The excited-state proton transfer (ESPT) via proton transfer wires in green fluorescent protein (GFP) plays an important role on the spectroscopic of GFP. In this work, we use the proton transfer wires and the chromophore complex to simulate the tautomer structures of neutral state and the intermediate state in wt-GFP. And we employ the time-dependent density functional theory combined with the sum-over-states method to calculate the one- and two-photon absorption properties of these complexes in GFP. We obtain the large stokes shift from 383 nm to 500 nm in GFP when simulating the ESPT process by these isomerous H-bonding complexes. We find that the TPA spectrum of the H-bonding complex of the intermediate state agrees more with experimental measurement than that of the H-bonding complex of the neutral state. The TPA spectrum of GFP might be mainly dominated by the structure which is similar to the H-bonding complex of intermediate state. Further, we simulate another kind of complex which possess short-strong hydrogen bonds in proton transfer wires, and find that TPA properties of these complexes are much stronger than that of the complexes with the long distance proton wires from GFP.