{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84032"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84032","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Part I. The Synthesis of Hyaluronan Oligosaccharides and the Mild Cleavage of 2-Amino-2-Deoxy-D-Glucoside Methoxycarbonyl Derivatives With Methytrichlorosilane. Part II. The Design and Engineering of a Manganese Binding Site in Cytochrome C Peroxidase","abstract":"Part II. A manganese binding site has been creating in CcP corresponding to the Mn-binding domain in MnP by site directed mutagenesis. Several spectroscopic techniques including paramagnetic NMR and EPR were employed to characterize the CcP mutant (MnCcP). The data is consistent with a newly formed metal site that binds a single Mn2+ near the heme periphery. Wild-type CcP exhibits none of the spectroscopic features as MnCcP. The new binding site provides a five-fold increase in Mn-oxidizing activity in MnCcP over that of WTCcP.","abstract_html":"Part II. A manganese binding site has been creating in CcP corresponding to the Mn-binding domain in MnP by site directed mutagenesis. Several spectroscopic techniques including paramagnetic NMR and EPR were employed to characterize the CcP mutant (MnCcP). The data is consistent with a newly formed metal site that binds a single Mn2+ near the heme periphery. Wild-type CcP exhibits none of the spectroscopic features as MnCcP. The new binding site provides a five-fold increase in Mn-oxidizing activity in MnCcP over that of WTCcP.","abstract_has_math":false,"creators":["Yeung, Bryan K.S."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Petillo, Peter A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:12:28Z","date_published":"2015-09-25T22:12:28Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3017260"],"render_values":[{"text":"(MiAaPQ)AAI3017260","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84032","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Petillo, Peter A."]},{"key":"dc:creator","label":"Author","values":["Yeung, Bryan K.S."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:12:28Z","10000-01-01","2001"]},{"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/2142/84032","(MiAaPQ)AAI3017260"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Part II. A manganese binding site has been creating in CcP corresponding to the Mn-binding domain in MnP by site directed mutagenesis. Several spectroscopic techniques including paramagnetic NMR and EPR were employed to characterize the CcP mutant (MnCcP). The data is consistent with a newly formed metal site that binds a single Mn2+ near the heme periphery. Wild-type CcP exhibits none of the spectroscopic features as MnCcP. The new binding site provides a five-fold increase in Mn-oxidizing activity in MnCcP over that of WTCcP.","Made available in DSpace on 2015-09-25T22:12:28Z (GMT). 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The Design and Engineering of a Manganese Binding Site in Cytochrome C Peroxidase"]}]}],"canonical_facts":{"dc:contributor":["Petillo, Peter A."],"dc:creator":["Yeung, Bryan K.S."],"dc:date":["2015-09-25T22:12:28Z","10000-01-01","2001"],"dc:description":["Part II. A manganese binding site has been creating in CcP corresponding to the Mn-binding domain in MnP by site directed mutagenesis. Several spectroscopic techniques including paramagnetic NMR and EPR were employed to characterize the CcP mutant (MnCcP). The data is consistent with a newly formed metal site that binds a single Mn2+ near the heme periphery. Wild-type CcP exhibits none of the spectroscopic features as MnCcP. The new binding site provides a five-fold increase in Mn-oxidizing activity in MnCcP over that of WTCcP.","Made available in DSpace on 2015-09-25T22:12:28Z (GMT). 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