Ah&act-Fourier-transformed Raman spectra of bacteriorhodopsin, the photosynthetic reaction center, and myoglobin in aqueous solution excited at 1064 nm are presented. These proteins are representative of three important classes of chromophoric proteins. The observed vibrational modes are assigned and discussed based on the known resonance Raman spectra of these proteins. In each case, chromophore vibrations dominate the Raman scattering, with little or no contribution from other protein vibrations. However, the limitations encountered in resonance Raman studies of chromophoric proteins due to sample fluorescence or sample photolability are circumvented. The relative intensities in the bacteriorhodopsin Raman spectrum excited at 1064 nm are nearly identical to the relative intensities previously observed by resonance excitation. The Raman spectrum of the reaction center of the photosynthetic bacterium Rhodobacter sphaeroides excited at 1064 mn contains contributions from both bacteriochlorophyll and bacteriopheophytin pigments, with possible preresonance enhancement of bacteriochlorophyll modes. The lWnm-excited Raman spectrum of myoglobin displays several marker bands that have been characterized previously in resonance Raman investigations with excitation in both the Soret and Q-band regions.