[Spectroscopic and photochemical properties of pigments bound to proteins]

Using gel-filtration and spectral-luminescent analysis properties of artificial chlorophyll-protein and chlorine-protein complexes on the basis of human serum albumin (HSA) were analysed. It has been shown that formation of joint complexes pigments - HSA does not induce essential changes in the spectral and energetic parameters of the pigment part of the complex. A change in the rate of photosensitized reduction of methylviologen (sensitizer-pigment) was found during the variation of the relative content of the pigment mixed with HSA. An increase of the photoreaction rate during maximal filling of the protein globule with pigment molecules is explained by different pattern of incorporation of these molecules into protein matrix.