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Science 1 August 1997:
Vol. 277. no. 5326, pp. 653 - 659
DOI: 10.1126/science.277.5326.653
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Articles

Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures

Helmut Beinert, Richard H. Holm, Eckard Münck

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.

H. Beinert is in the Institute for Enzyme Research and the Department of Biochemistry, University of Wisconsin, Madison, WI 53705, USA. R. H. Holm is in the Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. E. Münck is in the Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

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