4Fe-4S cluster assembles on NUBP2:NUBP1 scaffold

Stable Identifier
Reaction [omitted]
Homo sapiens
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A [4Fe-4S] cluster is assembled on a scaffold composed of the P-loop NTPases NUBP2 (CFD1 in yeast) and NUBP1 (Nbp35 in yeast) in a nucleotide-dependent fashion. The two proteins form a heterotetramer which transiently binds the [4Fe-4S] cluster in a bridged form between two subunits of the complex. The Fe/S cluster is bound to two highly conserved Cys residues in the C-termini of each of these proteins. NUBP1 contains an additional, stably associated [4Fe-4S] cluster at its N-terminus which is essential for function.
Mitochondria play a crucial role in cytosolic and nuclear Fe/S protein biogenesis. They export via a mitochondrial ABC transporter (yeast ATM1, human ABCB7) a still unknown, sulfur-containing compound which is essential for Fe/S cluster assembly in the cytosol.
The general cytosolic iron donor, the multi-domain monothiol glutaredoxin (human GRX3 or PICOT, yeast Grx3-Grx4) plays a crucial role in cytosolic-nuclear Fe/S protein biogenesis. The precise molecular function of the glutaredoxin is still unclear.

Literature References
PubMed ID Title Journal Year
18573874 Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis

Stehling, O, Netz, DJ, Niggemeyer, B, Rösser, R, Eisenstein, RS, Puccio, H, Pierik, AJ, Lill, R

Mol. Cell. Biol. 2008
Catalyst Activity

electron transfer activity of NDOR1:CIAPIN1 reduced [cytosol]

This event is regulated
Inferred From
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