The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster.
作者： D M Kurtz , R H Holm , F J Ruzicka , H Beinert , C J Coles
DOI: 10.1016/S0021-9258(18)50547-0
关键词: Ligand 、 Iron–sulfur cluster 、 Cluster (physics) 、 Hexamethylphosphoramide 、 Chemistry 、 Inorganic chemistry 、 Crystallography 、 Electron paramagnetic resonance 、 Aconitase 、 Yield (chemistry) 、 Absorption spectroscopy 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: 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 magnetic state corresponding to this thus far only found tetranuclear clusters model compounds proteins, it could be expected also contains a [4Fe-4S] cluster. We show here core extrusion, presence hexamethylphosphoramide o-xylyl-alpha,alpha'-dithiol subsequent ligand exchange with p-trifluoromethylbenzenethiol yield absorption spectra binuclear clusters. According absorbance measured, concentration extruded [2Fe-2S] cluster quantitatively accounts for content preparations examined. Preliminary studies 19F nuclear spectrum obtained on extrusion confirm aconitase.
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