In CcP mutants without the Mn(II)-binding site, Trp191 and Trp51 greatly influence the lifetime of the porphyrin pi-cation radical. The W51F, W191F, and W51F/W191F double mutations were incorporated along with the binding-site mutations (G41E,V45E,H181D) to create MnCcP(W51F), MnCcP(W191F) and MnCcP(W51F, W191F). The MnP activity observed varied between mutants and increased activity was observed for MnCcP(W51F,W191F) and MnCcP(W51F). The trend in activity reflects the extent of compound II stabilization present for the various mutants. MnC cP(W51F,W191F) is the most active protein model of MnP constructed to date.","Made available in DSpace on 2015-09-25T22:14:45Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9990003.pdf: 5897619 bytes, checksum: a22ee3786f07ab43564774c9d67a08b6 (MD5) Previous issue date: 2000","Embargo set by: Seth Robbins for item 85763 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","139 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000."]},{"key":"dc:title","label":"Title","values":["The Protein Redesign Approach to Modeling Manganese Peroxidase"]}]}],"canonical_facts":{"dc:contributor":["Lu, Yi"],"dc:creator":["Gengenbach, Alan James"],"dc:date":["2015-09-25T22:14:45Z","10000-01-01","2000"],"dc:description":["The active site tryptophans were removed from MnCcP in order to investigate the roles of Trp51 and Trp191 in MnP activity. These residues are phenyalanines in MnP. In CcP mutants without the Mn(II)-binding site, Trp191 and Trp51 greatly influence the lifetime of the porphyrin pi-cation radical. The W51F, W191F, and W51F/W191F double mutations were incorporated along with the binding-site mutations (G41E,V45E,H181D) to create MnCcP(W51F), MnCcP(W191F) and MnCcP(W51F, W191F). The MnP activity observed varied between mutants and increased activity was observed for MnCcP(W51F,W191F) and MnCcP(W51F). The trend in activity reflects the extent of compound II stabilization present for the various mutants. MnC cP(W51F,W191F) is the most active protein model of MnP constructed to date.","Made available in DSpace on 2015-09-25T22:14:45Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9990003.pdf: 5897619 bytes, checksum: a22ee3786f07ab43564774c9d67a08b6 (MD5) Previous issue date: 2000","Embargo set by: Seth Robbins for item 85763 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","139 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000."],"dc:identifier":["http://hdl.handle.net/2142/84482","(MiAaPQ)AAI9990003"],"dc:language":["eng"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["The Protein Redesign Approach to Modeling Manganese Peroxidase"],"dc:type":["text"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:23Z"}