Item Details

abstract

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.

subject

Cysteine Desulfurases

Fe-S Clusters

Gram-positive bacteria

Sulfur trafficking

contributor

Selbach, Bruna (author)

Dos Santos, Patricia C (committee chair)

Colyer, Christa (committee member)

Alexander, Rebecca W (committee member)

Bierbach, Ulrich (committee member)

Poole, Leslie B (committee member)

date

2014-01-15T09:35:34Z (accessioned)

2015-01-15T09:30:09Z (available)

2013 (issued)

degree

Chemistry (discipline)

embargo

2015-01-15 (terms)

identifier

http://hdl.handle.net/10339/39132 (uri)

language

en (iso)

publisher

Wake Forest University

title

Cysteine Desulfurases Mediating Sulfur Trafficking for the Biosynthesis of Fe-S Clusters

type

Dissertation