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Effects of energization and substrates on the reactivities of lysine residues of the chloroplast ATP synthase beta subunit



Effects of energization and substrates on the reactivities of lysine residues of the chloroplast ATP synthase beta subunit



European Journal of Biochemistry 228(2): 265-270



The incubation of chloroplast thylakoids with pyridoxal 5'-phosphate for a short time (5 s) modified the lysine residues of the ATP synthase beta subunit. Except for lysine residues in the N-terminal and C-terminal regions, the glycine-rich P-loop (GGAGVGKT)-, Lys154-, and Lys167-containing peptide (P-peptide) exhibited high reactivity with pyridoxal 5'-phosphate. The energization of thylakoids or addition of substrates (ADP, P-i, ATP) affected the modifications of the P-peptide, Lys447, and Lys399. For the P-peptide, substrates inhibited the modification with 0.5 mM ADP inhibiting by 80%. Energization enhanced the inhibitory effects of substrates. For Lys447, substrates also inhibited the modification; 0.5 mM ADP inhibited by 60%. For Lys399, the reactivity depended on the transmembrane DELTA-mu-H +. With increasing DELTA-mu-H + the reactivity decreased. These results suggest the existence of energy-dependent conformational changes at the catalytic nucleotide-binding site and around Lys399. The former increases the affinity of the site for substrates. Substrate binding at the catalytic site changes the conformation around Lys447.

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Accession: 008566048

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PMID: 7705338


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