02052nas a2200253   4500008004100000022001400041245009800055210006900153260011000222300001400332490000700346520109800353653003101451653002701482653001701509653000901526653002201535653002201557100002501579700002301604700002101627700002201648856012801670       2010                        eng d  a0376-471000aStructure-function mimicry of oxidized purple acid phosphatase-PAP(ox)-A new functional model0 aStructurefunction mimicry of oxidized purple acid phosphatasePAP  aDR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIAbNATL INST SCIENCE COMMUNICATION-NISCAIRcAUG  a1023-10290 v493 a<p>{Electronic structure and spectroscopic properties of the novel diiron active site of oxidized mammalian purple acid phosphatase analogues, Fe-6: [Fe-2 (mu-O) (mu-OAc) (4HNSQ(ox))(2 center dot-)(ONSQ(ox))(2 center dot-)(H2O)(4)] and Fe-7: [Fe-2 (mu-O) (mu-OAc)(ONSQ(ox))(2 center dot-)(OAc) (H2O)(4)] are described. Magnetic susceptibility SQUID data of Fe-6 are best fitted to Heisenberg's isotropic spin pair (S = 5/2, 3/2) model using magnetic parameters g = 2 and J = - 36.8 cm(-1) with R factor = 6.4 x 10(-4). The antiferromagnetic exchange establishes Fe(III)-O-Fe(III) dimeric core with Fe(III) site having two radical ligations in the naphthosemiquinone oxime form of lawsone oxime. In the model compound Fe-7 of oxidized purple acid phosphatase, bridged and terminal acetate functions are identified according to their different energies of activations, i.e, similar to 34 and 58 kJ mol(-1) respectively. Also, the reduced naphthoquinone oxime form of ligand is characterized by its energy of activation (similar to 15 kJ mol(-1)) from pyrolytic reaction. Mossbauer parameters</p>10aAntiferromagnetic exchange10aBioinorganic chemistry10aDNA cleavage10airon10aNuclease activity10aPAP(ox) analogues1 aWaghmode, Shobha, A.1 aDate, Sadgopal, K.1 aGupta, Vidya, S.1 aRane, Sandhya, Y.  uhttps://library.ncl.res.in/content/structure-function-mimicry-oxidized-purple-acid-phosphatase-papox-new-functional-model-0