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  • Title: [Damage to the chloroplast H+-ATPase complex by low concentrations of glutaraldehyde].
    Author: Krendeleva TE, Kukarskikh GP, Nizovskaia NV, Tulbu GV.
    Journal: Biokhimiia; 1982 Jun; 47(6):904-10. PubMed ID: 6214284.
    Abstract:
    The energy-dependent processes coupled to electron transport were studied in isolated pea chloroplasts treated with low concentrations (1-5 mM) of glutaraldehyde (GA) in the dark and in the light sufficient to cause energization of the membrane. After GA treatment the chloroplasts exhibited a strong suppression of cyclic and non-cyclic phosphorylation, coupled (+ADP+Pi) electron transport and diminution of the light-activated Mg2+-ATPase activity. The rate of basal electron transport was unaffected. The GA-treated chloroplasts were found to retain the capacity to form the osmotic component of the transmembrane potential. These data and the results of the effect of florizine and ATP on electron transport suggest that the effect of GA on energy transduction processes associated with photophosphorylation may consist in its action on reversible H+-ATPase. In light-adapted samples treated with GA the data characterizing the formation of a high energy state (rate of photophosphorylation, steady-state level of photo-induced quenching of atebrin fluorescence and its dark recovery; photo-induced absorbance changes at 520 nm; rate of the slow phase of delayed fluorescence increment) appear to be changed to a greater extent as compared to the dark-adapted samples. The observed changes may arise from a greater conductivity of thylakoid membranes due to fixation of the H+-ATPase proton channel in the "open" state.
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