Iron–sulfur protein

Iron–sulfur proteins (or iron–sulphur proteins in British spelling) are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, coenzyme Q – cytochrome c reductase, succinate – coenzyme Q reductase and nitrogenase. Iron–sulfur clusters are best known for their role in the oxidation-reduction reactions of electron transport in mitochondria and chloroplasts. Both Complex I and Complex II of oxidative phosphorylation have multiple Fe–S clusters. They have many other functions including catalysis as illustrated by aconitase, generation of radicals as illustrated by SA.

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  Iron–sulfur protein
• Rieske 2Fe-2S Cluster Oxidation States of Fe3+ and Fe2+
  Rieske 2Fe-2S Cluster Oxidation States of Fe3+ and Fe2+
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  Iron–sulfur protein
• 4Fe-4S Oxidation States of Fe3+
  4Fe-4S Oxidation States of Fe3+
• FeMoco Structure
  FeMoco Structure
• Ranges of reduction potentials
  Ranges of reduction potentials