2026-09-21T23:43:20Zhttps://wakespace.lib.wfu.edu/server/oai/request

oai:null:10339/939182026-09-02T08:56:59Zcom_10339_14934col_10339_38132

Zheng, Chenkang 2019-05-24T08:35:36Z 2021-05-23T08:30:11Z 2019 https://wakespace.lib.wfu.edu/handle/10339/93918 Sulfur-containing biomolecules including iron-sulfur clusters, thio-nucleosides, and other thio-cofactors are critical players in several biological processes. The sulfur element present in these molecules is predominantly originated from L-cysteine through activation by cysteine desulfurases and is relayed to specific pathways involving the synthesis of thio-cofactors. In this dissertation, we reviewed recent methods for detection and quantification of bacterial thio-nucleosides used for structural and functional studies. These approaches provide experimental tools to uncover the interconnectivity of sulfur trafficking pathways and regulatory mechanisms employed in the synthesis of thio-nucleosides and iron-sulfur clusters. This study has also surveyed distinct modes of regulation across sulfur trafficking pathways in bacteria and explored the reactivities of cysteine desulfurases from Bacillus subtilis and Azotobacter vinelandii. Despite differences in biosynthetic schemes, these pathways are controlled by specific and dynamic protein-protein interactions and dependent on the availability of reaction components including cysteine and reducing equivalents. en Wake Forest University bacteria cysteine desulfurase Iron-sulfur cluster physiological reductant thio-cofactors thionucleosides Protein Specificity Dictates Proper Sulfur Transfer in the Biosynthesis of Thio-cofactors in Bacteria Dissertation Dos Santos, Patricia C. Zhang, Ke Alexander, Rebecca W. Comstock-Ferguson, Lindsay R. Hinze, Willie Chemistry 2021-05-23 open.access