Retinal is the light-absorbing biochromophore responsible for the activation of vision pigments and light-driven ion-pumps. Nature has evolved molecular tuning mechanisms that significantly shift the optical properties of the retinal pigments to enable their ab-sorption of visible light. Using large-scale quantum chemical calculations at the density functional theory level combined with the frozen density embedding theory approach, we show here how the protein environment of vision pigments tune the absorption of retinal to the 2.3-2.6 eV (480-530 nm) region by electrostatically dominated interactions between the chromophore and the sur-rounding protein residues. The calculations accurately reproduce the experimental absorption maxima of rhodopsin (2.49 eV/498 nm), and the red, green, and blue color pigments (2.3-2.9 eV/430-530 nm). We further identify key interactions responsible for the red- and blue-shifting effects by mutating the rhodopsin structure in silico, and find that deprotonation of the retinyl is likely to be responsible for the blue shifted absorption in the blue cone vision pigment.