Iron-sulfur proteins: ancient structures, still full of surprises

  title={Iron-sulfur proteins: ancient structures, still full of surprises},
  author={Helmut Beinert},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  • H. Beinert
  • Published 1 February 2000
  • Chemistry, Medicine
  • JBIC Journal of Biological Inorganic Chemistry
This article is a survey of the properties and functions of Fe-S proteins under the following headings: sulfur and iron; iron-sulfur clusters; evolution of cofactor use; early observations; complex and extended clusters; sulfur exchange and core interconversions; synthesis and biosynthesis of Fe-S clusters; functions of Fe-S clusters: electron transfer, electron delocalization, spin states and magnetism, covalency of sulfur bonds; non-electron transfer functions of Fe-S clusters: substrate… 
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The current state of structural, spectroscopic, and computational knowledge for the iron-sulfur clusters in the nitrogenase iron and iron-molybdenum proteins is examined by comparison and contrast to 'simpler' ironclusters.
Structure, function, and formation of biological iron-sulfur clusters.
Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundamental life processes and important mechanistic questions related to the biosynthetic process involve the molecular details of how these clusters are assembled on scaffold proteins, how they are transferred from scaffolds to target proteins, and how the biosynthesis process is regulated.
Biogenesis of iron-sulfur proteins in plants.
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Iron–Sulfur Cluster Biogenesis in Archaea and Bacteria
The current status of Fe–S cluster biogenesis research in Bacteria and Archaea is reviewed and it is clear that a variety of accessory proteins and metabolites cooperate with these systems for cluster assembly.
Structural characterization of an iron–sulfur cluster assembly protein IscU in a zinc‐bound form
Sequence comparisons suggest IscU is a highly conserved protein and is homologous to the N-terminal domain of NifU (nNifU), an essential protein for nitrogen fixation and Isc U/nN ifU contains three strictly conserved cysteine residues.
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Iron–sulfur (Fe–S) clusters are protein cofactors of a multitude of enzymes performing essential biological functions. Specialized multi-protein machineries present in all types of organisms support
Iron–Sulfur Proteins
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New York Times, 7 July, front page
  • 1998
King RB (ed) Encyclopedia of inorganic chemistry
  • 1915