Iron-sulfur proteins: new roles for old clusters.
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.
Johnson
M K
MK
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA. johnson@sunchem.chem.uga.edu
D001426:Bacterial Proteins / Q000737:chemistry; D002384:Catalysis; D007501:Iron / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D009591:Nitrogenase / Q000737:chemistry; D010084:Oxidation-Reduction; D013455:Sulfur / Q000737:chemistry
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; C075199:prismane protein, Desulfovibrio vulgaris; D013455:Sulfur; D007501:Iron; D009591:Nitrogenase