Unknown

Dataset Information

0

Hemilabile Proton Relays and Redox Activity Lead to {FeNO} x and Significant Rate Enhancements in NO2- Reduction.

ABSTRACT: Incorporation of the triad of redox activity, hemilability, and proton responsivity into a single ligand scaffold is reported. Due to this triad, the complexes Fe(PyrrPDI)(CO)2 (3) and Fe(MorPDI)(CO)2 (4) display 40-fold enhancements in the initial rate of NO2- reduction, with respect to Fe(MeOPDI)(CO)2 (7). Utilizing the proper sterics and p Ka of the pendant base(s) to introduce hemilability into our ligand scaffolds, we report unusual {FeNO} x mononitrosyl iron complexes (MNICs) as intermediates in the NO2- reduction reaction. The {FeNO} x species behave spectroscopically and computationally similar to {FeNO}7, an unusual intermediate-spin Fe(III) coupled to triplet NO- and a singly reduced PDI ligand. These {FeNO} x MNICs facilitate enhancements in the initial rate.

SUBMITTER: Cheung PM 

PROVIDER: S-EPMC6668709 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Hemilabile Proton Relays and Redox Activity Lead to {FeNO} <sup>x</sup> and Significant Rate Enhancements in NO<sub>2</sub><sup>-</sup> Reduction.

Cheung Pui Man PM   Burns Kyle T KT   Kwon Yubin M YM   Deshaye Megan Y MY   Aguayo Kristopher J KJ   Oswald Victoria F VF   Seda Takele T   Zakharov Lev N LN   Kowalczyk Tim T   Gilbertson John D JD  

Journal of the American Chemical Society 20181130 49

Incorporation of the triad of redox activity, hemilability, and proton responsivity into a single ligand scaffold is reported. Due to this triad, the complexes Fe(<sup>Pyrr</sup>PDI)(CO)<sub>2</sub> (3) and Fe(<sup>Mor</sup>PDI)(CO)<sub>2</sub> (4) display 40-fold enhancements in the initial rate of NO<sub>2</sub><sup>-</sup> reduction, with respect to Fe(<sup>MeO</sup>PDI)(CO)<sub>2</sub> (7). Utilizing the proper sterics and p K<sub>a</sub> of the pendant base(s) to introduce hemilability into  ...[more]

Similar Datasets

Unknown A Nonheme Sulfur-Ligated {FeNO}<sup>6</sup> Complex and Comparison with Redox-Interconvertible {FeNO}<sup>7</sup> and {FeNO}<sup>8</sup> Analogues.
| S-EPMC6576265 | biostudies-literature
Unknown Sequential Deoxygenation of CO<sub>2</sub> and NO<sub>2</sub><sup>-</sup> via Redox-Control of a Pyridinediimine Ligand with a Hemilabile Phosphine.
| S-EPMC10520972 | biostudies-literature
Unknown N<sub>2</sub> O Reductase Activity of a [Cu<sub>4</sub> S] Cluster in the 4Cu<sup>I</sup> Redox State Modulated by Hydrogen Bond Donors and Proton Relays in the Secondary Coordination Sphere.
| S-EPMC6940516 | biostudies-literature
Unknown A Nonheme, High-Spin {FeNO}<sup>8</sup> Complex that Spontaneously Generates N<sub>2</sub>O.
| S-EPMC5997263 | biostudies-literature
Unknown A Nonheme Mononuclear {FeNO}<sup>7</sup> Complex that Produces N<sub>2</sub> O in the Absence of an Exogenous Reductant.
| S-EPMC8657876 | biostudies-literature
Unknown Mononuclear, Nonheme, High-Spin {FeNO}<sup>7/8</sup> Complexes Supported by a Sterically Encumbered N<sub>4</sub>S-Thioether Ligand.
| S-EPMC6715289 | biostudies-literature
Unknown Boron-lead multiple bonds in the PbB<sub>2</sub>O<sup>-</sup> and PbB<sub>3</sub>O<sub>2</sub><sup>-</sup> clusters.
| S-EPMC9814552 | biostudies-literature
Unknown Pourbaix Diagram, Proton-Coupled Electron Transfer, and Decay Kinetics of a Protein Tryptophan Radical: Comparing the Redox Properties of W<sub>32</sub><sup>•</sup> and Y<sub>32</sub><sup>•</sup> Generated Inside the Structurally Characterized α<sub>3</sub>W and α<sub>3</sub>Y Proteins.
| S-EPMC5762255 | biostudies-literature
Unknown Proton-Only Sensing of Hyperpolarized [1,2-<sup>13</sup>C<sub>2</sub>]Pyruvate.
| S-EPMC10284333 | biostudies-literature
Unknown A Mononuclear, Nonheme Fe<sup>II</sup>-Piloty's Acid (PhSO<sub>2</sub>NHOH) Adduct: An Intermediate in the Production of {FeNO}<sup>7/8</sup> Complexes from Piloty's Acid.
| S-EPMC6576269 | biostudies-literature