It was found that chlorophyll fluorescence spectra and spectra of fluorescence excitation of pigment-protein complexes of photosystem II are affected by treatment with DNase. Pigment-protein complexes were isolated from pea thylakoid membranes. Spectra were measured at room temperature. It was shown that the treatment with DNase leads to a 30% increase in fluorescence yield at excitation in chlorophyll absorption bands in the fraction containing CP47, CP43, and CP29, and also in the fraction containing reaction center complexes with minor contaminations of light-harvesting complexes. Upon excitation at 260-300 nm and in the region of 500 nm, a diminishing of fluorescence yield takes place. These results suggest that pigments and/or pigment-protein complexes are bound to nucleic acids. This association, by influencing the pigment properties, can participate in the photoregulation of biochemical reactions through changes in the thermal dissipation of excited chlorophyll molecules.
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