Raman spectroscopic studies on photoreactive retinal proteins are comp
rehensively described, including the basic physics of Raman scattering
and illustrative examples of the types of information on the structur
e and function of the retinal chromophore and its environment which ca
n be obtained from the vibrational Raman spectra. In addition, practic
al advice and recipes are given which should enable the reader to plan
and eventually perform a Raman experiment in a photolabile retinal pr
otein. A dominant role is played by the resonance Raman (RR) experimen
t with visible laser excitation which selelctively probes the retinal
chromophore. Much discussion is devoted to bacteriorhodopsin (bR) and
its photocycle as a paradigm for a light-induced reaction of a retinal
protein. Various time-resolved techniques are described to study the
temporal evolution of the bR chromophore by probing RR spectra of inte
rmediate states. Vibrational Raman spectra are interpreted in terms of
structure and structural changes of the chromophore. RR spectroscopic
studies on halorhodopsin, sensory rhodopsin, and visual pigments are
reported, as well as on modified proteins in which retinal analogues a
re incorporated, and on site-specific mutants. Results of ultraviolet
RR experiments which selectively probe the aromatic side chains in the
protein backbone are reported. In addition, a promising new technique
of near-infrared Raman excitation is discussed. Finally, application
of coherent anti-Stokes Raman spectroscopy (CARS) to retinal proteins
is reported.