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- W2023265655 abstract "FEBS LettersVolume 303, Issue 2-3 p. 233-236 Full‐length articleFree Access ATPase state and activity in thylakoids from normal and water‐stressed lupin First published: June 01, 1992 https://doi.org/10.1016/0014-5793(92)80527-NCitations: 2AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract To compare with the case of phosphorylation, ATP hydrolysis was investigated in thylakoids from plants submitted to drought. For medium stresses the relationship between hydrolysis rate and deactivation constant of the de‐energized enzyme when Δph varies is unchanged, hence the basic mechanisms are preserved; (PSI‐driven) energization then is neither affected, at any light intensity. As drought intensifies, hydrolysis and monogalactolipids fall somewhat in parallel. whereas the deactivation constant changes with digalactolipids and phosphatidic acid content. This alteration of the F0 lipid environment must be transduced to F1, the subunits of which, however, are preserved, as shown by LDS‐PAGE, ATP synthesis (thiol‐oxidized enzyme) and hydrolysis (thiol‐reduced enzyme) show an identical decrease with stress. Thus the latter impairs a common early step, probably the activation of the oxidized enzyme. Citing Literature Volume303, Issue2-3June 01, 1992Pages 233-236 ReferencesRelatedInformation" @default.
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- W2023265655 title "ATPase state and activity in thylakoids from normal and water‐stressed lupin" @default.
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