19th Sir Hans Krebs lecture. Engineering of protein bound iron-sulfur clusters. A tool for the study of protein and cluster chemistry and mechanism of iron-sulfur enzymes.
An increasing number of iron-sulfur (Fe-S) proteins are found in which the Fe-S cluster is not involved in net electron transfer, as it is in the majority of Fe-S proteins. Most of the former are (de)hydratases, of which the most extensively studied is aconitase. Approaches are described and discussed by which the Fe-S cluster of this enzyme could be brought into states of different structure, ligation, oxidation and isotope composition. The species, so obtained, provided the basis for spectroscopic and chemical investigations. Results from studies by protein chemistry, EPR, Mössbauer, 1H, 2H and 57Fe electron-nuclear double resonance spectroscopy are described. Conclusions, which bear on the electronic structure of the Fe-S cluster, enzyme-substrate interaction and the enzymatic mechanism, were derived from a synopsis of the recent work described here and of previous contributions from several laboratories. These conclusions are discussed and summarized in a final section.
Beinert
H
H
Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226.
Kennedy
M C
MC
D000154:Aconitate Hydratase / Q000138:chemical synthesis / Q000378:metabolism; D001051:Apoenzymes / Q000032:analysis / Q000138:chemical synthesis / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D007506:Iron-Sulfur Proteins / Q000032:analysis* / Q000138:chemical synthesis / Q000378:metabolism; D007553:Isotope Labeling; D008667:Metalloproteins / Q000032:analysis*; D013057:Spectrum Analysis / Q000379:methods; D013379:Substrate Specificity
D001051:Apoenzymes; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D000154:Aconitate Hydratase