Adsorption of histidine on cerium oxide model surfaces was investigated by synchrotron radiation photoemission, resonant photoemission, and near edge X-ray absorption fine structure spectroscopies. Histidine was evaporated in a vacuum onto ordered stoichiometric CeO2(111) and partially reduced CeO1.9 thin films grown on Cu(111). Histidine binds to CeO2 in anionic form via the carboxylate group and all three nitrogen atoms, with the imidazole ring parallel to the surface. The amino nitrogen atom of the imidazole ring (IM) is deprotonated, and both IM nitrogen atoms form strong bonds via π orbitals, while the α-amino nitrogen interacts with the oxide via its hydrogen atoms. In the case of CeO1.9, the deprotonation of the amino nitrogen of the imidazole ring is less pronounced and N K-edge spectra do not show a clear orientation of the ring with respect to the surface. A minor reduction of the cerium surface on adsorption of histidine was observed and explained by charge exchange as a result of hybridization of the π orbitals of the IM ring with the f and d orbitals of ceria. Knowledge of histidine adsorption on the cerium oxide surface can be used for design of mediator-less biosensors where the histidine-containing proteins can be strongly bound to the oxide surface via the imidazole side chain of this residue.