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Curr Opin Chem Biol. 1998 Apr;2(2):173-81.

Iron-sulfur proteins: new roles for old clusters.

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Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.


Several major advances in our understanding of the structure, function and properties of biological iron-sulfur clusters have occurred in the past year. These include a new structural type of cluster in the inappropriately named prismane protein, the establishment of redox-mediated [Fe2S2]2+ <--> [Fe4S4]2+ cluster conversions, and the characterization of valence-delocalized [Fe2S2]+ and all ferrous clusters with [Fe2S2]0, [Fe3S4]2- and [Fe4S4]0 cores. The emergence of novel types of redox, regulatory and enzymatic roles have also raised the possibility of iron-sulfur clusters mediating two electron redox processes, coupling proton and electron transfer, and catalyzing disulfide reduction and reductive cleavage of S-adenosylmethionine via sulfur-based cluster chemistry.

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