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Light-Dependent Incorporation of Adenine Nucleotide into Noncatalytic Sites of Chloroplast ATP Synthase

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Abstract

The binding of ADP and ATP to noncatalytic sites of dithiothreitol-modified chloroplast ATP synthase was studied. Selective binding of nucleotides to noncatalytic sites was provided by preliminary light incubation of thylakoid membranes with [14C]ADP followed by its dissociation from catalytic sites during dark ATP hydrolysis stimulated by bisulfite ions (“cold chase”). Incorporation of labeled nucleotides increased with increasing light intensity. Concentration-dependent equilibrium between free and bound nucleotides was achieved within 2–10 min with the following characteristic parameters: the maximal value of nucleotide incorporation was 1.5 nmol/mg of chlorophyll, and the dissociation constant was 1.5 µM. The dependence of nucleotide incorporation on Mg2+ concentration was slight and changed insignificantly upon substituting Ca2+ for Mg2+. Dissociation of nucleotide from noncatalytic sites was illumination dependent. The dissociation kinetics suggested the existence of at least two nucleotide-binding sites with different dissociation rate constants.

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Abbreviations

PMS:

phenazine methosulfate

DTT:

dithiothreitol

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Authors and Affiliations

  1. Institute of Basic Biological Problems, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    A. N. Malyan

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__________

Translated from Biokhimiya, Vol. 70, No. 11, 2005, pp. 1514–1520.

Original Russian Text Copyright © 2005 by Malyan.

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Malyan, A.N. Light-Dependent Incorporation of Adenine Nucleotide into Noncatalytic Sites of Chloroplast ATP Synthase. Biochemistry (Moscow) 70, 1245–1250 (2005). https://doi.org/10.1007/s10541-005-0254-5

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  • DOI: https://doi.org/10.1007/s10541-005-0254-5

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