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X-ray absorption spectroscopy and reactivity of thiolate-ligated Fe(III)-OOR complexes.

ABSTRACT: The reaction of a series of thiolate-ligated iron(II) complexes [Fe(II)([15]aneN(4))(SC(6)H(5))]BF(4) (1), [Fe(II)([15]aneN(4))(SC(6)H(4)-p-Cl)]BF(4) (2), and [Fe(II)([15]aneN(4))(SC(6)H(4)-p-NO(2))]BF(4) (3) with alkylhydroperoxides at low temperature (-78 °C or -40 °C) leads to the metastable alkylperoxo-iron(III) species [Fe(III)([15]aneN(4))(SC(6)H(5))(OOtBu)]BF(4) (1a), [Fe(III)([15]aneN(4))(SC(6)H(4)-p-Cl)(OOtBu)]BF(4) (2a), and [Fe(III)([15]aneN(4))(SC(6)H(4)-p-NO(2))(OOtBu)]BF(4) (3a), respectively. X-ray absorption spectroscopy (XAS) studies were conducted on the Fe(III)-OOR complexes and their iron(II) precursors. The edge energy for the iron(II) complexes (?7118 eV) shifts to higher energy upon oxidation by ROOH, and the resulting edge energies for the Fe(III)-OOR species range from 7121-7125 eV and correlate with the nature of the thiolate donor. Extended X-ray absorption fine structure (EXAFS) analysis of the iron(II) complexes 1-3 in CH(2)Cl(2) show that their solid state structures remain intact in solution. The EXAFS data on 1a-3a confirm their proposed structures as mononuclear, 6-coordinate Fe(III)-OOR complexes with 4N and 1S donors completing the coordination sphere. The Fe-O bond distances obtained from EXAFS for 1a-3a are 1.82-1.85 Å, significantly longer than other low-spin Fe(III)-OOR complexes. The Fe-O distances correlate with the nature of the thiolate donor, in agreement with the previous trends observed for ?(Fe-O) from resonance Raman (RR) spectroscopy, and supported by optimized geometries obtained from density functional theory (DFT) calculations. Reactivity and kinetic studies on 1a- 3a show an important influence of the thiolate donor.

SUBMITTER: Stasser J

PROVIDER: S-EPMC3221327 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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X-ray absorption spectroscopy and reactivity of thiolate-ligated Fe(III)-OOR complexes.

Stasser Jay J Namuswe Frances F Kasper Gary D GD Jiang Yunbo Y Krest Courtney M CM Green Michael T MT Penner-Hahn James J Goldberg David P DP

Inorganic chemistry 20101001 20

The reaction of a series of thiolate-ligated iron(II) complexes [Fe(II)([15]aneN(4))(SC(6)H(5))]BF(4) (1), [Fe(II)([15]aneN(4))(SC(6)H(4)-p-Cl)]BF(4) (2), and [Fe(II)([15]aneN(4))(SC(6)H(4)-p-NO(2))]BF(4) (3) with alkylhydroperoxides at low temperature (-78 °C or -40 °C) leads to the metastable alkylperoxo-iron(III) species [Fe(III)([15]aneN(4))(SC(6)H(5))(OOtBu)]BF(4) (1a), [Fe(III)([15]aneN(4))(SC(6)H(4)-p-Cl)(OOtBu)]BF(4) (2a), and [Fe(III)([15]aneN(4))(SC(6)H(4)-p-NO(2))(OOtBu)]BF(4) (3a), r ...[more]

