Journal
ANNUAL REVIEW OF BIOCHEMISTRY
Volume 74, Issue -, Pages 247-281Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.74.082803.133518
Keywords
iron-sulfur clusters; scaffolds; cysteine desulfurase; chaperones
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062524] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM62524] Funding Source: Medline
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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.
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