| Autor: |
Smith SJ; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane 4072, Australia., Peralta RA, Jovito R, Horn A Jr, Bortoluzzi AJ, Noble CJ, Hanson GR, Stranger R, Jayaratne V, Cavigliasso G, Gahan LR, Schenk G, Nascimento OR, Cavalett A, Bortolotto T, Razzera G, Terenzi H, Neves A, Riley MJ |
| Jazyk: |
angličtina |
| Zdroj: |
Inorganic chemistry [Inorg Chem] 2012 Feb 20; Vol. 51 (4), pp. 2065-78. Date of Electronic Publication: 2012 Jan 30. |
| DOI: |
10.1021/ic201711p |
| Abstrakt: |
A mixed-valence complex, [Fe(III)Fe(II)L1(μ-OAc)(2)]BF(4)·H(2)O, where the ligand H(2)L1 = 2-{[[3-[((bis(pyridin-2-ylmethyl)amino)methyl)-2-hydroxy-5-methylbenzyl](pyridin-2-ylmethyl)amino]methyl]phenol}, has been studied with a range of techniques, and, where possible, its properties have been compared to those of the corresponding enzyme system purple acid phosphatase. The Fe(III)Fe(II) and Fe(III)(2) oxidized species were studied spectroelectrochemically. The temperature-dependent population of the S = 3/2 spin states of the heterovalent system, observed using magnetic circular dichroism, confirmed that the dinuclear center is weakly antiferromagnetically coupled (H = -2JS(1)·S(2), where J = -5.6 cm(-1)) in a frozen solution. The ligand-to-metal charge-transfer transitions are correlated with density functional theory calculations. The Fe(III)Fe(II) complex is electron paramagnetic resonance (EPR)-silent, except at very low temperatures (<2 K), because of the broadening caused by the exchange coupling and zero-field-splitting parameters being of comparable magnitude and rapid spin-lattice relaxation. However, a phosphate-bound Fe(III)(2) complex showed an EPR spectrum due to population of the S(tot) = 3 state (J= -3.5 cm(-1)). The phosphatase activity of the Fe(III)Fe(II) complex in hydrolysis of bis(2,4-dinitrophenyl)phosphate (k(cat.) = 1.88 × 10(-3) s(-1); K(m) = 4.63 × 10(-3) mol L(-1)) is similar to that of other bimetallic heterovalent complexes with the same ligand. Analysis of the kinetic data supports a mechanism where the initiating nucleophile in the phosphatase reaction is a hydroxide, terminally bound to Fe(III). It is interesting to note that aqueous solutions of [Fe(III)Fe(II)L1(μ-OAc)(2)](+) are also capable of protein cleavage, at mild temperature and pH conditions, thus further expanding the scope of this complex's catalytic promiscuity. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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