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- W1970781760 abstract "Treatment of chloroplast thylakoids with pyridoxal 5′-phosphate (PLP)in the light or in the presence of Mg2+ causes inhibition of photophosphorylation which is partially competitive to ADP and to inorganic phosphate (Pi), suggesting that PLP may modify essential lysine residues in the catalytic nucleotide binding site of the thylakoid H+-ATPase. Treatment of thylakoids with PLP and NaB3H4 results in incorporation of about 4 mol [3H]PLP/mol CF1 almost equally distributed between α- and β-subunits. ADP plus Pi, prevents incorporation of one PLP per three α-subunits and one per three β-subunits, but causes almost full protection against PLP inactivation, suggesting that PLP modification of only one α- and one β-subunit is sufficient for inactivation of the enzyme. As PLP modification of the ATPase is largely excluded in the absence of Mg2+, modification of the active site may require ionic fixation of PLP with the help of the phosphate side-chain via Mg2+, similar to the interaction of Pβ and Pγ of ATP with the protein in order to facilitate the covalent attack to the vicinal lysine residue." @default.
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- W1970781760 date "1989-04-01" @default.
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- W1970781760 title "Characterization of nucleotide binding sites on membrane-bound chloroplast ATPase by modification with pyridoxal 5′-phosphate" @default.
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- W1970781760 doi "https://doi.org/10.1016/s0005-2728(89)80162-8" @default.
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