EXAFS studies on the active site of purple acid phosphatase from sweet potato Ipomoea batatas.
XAS investigations on the active site of the purple acid phosphatase isolated from the sweet potato Ipomoea batatas provided first information about the structure. Data analysis reveal a dinuclear active site containing an iron and a zinc atom. The first coordination sphere of each metal in the active site consists of six nitrogen/oxygen donor atoms, resulting in a distorted octahedral coordination sphere very similar to the active site of the enzyme isolated from the red kidney bean Phaseolus vulgaris. The XAS spectra were recorded in fluorescence mode at 18 K using a Canberra 13-element germanium solid state detector.