We theoretically investigated the ligand-to-metal charge-transfer (LMCT) excitation of the native iron(III)-dependent catechol dioxygenase and its functional model complexes with multistate complete active space second-order perturbation theory (MS-CASPT2) because the LMCT (catecholate-to-iron(III) charge-transfer) excitation energy is believed to relate to the reactivity of the native enzyme and its functional model complexes. The ground state calculated by the MS-CASPT2 method mainly consists of the iron(III)-catecholate electron configuration and moderately of the iron(II)-semiquinonate electron configuration for both of the enzyme active centers and the model complexes when the active center exists in the protein environment and the complexes exist in the solution. However, the ground state wave function mainly consists of the iron(II)-semiquinonate electron configuration for both the enzyme active site without a protein environment and the model complex in vacuo. These results clearly show that the protein environment and solvent play important roles to determine the electronic structure., of the catecholatoiron(III) complex. The LMCT excitation energy dearly relates to the weight of the iron. (III)-catecholate configuration in the ground state. The reactivity and the LMCT excitation energy directly relate to the ionization potential of the catecholate (IPCAT) in the model complex. This is because the charge transfer from the catecholate moiety to the dioxygen molecule plays a key role to activate the dioxygen molecule. However, the reactivity of the native catechol dioxygenase is much larger than those of the model complexes, despite the similar IPCAT values, suggesting that other factors such as the coordinatively unsaturated iron(III) center of the native enzyme play a crucial role in the reactivity.