Evaluation of the proton-coupled electron transfer thermodynamics of immobilized hemin is challenging due to the disparity of its electrochemical titration curves reported in the literature. Deviations from the one-electron, one-proton transfer at circumneutral pHs have been commonly ascribed to either the formation of dimeric species or the ionization of a second iron-bound water molecule. Herein, however, we report on non-idealities in the more acidic region, whose onset and extent vary with the nature and concentration of the commonly used phosphate and acetate buffers. It is shown that these deviations originate in the ligand-exchange binding between the oxidized aquo-hemin complex and the anionic components of the buffer, so that they are restricted to the pH interval where these forms coexist. A stepwise approach was developed to quantify unambiguously the apparent and intrinsic binding equilibrium constants. The apparent binding equilibrium constant exhibits a peakshaped pH dependence, whose maximum is located at approximately the midpoint between the pK(a) of the iron-bound water and the first pK(a) of the buffer, and its magnitude is greater for the phosphate than for the acetate buffer. But strikingly, the opposite trend was found for the magnitude of the intrinsic binding equilibrium constants determined from the apparent ones, due to the different relative locations of the phosphoric and acetic pK(a) values with respect to that of the oxidized aquo-hemin. To probe the role of the heme propionic residues, a similar study was carried out with a propionic-free iron porphyrin containing eight ethyl residues. These substituents decrease the acidity of the iron-bound water, strengthen the iron(III)-acetate binding, weaken the iron(III)-dihydrogen phosphate binding, and enable the binding between iron(III) and monohydrogen phosphate, which was hampered in hemin by the presence of the negatively charged propionate residues. Overall, this work provides a more complete speciation of immobilized iron porphyrins under acidic conditions than previously considered, showing the substitutional lability of the aqua ligand in the oxidized state of the iron center and the reluctance of its hydroxyl counterpart to anion exchange. Knowledge of these redox- and pH-dependent bindings with the buffer components is crucial for a rigorous quantification of the proton-coupled electron transfer and the electrocatalytic activity of iron porphyrins.