Nucleotide binding to noncatalytic sites is essential for ATP-dependent stimulation and ADP-dependent inactivation of the chloroplast ATP synthase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2010-09

AUTHORS

Alexander N. Malyan

ABSTRACT

Light-dependent binding of labeled ADP and ATP to noncatalytic sites of chloroplast ATP synthase and the effect of light-exposed thylakoid membrane preincubation with ADP or ATP on ATPase activity were studied. ADP binding during the preincubation was shown to inactivate the chloroplast ATPase, whereas ATP binding caused its activation. The rate and equilibrium constants of ATPase inactivation and activation were close to those of ADP and ATP binding to a noncatalytic site, with K (d) values of 38 and 33 μM, respectively. It is suggested that ADP- or ATP-binding to one of the noncatalytic sites affects the ATPase activity of chloroplast ATP synthase through a mechanism that modulates tightness of ADP binding to a catalytic site. More... »

PAGES

243-248

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11120-010-9586-0

DOI

http://dx.doi.org/10.1007/s11120-010-9586-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027768342

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20706787


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