G protein-coupled receptors (GPCRs) are heptahelical transmembrane proteins. They transduce a large variety of extracellular signals, allowing perception of taste, odor, hormones, and light. Binding of an extracellular ligand induces structural changes in the cytosolic domain of a GPCR which, thereby, catalyzes nucleotide exchange in a G protein. Rhodopsins, the visual pigments, are prototypical GPCRs that are activated by photoisomerization of covalently bound 11-cis retinal. Unlike other GPCRs, bovine rhodopsin and transducin, its cognate G protein, can be prepared from cow eyes in large quantities for spectroscopic and biochemical investigations. Rhodopsin is the best studied GPCR and the only one for which an X-ray structure has been solved. Structural information together with the wealth of biophysical data on native and recombinant rhodopsins allows to determine structure function relationships that are relevant to GPCR-dependent signaling in general. Here, results from Fourier-transforminfrared (FTIR) spectrocopic studies of rhodopsin and measurements of nucleotide-dependent transducin fluorescence a re reviewed. Intra- and intermolecular processes during signaling by the photoreceptor have thus been identified and analyzed kinetically. Recent applications of these techniques concern rhodopsin transducin coupling in synthetic lipidic matrices and analysis of drug action at the receptor G protein interface.The data are discussed in the context of the crystal structure of rhodopsin and additional biochemical information if required for the understanding of the spectroscopic results.