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oai:null:10339/391322026-09-18T12:38:39Zcom_10339_14934col_10339_38132

Selbach, Bruna 2014-01-15T09:35:34Z 2015-01-15T09:30:09Z 2013 https://wakespace.lib.wfu.edu/handle/10339/39132 Bacteria have developed systems to safely traffic intracellular iron and sulfur for the biosynthesis of Fe-S clusters. These dedicated pathways guarantee the recruitment of individual components, their assembly into clusters and delivery to final targets. Despite variations on pathway composition, all systems identified to date include the participation of at least a cysteine desulfurase and an Fe-S cluster scaffold. The first step in sulfur mobilization for the assembly of Fe-S clusters as well as other thiocofactors within the cell involves a PLP-dependent enzymatic mechanism, catalyzed by cysteine desulfurases. There have been identified two groups of cysteine desulfurases: group I - NifS and IscS and group II - SufS and CsdA. Tertiary structural signature motifs within these groups provide a rationale for their catalytic differences and specific interactions that occurs between the cysteine desulfurases and sulfur acceptors. en Wake Forest University Cysteine Desulfurases Fe-S Clusters Gram-positive bacteria Sulfur trafficking Cysteine Desulfurases Mediating Sulfur Trafficking for the Biosynthesis of Fe-S Clusters Dissertation Dos Santos, Patricia C Colyer, Christa Alexander, Rebecca W Bierbach, Ulrich Poole, Leslie B Chemistry 2015-01-15 open.access