[Characteristics of complex-formation of chlorine e6 with human and bovine serum albumins].

Pigment-protein complexes of chlorin e6 (Chl e6) with human (HSA) and bovine serum albumines (BSA) have been investigated by spectral-luminescent methods. Fluorescence quenching of tryptophan residues caused by the inductive-resonance energy transfer to pigment molecules and the rise of the polarization degree of Chl e6 emission were observed upon incorporation of Chl e6 in the protein globula. The obtained data on spectral-energetic parameters of protein tryptophanyls and Chl e6 permitted us to calculate the energy transfer critical distances R0 in complexes of Chl e6 with HSA (R0 = 32 A) and BSA (R0 = 35A).

[Characteristics of mixed association and deactivation of electron excitation in chlorophyll-pheophytin complexes].

The regularities of the individual and mixed association of chlorophylls (Chl a, PChl a) with pheophytin (Pheo) were investigated. The complex studies of optical activity, spectral--luminescent and energetic characteristics of aggregates were carried out in mixture of solvents aceton-water (1:49). The formation of pigment mixed associates leads to intracomplex energy transfer from Chl (or PChl) to Pheo.

[Influence of acids and metal salts on associates of pheophytin and its derivatives in binary mixtures of solvents].

The experimental investigation of the influence of HCl and Zn, Cd and Cu acetates on association of pheophytin alpha and rodin g7 was carried out in water-ethanolic (4 : 1) media. It is shown that during acidation of a binary solvent mixtures containing pheophytin alpha associate, the formation of product with the absorption maximum 702nm takes place, which is the pigment associated form. The formation of the same product is found under the action of metal acetates on pigment associated complexes.

[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.

[Regularities of aggregation and excitation electronic energy transfer in associates of pheophytin and its mesoderivatives].

The spectral-luminescent characteristics of mesoderivatives of pheophytin and its analogs were investigated in binar mixtures of solvents (ethanol--water; dioxane--water). The mesoderivatives were shown not to form stable longwave selfassociates. Under similar conditions the pheophytin mesoderivatives were inclined to the formation of stable mixed associates with pigments, containing vinyl groups and free keto groups in position 9.