The structure and reactivity of ferryl centers in heme as well as in non-heme systems is generally discussed within three well-understood coordinates: (1) the highly-covalent and electronically-robust S=1 double-bonded Fe(IV)-oxo unit, (2) its occasional magnetic coupling (e.g., with a porphyrin cation radical in Compound I, or to another iron atom in binuclear non-heme enzymes) and ensuing illuminating particularities such as the two-state reactivity (TSR), and (3) its protonation in heme complexes 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 – where in some cases exceptions to the three rules/coordinates can be argued, and in some cases new ferryl-related chemistry is uncovered (1-7).