The effect of spatial confinement in reverse micelles (RMs) on the spectral and fluorescent characteristics of eosin (E), erythrosin (ER), rose bengal (RB), bovine serum albumin (BSA), and their mixtures was studied. It was found that the size of the reverse micelles (their hydrodynamic radius R_h) affects the spectral and luminescent characteristics of both BSA and dye molecules (DM). The microenvironment of tyrosine residues in BSA does not undergo any significant changes with changing R_h, while a decrease in the micelle radius leads to an increase in the fluorescence intensity of tryptophan residues. For DMs, spatial confinement in aqueous pools of micelles affects the change in the dipole moment of the molecules upon their excitation. The dependences of the BSA fluorescence quenching coefficient (K_SV) on DM were experimentally obtained, and it was determined that for the studied dyes, this characteristic differs for micellar solutions compared to buffer solutions. The static quenching constants (K_S) for complexes in micelles in the studied region of their hydrodynamic radii are two orders of magnitude smaller than the Stern-Volmer constant (K_SV) for aqueous solutions. K_S values decrease in the E->ER->BR series, which is due to conformational changes in the molecular structure in this series associated with the redistribution of charges on the molecular atoms. Dynamic fluorescence quenching, which is the main one, is caused by the transfer of electronic excitation energy from BSA to DM. The efficiency of electronic excitation transfer increases with decreasing R_h. Keywords: reverse micelles, fluorescence, fluorescent dyes, serum albumin, halogenated fluorescein.