Defined Dimensional Alterations in Enzyme Substrates. Synthesis and Enzymatic Evaluation of Some Lin-Naphthopurines

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Moder, Kenneth Philip

• Chemistry, Organic

Identifier

(UMI)AAI8203537

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70164