Iron–sulfur clusters are multifaceted iron-containing cofactors coordinated and utilized by numerous proteins in nearly all biological systems. Fe–S-cluster-containing proteins help direct pathways essential for cell viability and participate in biological applications ranging from nucleotide biosynthesis and stability, protein translation, enzyme catalysis, and mitochondrial metabolism. Fe–S-containing proteins function by utilizing the unique electronic and chemical properties inherent in the Fe containing cofactor. Fe–S clusters are constructed of inorganic iron and sulfide arranged in a distinct caged structural makeup ranging from [Fe2–S2], [Fe3–S4], [Fe4–S4], up to [Fe8–S8] clusters. In eukaryotes, cluster activity is controlled in part at the assembly level and the major pathway for cluster production exists within the mitochondria. Recent insight into the pathway of mitochondrial cluster assembly has come from new in vivo and in vitro reports that provided direct insight into how all protein partners within the assembly pathway interact. However, we are only just beginning to understand the role of each protein within this complex pageant that is mitochondrial Fe–S cluster assembly. In this report we present results, using the yeast model for mitochondrial assembly, to describe the molecular details of how important proteins in the pathway coordinate for cluster assembly.