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Iron-sulfur Fe-S clusters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundamental life processes. Owing to their remarkable structural plasticity and versatile chemical/electronic features Fe-S clusters participate in electron transfer, substrate binding/activation, iron/sulfur storage, regulation of gene expression, and enzyme activity. Formation of intracellular Fe-S clusters does not occur spontaneously but requires a complex biosynthetic machinery. Three different types of Fe-S cluster biosynthetic systems have been discovered, and all of them are mechanistically unified by the requirement for a cysteine desulfurase and the participation of an Fe-S cluster scaffolding protein. Important mechanistic questions related to Fe-S cluster biosynthesis involve the molecular details of how Fe-S clusters are assembled on scaffold proteins, how Fe-S clusters are transferred from scaffolds to target proteins, how various accessory proteins participate in Fe-S protein maturation, and how the biosynthetic process is regulated.
Johnson et al. (Sat,) studied this question.
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