PMID:15952888
| Citation |
Johnson, DC, Dean, DR, Smith, AD and Johnson, MK (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74:247-81 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1146/annurev.biochem.74.082803.133518 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genes, Bacterial; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Molecular Sequence Data; Nitrogenase/chemistry; Nitrogenase/genetics; Nitrogenase/metabolism; Protein Processing, Post-Translational; Sequence Homology, Amino Acid |
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