The thermosensitivity of delayed fluorescence, the relative values of variable chlorophyll fluorescence and the degree of quenching of 9-aminoacridine fluorescene were studied in the chloroplasts from heat-acclimated and non-acclimated (treated 6 h at 52,5°C) young bean plants. The temperature sensitivity of each parameter studied was defined by that temperature at which chloroplast activity decreased by 50% (T50) of its maximum value. There was appreciable increase in the thermostability of membrane energization in chloroplasts isolated from acclimated and non-acclimated plants compared with the controls. The photosynthetic parameters differed according to the suspending medium and the preacclimation treatment. When chloroplast were suspended in phosphate buffer with the addition of stabilizing compounds (2 M sucrose or 0.5% human serum albumin) the thermostability of the thylakoid membranes increased, as was evident by the increases in T50 of about 8-10° C (sucrose) and 2-5° C (human serum albumin) for all the parameters investigated. Photoinduced quenching of 9-aminoacridine fluorescence decreased to some extent in the presence of protective compounds, but in chloroplasts from acclimated plants the T50 was practically equal to that for their long-lived luminescence under the same conditions. At the thylakoid membrane level, acclimation was clearly manifested as an increased thermostability of photoinduced proton-gradient formation.
Unsaturated fatty acids at concentrations of 1-2 μmol mg(-1) chlorophyll decrease the intensity of long-lived delayed fluorescence and inhibit the Hill reaction in Pisum sativum L. chloroplasts in a pH-dependent and reversible manner. A charged form of the fatty acids is two times more effective than an undissociated form. Fatty acids, anionic and cationic detergents and urea inhibit activity and decrease the temperature of heat inactivation of the water-spilitting system. Sucrose at a concentration of 2.5 M protects chloroplasts against the effects of these compounds. It is concluded that their action can be explained by the denaturation of the water-splitting protein.
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