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Querci, Leonardo; Piccioli, Mario; Ciofi-Baffoni, Simone; Banci, Lucia
Biochimica et biophysica acta. Molecular cell research, 10/2024, Letnik: 1871, Številka: 7Journal Article
Over the last decade, structural aspects involving iron‑sulfur (Fe/S) protein biogenesis have played an increasingly important role in understanding the high mechanistic complexity of mitochondrial and cytosolic machineries maturing Fe/S proteins. In this respect, solution NMR has had a significant impact because of its ability to monitor transient protein-protein interactions, which are abundant in the networks of pathways leading to Fe/S cluster biosynthesis and transfer, as well as thanks to the developments of paramagnetic NMR in both terms of new methodologies and accurate data interpretation. Here, we review the use of solution NMR in characterizing the structural aspects of human Fe/S proteins and their interactions in the framework of Fe/S protein biogenesis. We will first present a summary of the recent advances that have been achieved by paramagnetic NMR and then we will focus our attention on the role of solution NMR in the field of human Fe/S protein biogenesis. •Impact of solution NMR in mitochondrial and cytosolic Fe/S protein biogenesis•Dedicated paramagnetic NMR methodologies to characterize challenging Fe/S proteins•NMR unravels the mechanisms of 2Fe-2S and 4Fe-4S cluster assembly.•NMR elucidates electron transfer pathways required to assemble Fe/S clusters.•NMR describes mechanisms of Fe/S cluster trafficking and insertion in apo proteins.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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