Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

Mitochondria play a key role in iron metabolism in that they synthesize heme, assemble iron–
sulfur (Fe/S) proteins, and participate in cellular iron regulation. Here, we review the latter …

Iron-sulfur (Fe/S) proteins are involved in a wide variety of cellular processes such as
enzymatic reactions, respiration, cofactor biosynthesis, ribosome biogenesis, regulation of …

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 …

Cellular depletion of the human protein frataxin is correlated with the neurodegenerative
disease Friedreich's ataxia and results in the inactivation of Fe− S cluster proteins. Most …

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

Abstract Iron-sulfur (Fe/S) clusters require a complex set of proteins to become assembled
and incorporated into apoproteins in a living cell. Researchers have described three distinct …

As essential organelles, mitochondria are intimately integrated into the metabolism of a
eukaryotic cell. The maintenance of the functional integrity of the mitochondrial proteome …

Iron–sulfur (Fe–S) clusters are prosthetic groups of proteins biosynthesized on scaffold
proteins by highly conserved multi-protein machineries. Biosynthesis of Fe–S clusters into …

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 …