BACKGROUND: Glutathione-dependent catalysis is a metabolic adaptation to chemical
challenges encountered by all life forms. In the course of evolution, nature optimized …

Abstract Thioredoxins (Trxs), glutaredoxins (Grxs), and peroxiredoxins (Prxs) have been
characterized as electron donors, guards of the intracellular redox state, and “antioxidants” …

The biogenesis of iron–sulfur (Fe/S) proteins in eukaryotes is a multistage,
multicompartment process that is essential for a broad range of cellular functions, including …

Glutaredoxins catalyze the reduction of disulfides and are key players in redox metabolism
and regulation. While important insights were gained regarding the reduction of glutathione …

Glutaredoxin, Grx, is a small protein containing an active site cysteine pair and was
discovered in 1976 by Arne Holmgren. The Grx system, comprised of Grx, glutathione …

Glutathione (GSH) is the most abundant cellular tripeptide (L‐γ‐glutamate‐L‐cysteinyl‐
glycine) which is as critical as oxygen and water. This low molecular mass antioxidant has a …

Over the last decade fundamentally new features have been revealed for the participation of
glutathione and glutathione-dependent enzymes (glutathione transferase and glutaredoxin) …

Work during the past 14 years has shown that mitochondria are the primary site for the
biosynthesis of iron–sulfur (Fe/S) clusters. In fact, it is this process that renders mitochondria …

The essential process of iron-sulfur (Fe/S) cluster assembly (ISC) in mitochondria occurs in
three major phases. First,[2Fe-2S] clusters are synthesized on the scaffold protein ISCU2; …

Iron has emerged as a significant cause of neurotoxicity in several neurodegenerative
conditions, including Alzheimer's disease (AD), Parkinson's disease (PD), sporadic …