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אסיף מאגר המחקר החקלאי
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Differential effect of thiol oxidants on the chloroplast H+-ATPase in the light and in the dark.
Year:
1985
Source of publication :
Journal of Biological Chemistry
Authors :
Shahak, Yosepha
;
.
Volume :
260
Co-Authors:
Shahak, Y.
Facilitators :
From page:
1459
To page:
1464
(
Total pages:
6
)
Abstract:
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.
Note:
Related Files :
ferricyanide
light
metabolism
pH
plant
Plants
Proton-Translocating ATPases
Proton Translocating ATPases
Show More
Related Content
More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29227
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:45
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Scientific Publication
Differential effect of thiol oxidants on the chloroplast H+-ATPase in the light and in the dark.
260
Shahak, Y.
Differential effect of thiol oxidants on the chloroplast H+-ATPase in the light and in the dark.
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.
Scientific Publication
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