AI Article Synopsis
- Iron-sulfur proteins, containing clusters like Fe2S2 and Fe4S4, are vital components across all life forms and participate in various biochemical reactions.
- These clusters facilitate electron transfer, serve as catalytic centers, and help in sensing iron and oxygen levels within cells.
- Their magnetic properties, primarily in paramagnetic oxidation states, present complexities that make studying these mixed-valence systems challenging.
Article Abstract
Iron-sulfur proteins are found in all life forms. Most frequently, they contain Fe2S2, Fe3S4, and Fe4S4 clusters. These modular clusters undergo oxidation-reduction reactions, may be inserted or removed from proteins, can influence protein structure by preferential side chain ligation, and can be interconverted. In addition to their electron transfer function, iron-sulfur clusters act as catalytic centers and sensors of iron and oxygen. Their most common oxidation states are paramagnetic and present significant challenges for understanding the magnetic properties of mixed valence systems. Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.
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| http://dx.doi.org/10.1126/science.277.5326.653 | DOI Listing |
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