PMID: 20839847

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Project description:Kinetic studies aimed at determining the most probable mechanism for the proton-dependent [Fe(II)(S(Me2)N(4)(tren))](+) (1) promoted reduction of superoxide via a thiolate-ligated hydroperoxo intermediate [Fe(III)(S(Me2)N(4)(tren))(OOH)](+) (2) are described. Rate laws are derived for three proposed mechanisms, and it is shown that they should conceivably be distinguishable by kinetics. For weak proton donors with pK(a(HA)) > pK(a(HO(2))) rates are shown to correlate with proton donor pK(a), and display first-order dependence on iron, and half-order dependence on superoxide and proton donor HA. Proton donors acidic enough to convert O(2)(-) to HO(2) (in tetrahydrofuran, THF), that is, those with pK(a(HA)) < pK(a(HO(2))), are shown to display first-order dependence on both superoxide and iron, and rates which are independent of proton donor concentration. Relative pK(a) values were determined in THF by measuring equilibrium ion pair acidity constants using established methods. Rates of hydroperoxo 2 formation displays no apparent deuterium isotope effect, and bases, such as methoxide, are shown to inhibit the formation of 2. Rate constants for p-substituted phenols are shown to correlate linearly with the Hammett substituent constants ?(-). Activation parameters ((?H(++) = 2.8 kcal/mol, ?S(++) = -31 eu) are shown to be consistent with a low-barrier associative mechanism that does not involve extensive bond cleavage. Together, these data are shown to be most consistent with a mechanism involving the addition of HO(2) to 1 with concomitant oxidation of the metal ion, and reduction of superoxide (an "oxidative addition" of sorts), in the rate-determining step. Activation parameters for MeOH- (?H(++) = 13.2 kcal/mol and ?S(++) = -24.3 eu), and acetic acid- (?H(++) = 8.3 kcal/mol and ?S(++) = -34 eu) promoted release of H(2)O(2) to afford solvent-bound [Fe(III)(S(Me2)N(4)(tren))(OMe)](+) (3) and [Fe(III)(S(Me2)N(4)(tren))(O(H)Me)](+) (4), respectively, are shown to be more consistent with a reaction involving rate-limiting protonation of an Fe(III)-OOH, than with one involving rate-limiting O-O bond cleavage. The observed deuterium isotope effect (k(H)/k(D) = 3.1) is also consistent with this mechanism.

Project description:Superoxide reductase (SOR) is a non-heme iron enzyme that reduces superoxide to peroxide at a diffusion-controlled rate. Sulfur K-edge X-ray absorption spectroscopy (XAS) is used to investigate the ground-state electronic structure of the resting high-spin and CN- bound low-spin FeIII forms of the 1Fe SOR from Pyrococcus furiosus. A computational model with constrained imidazole rings (necessary for reproducing spin states), H-bonding interaction to the thiolate (necessary for reproducing Fe-S bond covalency of the high-spin and low-spin forms), and H-bonding to the exchangeable axial ligand (necessary to reproduce the ground state of the low-spin form) was developed and then used to investigate the enzymatic reaction mechanism. Reaction of the resting ferrous site with superoxide and protonation leading to a high-spin FeIII-OOH species and its subsequent protonation resulting in H2O2 release is calculated to be the most energetically favorable reaction pathway. Our results suggest that the thiolate acts as a covalent anionic ligand. Replacing the thiolate with a neutral noncovalent ligand makes protonation very endothermic and greatly raises the reduction potential. The covalent nature of the thiolate weakens the FeIII bond to the proximal oxygen of this hydroperoxo species, which raises its pKa by an additional 5 log units relative to the pKa of a primarily anionic ligand, facilitating its protonation. A comparison with cytochrome P450 indicates that the stronger equatorial ligand field from the porphyrin results in a low-spin FeIII-OOH species that would not be capable of efficient H2O2 release due to a spin-crossing barrier associated with formation of a high-spin 5C FeIII product. Additionally, the presence of the dianionic porphyrin pi ring in cytochrome P450 allows O-O heterolysis, forming an FeIV-oxo porphyrin radical species, which is calculated to be extremely unfavorable for the non-heme SOR ligand environment. Finally, the 5C FeIII site that results from the product release at the end of the O2- reduction cycle is calculated to be capable of reacting with a second O2-, resulting in superoxide dismutase (SOD) activity. However, in contrast to FeSOD, the 5C FeIII site of SOR, which is more positively charged, is calculated to have a high affinity for binding a sixth anionic ligand, which would inhibit its SOD activity.

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X-ray absorption spectroscopy and reactivity of thiolate-ligated Fe(III)-OOR complexes.

Publications

X-ray absorption spectroscopy and reactivity of thiolate-ligated Fe(III)-OOR complexes.

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