Binding Affinity of Flavins to the Dehydrogenase Domain of SpNOX

<p>NADPH oxidases (NOX’s) are enzymes that catalyze the production of superoxide through single electron transfer. This superoxide production leads to the production of other reactive oxygen species (ROS). ROS affect many metabolic processes throughout the body that can cause several different diseases, making this an ideal target for drug discovery. The general structure of NOX contains a transmembrane (TM) domain and a dehydrogenase (DH) domain connected by a linker. The DH domain contains binding sites for FAD and NADPH/NADH that both participate in the electron transfer necessary for producing superoxide. Structural information of NOX’s is still relatively new to the scientific community. A recent structure of CsNOX (<em>cyanobacterial</em> NOX) provided new structural information, but atomic coordinate clashes between FAD, NADPH and multiple sidechains still raises questions on actual structural activity.¹ The structural similarities within the NOX family make SpNOX (<em>Streptococcus pneumoniae</em> NOX), a bacterial NOX homolog with vigorous activity in detergents, ideal for use to identify NOX properties. Homologous to FNR, FAD is the end of the redox chain until its transfer to the hemes within the transmembrane domain. The FAD binding sites could serve as focus point in drug discovery for NOX’s. In this study, we examine the binding affinity of flavins (FAD, FMN, and riboflavin) to the DH domain of NOX.</p>

Name thesis:degree_name

Master of Science in Chemical Sciences (MSCB)

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Chemistry

Year dc:date.available

2021

Author dc:creator

• Williams, Quinesha

Contributors dc:contributor

• Susan M. E. Smith
• Thomas Leeper
• Michael Van Dyke

• NADPH oxidase
• FAD
• isothermal titration calorimetry
• binding affinity
• Biochemistry
• Chemistry

Repository record dc:identifier

https://digitalcommons.kennesaw.edu/mscs_etd/39

OAI identifier oai:identifier

oai:digitalcommons.kennesaw.edu:mscs_etd-1040