Abstract
The electronic structure and magnetic interaction of the active site of pig purple acid phosphatase (PAP, uteroferrin) were investigated using pure DFT (UBLYP) and hybrid DFT methods (UB3LYP and UB2LYP). Uteroferrin catalyzes the hydrolysis of a phosphate ester under acidic conditions and contains a binuclear iron center. The mammalian PAPs are expected to be targets for drug design of osteoporosis. Their active sites are typical examples of the Fe(II)-Fe(III) mixed-valence system. We studied double exchange interaction of the mixed-valence system, using the potential energy difference between the Fe(II)-Fe(III) and the Fe(III)-Fe(II) states. The pathway of the antiferromagnetic coupling between Fe(III) and Fe(II) were also discussed by using chemical indices, which are evaluated by the occupation numbers of singly occupied natural orbitals. © 2009 Wiley Periodicals, Inc. Int J Quantum Chem, 2010
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