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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase.

Active beef heart aconitase contains an iron-sulfur cluster with an [Fe4S4]2+ core. This cluster can be converted into Fe3S4 with concomitant loss of enzymatic activity. We have reconstituted apo-aconitase with iron and selenide to obtain Fe4Se4 aconitase. The Se analog has higher catalytic activity than the native S-containing enzyme when isocitrate is the substrate. Oxidation of [Fe4Se4]2+ with ferricyanide yields the inactive [Fe3Se4]1+ form. The Se-containing 3-Fe cluster can be reduced to [Fe3Se4]0. We have studied the [Fe3S4]1+,0, [Fe3Se4]1+,0, and [Fe4Se4]2+ states with Mössbauer spectroscopy from 1.3 K to 200 K in magnetic fields up to 6.0 T. The spectra of the S- and Se-containing enzymes were found to be remarkably similar. The spectra of the 3-Fe clusters were analyzed and the salient features of the electronic structure are discussed.[1]

References

  1. Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase. Surerus, K.K., Kennedy, M.C., Beinert, H., Münck, E. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
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