ABSTRACT
Two iron porphyrin complexes with either mesityl (FeTMP) or thiophene (FeT3ThP) peripheral substituents were attached to basal pyrolytic graphite and Ag electrodes via different immobilization methods. By combining cyclic voltammetry and in-operando surface-enhanced Raman spectroscopy along with MD simulations and DFT calculations, their respective surface attachment, redox chemistry and activity toward electrocatalytic oxygen reduction was investigated. For both porphyrin complexes, it could be shown that catalytic activity is restricted to the first (few) molecular layer(s), although electrodes covered with thiophene-substituted complexes showed a better capability to consume the oxygen at a given overpotential even in thicker films. The spectroscopic data and simulations suggest that both porphyrin complexes attach to a Ag electrode surface in a way that maximum planarity and minimum distance between the catalytic iron site and the electrode is achieved. However, due to the distinctive design of the FeT3ThP complex, the thiophene rings are capable of occupying a conformation, via rotation around the bonding axis to the porphyrin, in which all four sulfur atoms can coordinate to the Ag surface. This effect creates a dense and planar surface coverage of the porphyrin on the electrode facilitating a fast (multi) electron transfer via several covalent Ag-S bonds. In contrast, bulky mesityl groups as peripheral substituents, which have been initially introduced to prevent aggregation and improve catalytic behavior in solution, exert a negative effect on the overall electrocatalytic performance in the immobilized state as a less dense coverage and less stable interactions with the surface are formed. Our results underline the importance of rationally designed heterogenized molecular catalysts to achieve optimal turnover, which not only strictly applies to the here discussed oxygen reduction reaction but eventually holds also true for other energy conversion reactions such as carbon dioxide reduction.
ABSTRACT
Proteins carrying an iron-porphyrin (heme) cofactor are essential for biological O2 management. The nature of Fe-O2 bonding in hemoproteins is debated for decades. We used energy-sampling and rapid-scan X-ray Kß emission and K-edge absorption spectroscopy as well as quantum chemistry to determine molecular and electronic structures of unligated (deoxy), CO-inhibited (carboxy), and O2-bound (oxy) hemes in myoglobin (MB) and hemoglobin (HB) solutions and in porphyrin compounds at 20-260 K. Similar metrical and spectral features revealed analogous heme sites in MB and HB and the absence of low-spin (LS) to high-spin (HS) conversion. Amplitudes of Kß main-line emission spectra were directly related to the formal unpaired Fe(d) spin count, indicating HS Fe(II) in deoxy and LS Fe(II) in carboxy. For oxy, two unpaired Fe(d) spins and, thus by definition, an intermediate-spin iron center, were revealed by our static and kinetic X-ray data, as supported by (time-dependent) density functional theory and complete-active-space self-consistent-field calculations. The emerging Fe-O2 bonding situation includes in essence a ferrous iron center, minor superoxide character of the noninnocent ligand, significant double-bond properties of the interaction, and three-center electron delocalization as in ozone. It resolves the apparently contradictory classical models of Pauling, Weiss, and McClure/Goddard into a unifying view of O2 bonding, tuned toward reversible oxygen transport.
