[NaCl-induced photoinhibition and the recovery of the photosynthetic activity of katG- mutant of the cyanobacterium Synechocystis sp. PCC 6803].

The joint effects of 0.5 M NaCI and light of different intensities on the activity of the photosynthetic apparatus and ATP contents in cells of the katG- mutant of cyanobacterium Synechocystis sp. PCC 6803 have been studied.

[Covalent binding of 1,N(6)-ethenoadenosine diphosphate to catalytic and noncatalytic sites of chloroplast ATP-synthase].

The catalytic and noncatalytic sites of the chloroplast coupling factor (CF1) were selectively modified by incubation with the dialdehyde derivative of the fluorescent adenosine diphosphate analogue 1,N(6)-ethenoadenosine diphosphate. The modified CF1 was reconstituted with EDTA-treated chloroplast thylakoid membranes. The influence of light-induced transmembrane proton gradient and of phosphate ions on the fluorescence of 1,N(6)-ethenoadenosine diphosphate covalently bound to catalytic sites of reconstituted CF1 (ATP-synthase) was studied.

[Low-frequency oscillations of the energy-conserving reactions of photosynthesis and level of indoles in wheat ontogenesis].

Changes in the rates of photophosphorylation and the content of indoles in wheat ontogeny were studied. On the basis of experimental data, a phenomenological parametrical model was elaborated. It was found that the temporal changes in the parameters examined are nonmonotonous and include an oscillatory component.

[The special reaction of photophosphorylation using epsilon ADP--a fluorescent analog of ADP].

Photophosphorylation of epsilon ADP in a chloroplast synthetase system reconstituted with CF1 or with CF1 modified by covalently bound epsilon ADP has been studied. The reconstitution of EDTA-treated chloroplasts with CF1 restores the photophosphorylating activity to about 90%. When the CF1 modified by covalently bound epsilon ADP is used for reconstitution the photophosphorylating activity of EDTA-treated chloroplasts is restored to 37%.

[Properties of epsilon-ATP hydrolysis by CF1-ATPase from pea chloroplasts].

The ATPase activity of CF1 isolated from pea chloroplasts with epsilon-ATP, the fluorescent analog of ATP and ATP used as substrates, in the presence of Mg2+, Ca2+ and sodium sulfite (stimulator of the ATPase activity) was studied. The rate of epsilon-ATP hydrolysis in the presence of Mg2+ is nearly two times as low as that of ATP; an addition of sodium sulfite to the reaction mixture increases the reaction rate without changing the above ratio. The rate of Ca2+-dependent hydrolysis of epsilon-ATP is rather low as compared to that in the presence of Mg2+.