CHARACTERIZATION OF ACTIVE-CENTER OF A NONHEME CHLOROPEROXIDASE BY X-RAY-ABSORPTION FINE-STRUCTURE

XAFS studies on this non-heme chloroperoxidase reveal that its Fe core is in a saturated six-coordinate, octahedral environment with four pl aner N atoms and two axial S atoms. The active site is very similar to Fe porphyrine center in P450 oxidase, but the coordinated N atoms com e from amino acids of polypeptides or other molecules, but not porphyr in.