Function and biogenesis of iron–sulphur proteins

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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.

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Figure 1: A model for Fe–S-protein biogenesis in bacteria: the ISC and SUF machineries.
Figure 2: A model for Fe–S-protein assembly in mitochondria.
Figure 3: The roles of mitochondria and the CIA machinery in Fe–S-protein biogenesis in the cytosol and nucleus of eukaryotes.


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I wish to thank all present and past members of my group for their excellent and dedicated work. Generous financial support from the Deutsche Forschungsgemeinschaft (SFB 593 and TR1, Gottfried-Wilhelm Leibniz programme and GRK 1216), the Max-Planck Gesellschaft, the von Behring-Röntgen-Stiftung, the German-Israeli Foundation for Scientific Research and Development, the Alexander von Humboldt-Stiftung, Rhön Klinikum AG and Fonds der Chemischen Industrie is gratefully acknowledged. I apologize to all colleagues whose original work could not be discussed or cited owing to length limitations.

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Lill, R. Function and biogenesis of iron–sulphur proteins. Nature 460, 831–838 (2009) doi:10.1038/nature08301

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