Function and biogenesis of iron-sulphur proteins.
Iron-sulphur (Fe-S) clusters have long been recognized as essential and versatile cofactors of proteins involved in catalysis, electron transport and sensing of ambient conditions. Despite the relative simplicity of Fe-S clusters in terms of structure and composition, their synthesis and assembly into apoproteins is a highly complex and coordinated process in living cells. Different biogenesis machineries in both bacteria and eukaryotes have been discovered that assist Fe-S-protein maturation according to uniform biosynthetic principles. The importance of Fe-S proteins for life is documented by an increasing number of diseases linked to these components and their biogenesis.
Lill
Roland
R
Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, D-35033 Marburg, Germany. lill@staff.uni-marburg.de
D001419:Bacteria / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D005057:Eukaryotic Cells / Q000166:cytology / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000096:biosynthesis*; D008928:Mitochondria / Q000378:metabolism; D018087:Plastids / Q000378:metabolism
D007506:Iron-Sulfur Proteins
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