The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster

It has been reported (Ruzicka, F.J., and Beinert, H. (1978) J. Biol. Chem. 253, 2514-2517) that aconitase in the oxidized state, as isolated, shows an electron paramagnetic resonance signal centered at g = 2.01, typical of high potential iron-sulfur proteins. Since the magnetic state corresponding t...

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Bibliographic Details
Published in:The Journal of biological chemistry 1979-06, Vol.254 (12), p.4967-4969
Main Authors: Kurtz, D M, Holm, R H, Ruzicka, F J, Beinert, H, Coles, C J, Singer, T P
Format: Article
Language:English
Subjects:
Aconitate Hydratase
Animals
Cattle
Iron - analysis
Iron-Sulfur Proteins
Magnetic Resonance Spectroscopy
Metalloproteins
Molecular Weight
Myocardium - enzymology
Oxidation-Reduction
Protein Binding
Protein Conformation
Spectrophotometry
Sulfur - analysis
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Summary:It has been reported (Ruzicka, F.J., and Beinert, H. (1978) J. Biol. Chem. 253, 2514-2517) that aconitase in the oxidized state, as isolated, shows an electron paramagnetic resonance signal centered at g = 2.01, typical of high potential iron-sulfur proteins. Since the magnetic state corresponding to this signal has thus far only been found in tetranuclear iron-sulfur clusters in model compounds and proteins, it could be expected that aconitase also contains a [4Fe-4S] cluster. We show here that core extrusion, in the presence of hexamethylphosphoramide and o-xylyl-alpha,alpha'-dithiol and subsequent ligand exchange with p-trifluoromethylbenzenethiol yield absorption spectra typical of binuclear iron-sulfur clusters. According to the absorbance measured, the concentration of the extruded [2Fe-2S] cluster quantitatively accounts for the iron-sulfur content of the preparations examined. Preliminary studies of the 19F nuclear magnetic resonance spectrum obtained on extrusion with p-trifluoromethylbenzenethiol confirm the presence of a binuclear cluster in aconitase.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)50547-0