In this paper we use ab initio multireference Moller-Plesset second-order perturbation theory computations to map the first five singlet states (S-0, S-1, S-2, S-3, and S-4) along the initial part of the photoisomerization coordinate for the isolated rhodopsin chromophore model 4-cis-gamma-methylnona-2,4,6,8-tetraeniminium cation. We show that this information not only provides an explanation for the spectral features associated to the chromophore in solution but also, subject to a tentative hypothesis on the effect of the protein cavity, may be employed to explain/assign the ultrafast near-IR excited-state absorption, stimulated emission, and transient excited-state absorption bands observed in rhodopsin proteins (e.g. rhodopsin and bacteriorhodopsin). We also show that the results of vibrational frequency computations reveal a general structure for the first (S-1) excited-state energy surface of PSBs that is consistent with the existence of the coherent oscillatory motions observed both in solution and in bacteriorhodopsin.