Iron–Sulfur Proteins: Structure, Function and Biogenesis

Abstract Iron–sulfur clusters rank among the most versatile protein cofactors. Proteins using Fe–S clusters intervene in many cellular processes in both bacteria and eukaryotes. Fe–S cluster biogenesis has been a research area of intensive investigations in the past decade. The success of Fe–S cluster‐based biology during evolution is indicated by the myriad of processes that depend on Fe–S cluster‐containing proteins. These include basic metabolic, bioenergetics and genetic information‐related processes. Conserved multiprotein systems, called ISC and SUF , have been identified in most living organisms, from bacteria to plant and mammals. They catalyse assembly of clusters and their delivery to the many apoproteins, the activity of which depends on the acquisition of clusters. Recently, their role in bacterial pathogenicity and bacterial resistance to antibiotics was brought to light. Key Concepts Fe–S clusters are versatile and ubiquitous cofactors. Fe–S cluster biogenesis is catalysed by multiprotein systems. ISC and SUF Fe–S biogenesis systems are conserved in bacterias and eukaryotes. The IscR regulator controls Fe–S cluster homeostasis. The IscR regulator allows bacteria to adapt to various environmental conditions and hosts. Iron external levels modify aminoglycoside resistance of E. coli via its influence on Fe–S biogenesis.