The essential function of ACP is not related to mitochondrial fatty acid and lipoic acid synthesis, but rather an evolutionarily-conserved role in iron sulfur cluster biogenesis.

Mitochondrial proteins Nfu1 and BolA3 mediate the transfer of preformed [4Fe-4S] clusters within the mitochondria to recipient proteins to shield clusters from oxidative damage during transfer.

The intracellular network that distributes iron-sulfur clusters in bacteria is surprisingly 'plug and play' with iron-sulfur enzymes acquired from distantly related species, whereas the intracellular electron transfer network often needs plug adapters to connect with foreign enzymes.

Cell biological, biochemical and structural studies reveal the mechanistic roles of two new mitochondrial iron-sulfur protein assembly factors, explaining the patho-biochemical defects of affected patients.

Two newly identified assembly factors for the ribosome-associated iron-sulfur protein Rli1 reveal a general mechanism for how the cytosolic iron-sulfur protein assembly (CIA) machinery recruits apoproteins.

Spermidine-mediated superoxide generation affects iron homeostasis in Escherichia coli.

Malaria parasites have simplified and adapted their mitochondrial metabolism to lack fatty acid synthesis but retain an unusual acyl carrier protein required for stability of the core iron-sulfur cluster biogenesis complex.

HSCB could be activated by PI3K signaling to facilitate FOG1 nuclear translocation to promote human erythropoiesis and megakaryopoiesis, highlighting an important, previously unrecognized iron–sulfur cluster delivery independent function of HSCB.

In vivo studies reveal that mitochondrial Complex I deficiencies induce iron misregulation and liver iron overload that may contribute to neurodegeneration in mitochondrial disease mice, and that iron restriction is effective in reducing disease progression.