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Abstract
Primate green- and red-sensitive proteins are highly homologous, but display maximum absorption at 530 and 560 nm, respectively. Origin of the 30-nm difference is owing to the three amino acids (Ala, Phe, and Ala in green, and Ser, Tyr, and Thr in red, respectively). Here we examined the role of an O-H group of S180 in Monkey Red-sensitive pigment (MR) by comparing the light-induced difference FTIR spectra between the wild-type and S180A mutant. From very similar spectral features, it was concluded that the dipole moment of the O-H group leads to the spectral red-shift by 4 nm without altering local protein structure.
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