Abstract Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are
involved in numerous cellular processes such as respiration, photosynthesis, metabolic …

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 …

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 …

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 …

Members of the bacterial and mitochondrial iron–sulfur cluster (ISC) assembly machinery
include the so-called A-type ISC proteins, which support the assembly of a subset of Fe/S …

Respiratory complex I (NADH: ubiquinone oxidoreductase) is a large mitochondrial inner
membrane enzyme consisting of 45 subunits and 8 iron-sulfur (Fe/S) clusters. While …

Many metabolic pathways and cellular processes occurring in most sub-cellular
compartments depend on the functioning of iron-sulfur (Fe-S) proteins, whose cofactors are …

Iron sulfur (Fe/S) proteins are ubiquitous and participate in multiple biological processes,
from photosynthesis to DNA repair. Iron and sulfur are highly reactive chemical species, and …

Most eukaryotes contain iron-sulfur cluster (ISC) assembly proteins related to
Saccharomyces cerevisiae Isa1 and Isa2. We show here that Isa1 but not Isa2 can be …