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J. Biol. Chem., Vol. 260, Issue 3, 1459-1464, 02, 1985
Y Shahak
The effect of thiol oxidants on the light-activated H+-ATPase has been
studied in freshly broken and intact chloroplasts. The following
observations were made: (i) in chloroplasts which are osmotically shocked
after light activation, ferricyanide stimulates the deactivation of the
enzyme in the dark, but has little effect in the light; (ii) similarly,
o-iodosobenzoate is a most efficient deactivator of the ATPase in intact
chloroplasts in the dark but not in the light; (iii) the activated ATPase
becomes sensitive to oxidants in the light upon the addition of an
uncoupler; (iv) the oxidant-induced deactivation in the dark dominates the
stabilizing effect of pyrophosphate or ADP plus Mg2+; (v) full deactivation
of the ATPase by dark adaptation or by oxidants does not affect the rate of
photophosphorylation under saturating conditions. A model is suggested in
which two kinds of conformational changes are involved in the regulation of
the ATPase: those induced by the trans-membrane-proton gradient and those
by oxidation-reduction of the enzyme. These changes result in the
preferential interaction with thiol reductants in the light but with thiol
oxidants in the dark.
Differential effect of thiol oxidants on the chloroplast H+-ATPase in the light and in the dark
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