{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/70164"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/70164","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Defined Dimensional Alterations in Enzyme Substrates. Synthesis and Enzymatic Evaluation of Some Lin-Naphthopurines","abstract":"The development of methodology for the regioselective synthesis of tetra-beta-substituted naphthalenes via a combination of bicyclo{4.2.0}octa-1,3,5-triene and aryl trimethylsilyl chemistry led to the synthesis of benzimidazo{5,6-g}-8H-quinazolin-9-one and benzimidazo{5,6-g}-6H,8H-quinazoline-7,9-dione 4.8 (ANGSTROM) laterally extended dimensional derivatives of hypoxanthine and xanthine. These compounds, lin-naphthohypoxanthine and lin-naphthoxanthine, exhibited intense fluorescence. lin-Naphthoxanthine was not oxidized to lin-naphthouric acid by xanthine oxidase but functioned as a noncompetitive inhibitor. However, lin-naphthohypoxanthine was readily converted to lin-naphthoxanthine by xanthine oxidase. In this reaction, lin-naphthohypoxanthine functioned as a competitive inhibitor of xanthine oxidase. The enzymatic results for the naphthologs when compared with the benzologs demonstrate, in part, a useful application of defined dimensional probes for determining the limiting spatial restrictions of the binding region for xanthine oxidase.","abstract_html":"The development of methodology for the regioselective synthesis of tetra-beta-substituted naphthalenes via a combination of bicyclo{4.2.0}octa-1,3,5-triene and aryl trimethylsilyl chemistry led to the synthesis of benzimidazo{5,6-g}-8H-quinazolin-9-one and benzimidazo{5,6-g}-6H,8H-quinazoline-7,9-dione 4.8 (ANGSTROM) laterally extended dimensional derivatives of hypoxanthine and xanthine. These compounds, lin-naphthohypoxanthine and lin-naphthoxanthine, exhibited intense fluorescence. lin-Naphthoxanthine was not oxidized to lin-naphthouric acid by xanthine oxidase but functioned as a noncompetitive inhibitor. However, lin-naphthohypoxanthine was readily converted to lin-naphthoxanthine by xanthine oxidase. In this reaction, lin-naphthohypoxanthine functioned as a competitive inhibitor of xanthine oxidase. The enzymatic results for the naphthologs when compared with the benzologs demonstrate, in part, a useful application of defined dimensional probes for determining the limiting spatial restrictions of the binding region for xanthine oxidase.","abstract_has_math":false,"creators":["Moder, Kenneth Philip"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-15T23:17:25Z","date_published":"2014-12-15T23:17:25Z","updated_at":"2026-07-22T22:26:02Z","subjects":["Chemistry, Organic"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8203537"],"render_values":[{"text":"(UMI)AAI8203537","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/70164","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Moder, Kenneth Philip"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-15T23:17:25Z","10000-01-01","1981"]},{"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, Organic"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/70164","(UMI)AAI8203537"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The development of methodology for the regioselective synthesis of tetra-beta-substituted naphthalenes via a combination of bicyclo{4.2.0}octa-1,3,5-triene and aryl trimethylsilyl chemistry led to the synthesis of benzimidazo{5,6-g}-8H-quinazolin-9-one and benzimidazo{5,6-g}-6H,8H-quinazoline-7,9-dione 4.8 (ANGSTROM) laterally extended dimensional derivatives of hypoxanthine and xanthine. These compounds, lin-naphthohypoxanthine and lin-naphthoxanthine, exhibited intense fluorescence. lin-Naphthoxanthine was not oxidized to lin-naphthouric acid by xanthine oxidase but functioned as a noncompetitive inhibitor. However, lin-naphthohypoxanthine was readily converted to lin-naphthoxanthine by xanthine oxidase. In this reaction, lin-naphthohypoxanthine functioned as a competitive inhibitor of xanthine oxidase. The enzymatic results for the naphthologs when compared with the benzologs demonstrate, in part, a useful application of defined dimensional probes for determining the limiting spatial restrictions of the binding region for xanthine oxidase.","Investigation of alternative synthetic routes to the lin-naphthopurines via preformed tetra-beta-substituted naphthalenes or other benzenoid precursors reinforced the intrinsically unfavorable substitution pattern of naphthalene and reminded us of the problems associated with the formation of halomethyl groups nitrogen-substituted aromatics. In exploring the alternative synthetic routes several 4,5-disubstituted-1,2-di(halomethyl)-benzene compounds and their potential precursors were made wherein the halogen was Cl, Br, I and the disubstitution was with H, OMe, NHAc, NHCOPh, or N(Ac)(,2).","Made available in DSpace on 2014-12-15T23:17:25Z (GMT). No. of bitstreams: 1 8203537.pdf: 4109960 bytes, checksum: c386f3ebfe8820ef085b3a1ebc2e737f (MD5) Previous issue date: 1981","Embargo set by: Seth Robbins for item 70330 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","159 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1981."]},{"key":"dc:title","label":"Title","values":["Defined Dimensional Alterations in Enzyme Substrates. Synthesis and Enzymatic Evaluation of Some Lin-Naphthopurines"]}]}],"canonical_facts":{"dc:creator":["Moder, Kenneth Philip"],"dc:date":["2014-12-15T23:17:25Z","10000-01-01","1981"],"dc:description":["The development of methodology for the regioselective synthesis of tetra-beta-substituted naphthalenes via a combination of bicyclo{4.2.0}octa-1,3,5-triene and aryl trimethylsilyl chemistry led to the synthesis of benzimidazo{5,6-g}-8H-quinazolin-9-one and benzimidazo{5,6-g}-6H,8H-quinazoline-7,9-dione 4.8 (ANGSTROM) laterally extended dimensional derivatives of hypoxanthine and xanthine. These compounds, lin-naphthohypoxanthine and lin-naphthoxanthine, exhibited intense fluorescence. lin-Naphthoxanthine was not oxidized to lin-naphthouric acid by xanthine oxidase but functioned as a noncompetitive inhibitor. However, lin-naphthohypoxanthine was readily converted to lin-naphthoxanthine by xanthine oxidase. In this reaction, lin-naphthohypoxanthine functioned as a competitive inhibitor of xanthine oxidase. The enzymatic results for the naphthologs when compared with the benzologs demonstrate, in part, a useful application of defined dimensional probes for determining the limiting spatial restrictions of the binding region for xanthine oxidase.","Investigation of alternative synthetic routes to the lin-naphthopurines via preformed tetra-beta-substituted naphthalenes or other benzenoid precursors reinforced the intrinsically unfavorable substitution pattern of naphthalene and reminded us of the problems associated with the formation of halomethyl groups nitrogen-substituted aromatics. In exploring the alternative synthetic routes several 4,5-disubstituted-1,2-di(halomethyl)-benzene compounds and their potential precursors were made wherein the halogen was Cl, Br, I and the disubstitution was with H, OMe, NHAc, NHCOPh, or N(Ac)(,2).","Made available in DSpace on 2014-12-15T23:17:25Z (GMT). No. of bitstreams: 1 8203537.pdf: 4109960 bytes, checksum: c386f3ebfe8820ef085b3a1ebc2e737f (MD5) Previous issue date: 1981","Embargo set by: Seth Robbins for item 70330 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","159 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1981."],"dc:identifier":["http://hdl.handle.net/2142/70164","(UMI)AAI8203537"],"dc:subject":["Chemistry, Organic"],"dc:title":["Defined Dimensional Alterations in Enzyme Substrates. Synthesis and Enzymatic Evaluation of Some Lin-Naphthopurines"],"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":"2026-07-22T22:26:02Z"}