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 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.

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.

PINK1 deficiency in Parkinson's disease models causes toxic oxidized and iron-depleted CISD1 yet CISD1 removal benefits PINK1 mutant Drosophila indicating its potential as a therapeutic target for mitochondrial dysfunction and neurodegeneration.

Plasmodium falciparum apicoplast SufS is required for both iron-sulfur synthesis and tRNA modification by MnmA, a novel paradigm that is likely to apply to other plastid-containing organisms.

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.

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.

X-ray crystal structures capture ATP-dependent chalcogenide exchange from selenocyanate at the nitrogenase Fe protein cluster in the absence of the MoFe protein, an unexpected result as the Fe protein cluster is not traditionally perceived as a site of substrate binding.

Cryo-EM and particle classification techniques reveal how the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima multimerizes to connect distant active sites and reveal different conformational states that enable catalysis.