Abstract Iron–sulphur (Fe–S) clusters have long been recognized as essential and versatile
cofactors of proteins involved in catalysis, electron transport and sensing of ambient …

Iron/sulfur centers are key cofactors of proteins intervening in multiple conserved cellular
processes, such as gene expression, DNA repair, RNA modification, central metabolism and …

Iron-sulfur (Fe-S) clusters are ubiquitous cofactors composed of iron and inorganic sulfur.
They are required for the function of proteins involved in a wide range of activities, including …

The broad range of cellular activities carried out by Fe–S proteins means that they have a
central role in the life of most organisms. At the interface between biology and chemistry …

In plants iron–sulfur (Fe–S) proteins are found in the plastids, mitochondria, cytosol and
nucleus, where they are essential for numerous physiological and developmental …

These can be considered substituted versions of all-iron 36. Although MFe3S4 cores depart
from the familiar and efficient idealized symmetry of the Fe4S4 cubane structure, the …

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 …

The cysteine desulfurase IscS is a highly conserved master enzyme initiating sulfur transfer
via persulfide to a range of acceptor proteins involved in Fe-S cluster assembly, tRNA …

Background Frataxin, the mitochondrial protein deficient in Friedreich ataxia, a rare
autosomal recessive neurodegenerative disorder, is thought to be involved in multiple iron …

Environmental H2O2 creates several injuries in Escherichia coli, including the oxidative
conversion of dehydratase [4Fe–4S] clusters to an inactive [3Fe–4S] form. To protect itself …