1982•PubMedRequires access
[Effect of redox and chelating agents on the properties of chloroplast ATPase].
Gol'dfel'd Mg, Dmitrovskiĭ Lg, Bliumenfel'd La
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Abstract
The effect of redox and chelating reagents on the ATPase and ATP-synthetase activity in chloroplast membranes as well as the ATPase activity of isolated CF1-coupling factor from chloroplasts has been studied. The Mg2+-ATPase in thylakoid membranes and isolated Ca2+-ATPase is stimulated by dithionite. In the presence of reduced glutathione the effect of dithionite is similar to those of prolonged illumination or heating. Dichlorophenolindophenol partially inhibits this activity as well as citrate, tenoyltrifluoroacetone and the excess fo ATP. Photophosphorylation in chloroplast lamellae is inhibited with dithionite. It is suggested that the membrane bound ATPase from chloroplasts may be in two structural states which differ in their enzymic activity and in the coupling to electron transfer in membrane. The transitions between these states can be induced by redox reagents.