Evidence for a tetranuclear iron-sulfur center in glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis.
Glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis is an unusual enzyme because it contains an essential iron-sulfur center but does not catalyze an obvious oxidation-reduction reaction. In this communication, results of revised sulfide analyses, iron-sulfur cluster displacement studies, and Mössbauer spectroscopy are presented that lead to the conclusion that the native enzyme contains a tetranuclear [4Fe-4S] center in a diamagnetic state.
D000582:Amidophosphoribosyltransferase / Q000032:analysis*; D001412:Bacillus subtilis / Q000201:enzymology*; D003013:Clostridium / Q000201:enzymology; D005288:Ferredoxins / Q000032:analysis; D007501:Iron / Q000032:analysis*; D008968:Molecular Conformation; D010430:Pentosyltransferases / Q000032:analysis*; D013057:Spectrum Analysis / Q000379:methods; D013440:Sulfides / Q000032:analysis*
D005288:Ferredoxins; D013440:Sulfides; D007501:Iron; D010430:Pentosyltransferases; D000582:Amidophosphoribosyltransferase