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 …

Iron is a crucial transition metal for virtually all life. Two major destinations of iron within
mammalian cells are the cytosolic iron-storage protein, ferritin, and mitochondria. In …

Abstract Iron-sulfur (Fe-S) clusters are essential protein cofactors whose biosynthetic defects
lead to severe diseases among which is Friedreich's ataxia caused by impaired expression …

Iron–sulfur (Fe/S) clusters (ISCs) are redox-active protein cofactors that their synthesis,
transfer, and insertion into target proteins require many components. Mitochondrial ISC …

Abstract Iron–sulfur (Fe–S) clusters are versatile protein cofactors that require numerous
components for their synthesis and insertion into apoproteins. In eukaryotes, maturation of …

Fe–S clusters are partners in the origin of life that predate cells, acetyl-CoA metabolism,
DNA, and the RNA world. The double helix solved the mystery of DNA replication by base …

Abstract Iron–sulfur (Fe–S) clusters are ancient, ubiquitous cofactors composed of iron and
inorganic sulfur. The combination of the chemical reactivity of iron and sulfur, together with …

Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of
eukaryotes. Numerous bacterial functions have been maintained inside the organelles …

In eukaryotes, sulfur is mobilized for incorporation into multiple biosynthetic pathways by a
cysteine desulfurase complex that consists of a catalytic subunit (NFS1), LYR protein …

Maturation of iron–sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo
synthesis of [2Fe–2S] clusters on the mitochondrial scaffold protein Isu1 requires the …