The synthesis and trafficking of iron-sulfur (Fe-S) clusters in both prokaryotes and
eukaryotes requires coordination within an expanding network of proteins that function in the …

Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme
cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all …

Members of the monothiol glutaredoxin family and members of the BolA-like protein family
have recently emerged as specific interacting partners involved in iron-sulfur protein …

The Bol2 homolog Fra2 and monothiol glutaredoxin Grx4 together play essential roles in
regulating iron homeostasis in Schizosaccharomyces pombe. In vivo studies indicate that …

Among the thioredoxin superfamily of proteins, the observation that numerous glutaredoxins
bind iron-sulphur (Fe/S) clusters is one of the more recent and major developments …

Abstract Iron–sulfur (Fe–S) clusters are inorganic ubiquitous and ancient cofactors. Fe–S-
bound proteins contribute to most cellular processes, including DNA replication and …

This study examines the relative binding strength of a series of thiolate ligands to the
surfaces of zincblende CdSe/ZnS core/shell quantum dots (QDs) passivated by …

The NADH: ubiquinone oxidoreductase (respiratory complex I) is the main entry point for
electrons into the Escherichia coli aerobic respiratory chain. With its sophisticated setup of …

Apd1, a cytosolic yeast protein, and Aim32, its counterpart in the mitochondrial matrix, have
a C-terminal thioredoxin-like ferredoxin (TLF) domain and a widely divergent N-terminal …

Glutaredoxins (Grxs), ubiquitous redox enzymes belonging to the thioredoxin family,
catalyze the reduction of thiol-disulfide exchange reactions in a glutathione-dependent …