Radu Silaghi-Dumitrescu cover image

Affiliation

Department of Chemistry, Babes-Bolyai University, 11 Arany Janos Street, 400028 Cluj-Napoca, Romania - Research


Do you even own a proton? Awkward spectroscopic quirks with reactivity implications for hemoprotein ferryls


Abstract

The structure and reactivity of biological ferryl centers generally entails three coordinates: (1) the highly-covalent and electronically-robust S=1 double-bonded Fe(IV)-oxo unit, (2) its occasional magnetic coupling and ensuing illuminating particularities such as the two-state reactivity (TSR), and (3) its protonation in hemoproteins where the axial ligand is an anionic cysteine thiolate or tyrosine phenolate. Occasional x-ray diffraction and spectroscopy reports explore situations where exceptions or additions to these coordinates can be argued. Among these are some unusually long iron-oxygen distances in some ferryl crystal structures of histidine-ligated heme proteins, and some accompanying spectroscopy data that raises the intriguing question of whether two ferryl systems with differing Fe-O distances can have (near?)-identical properties when probed spectroscopically. We discuss here such experimental data and explore the topic using, DFT, TD-DFT, QM/MM and ab initio dynamics in conjunction with new experimental data where in some cases exceptions to the three rules/coordinates can be argued, including excited-state chemistry. Case studies in heme peroxidases, globins, and chlorite dismutase are presented (1–5)


References

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