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    Influence of Thiolate Ligands on Reductive N−O Bond Activation. Probing the O<sub>2</sub><sup>−</sup> Binding Site of a Biomimetic Superoxide Reductase Analogue and Examining the P... by Gloria Villar-Acevedo (2232583)

    Published 2011
    “…Like NO-bound <i>trans</i>-cysteinate-ligated SOR (SOR-NO), the rhombic <i>S</i> = 3/2 EPR signal of NO-bound <i>cis</i>-thiolate-ligated [Fe(S<sup>Me<sub>2</sub></sup>N<sub>4</sub>(tren)(NO)]<sup>+</sup> (<b>2</b>; <i>g</i> = 4.44, 3.54, 1.97), the isotopically sensitive ν<sub>NO</sub>(ν<sub><sup>15</sup>NO</sub>) stretching frequency (1685(1640) cm<sup>−1</sup>), and the 0.05 Å decrease in Fe−S bond length are shown to be consistent with <i>the oxidative addition of NO to Fe(II)</i> to afford an Fe(III)−NO<sup>−</sup> {FeNO}<sup>7</sup> species containing high-spin (<i>S</i> = 5/2) Fe(III) antiferromagnetically coupled to NO<sup>−</sup> (<i>S</i> = 1). …”
  20. 720

    Influence of Thiolate Ligands on Reductive N−O Bond Activation. Probing the O<sub>2</sub><sup>−</sup> Binding Site of a Biomimetic Superoxide Reductase Analogue and Examining the P... by Gloria Villar-Acevedo (2232583)

    Published 2011
    “…Like NO-bound <i>trans</i>-cysteinate-ligated SOR (SOR-NO), the rhombic <i>S</i> = 3/2 EPR signal of NO-bound <i>cis</i>-thiolate-ligated [Fe(S<sup>Me<sub>2</sub></sup>N<sub>4</sub>(tren)(NO)]<sup>+</sup> (<b>2</b>; <i>g</i> = 4.44, 3.54, 1.97), the isotopically sensitive ν<sub>NO</sub>(ν<sub><sup>15</sup>NO</sub>) stretching frequency (1685(1640) cm<sup>−1</sup>), and the 0.05 Å decrease in Fe−S bond length are shown to be consistent with <i>the oxidative addition of NO to Fe(II)</i> to afford an Fe(III)−NO<sup>−</sup> {FeNO}<sup>7</sup> species containing high-spin (<i>S</i> = 5/2) Fe(III) antiferromagnetically coupled to NO<sup>−</sup> (<i>S</i> = 1). …”