Author ORCID Identifier
Year of Publication
Master of Science (MS)
Arts and Sciences
Dr. Anne-Frances Miller
Flavodoxin is a small, highly stable protein that contain a single FMN cofactor used to transfer single electrons at low potentials. The organism Rhodopseudomonas palustris contains a long-chain flavodoxin. Long-chain flavodoxins are characterized by a 20 amino acid loop that is proposed to allow interactions with partner proteins. We plan to utilize this protein as a model to build our repertoire with protein fluorination and fluorine NMR in flavoproteins. This tool kit will then be applied to the study of a partner protein of interest that is capable of performing electron bifurcation. We have incorporated m-fluoro tyrosine into flavodoxin and carried out 19F NMR studies. We have completed peak assignment via mutation, observed temperature-based dynamics, observed flavin tyrosine interactions during flavin reduction, monitored reduction titrations optically, and observed a single residue in slow exchange which was studied using 2D exchange spectroscopy. All of these studied have worked to further our understanding of flavodoxin. Our hope is that these works can be used to further understand of protein conformational changes, dynamics, and partner protein interactions in bifurcating electron transfer proteins from Rhodopseudomonas palustris
Digital Object Identifier (DOI)
National Science Foundation under CLP1808433 2018.
Varner, Taylor, "FLAVODOXIN, THE HYDROGEN ATOM OF FLAVOPROTEINS: A 19F NMR STUDY OF DYNAMICS AND CONFORMATIONAL CHANGES UTILIZING FLAVODOXIN FROM RHODOPSEUDOMONAS PALUSTRIS" (2020). Theses and Dissertations--Chemistry. 134.